|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
46-519 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 850.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 46 EQPTGLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGVWSKVDPLVRSQCLSKLADYIEK 125
Cdd:cd07091 1 EQPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 126 DLDTIASIESLDNGKAIS-SAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAW 204
Cdd:cd07091 81 DRDELAALESLDNGKPLEeSAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 205 KIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNA 284
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 285 G-VNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDA 363
Cdd:cd07091 241 AkSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 364 ETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELI 443
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50310159 444 EKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
43-521 |
0e+00 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 693.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 43 ISYEQPTGLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGVWSKVDPLVRSQCLSKLADY 122
Cdd:cd07143 1 GKYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVSGSKRGRCLSKLADL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 123 IEKDLDTIASIESLDNGKAISSAKG-DVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLM 201
Cdd:cd07143 81 MERNLDYLASIEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 202 WAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIY 281
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 282 QNAG-VNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDP 360
Cdd:cd07143 241 EAAAkSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 361 FDAETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTID 440
Cdd:cd07143 321 FAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 441 ELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRVK 520
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
.
gi 50310159 521 L 521
Cdd:cd07143 481 L 481
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
57-517 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 676.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 57 FVPSkQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESL 136
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA--WRKTPAAERAAILRKAADLLEERKDELAELETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 137 DNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTV 216
Cdd:pfam00171 78 ENGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 217 VLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELG 296
Cdd:pfam00171 158 VLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 297 GKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQL 376
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 377 DKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAG 456
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50310159 457 IHTSNINTAIQVSNRLNAGTVWINTYNDFHHC-VPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
46-521 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 671.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 46 EQPTGLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEK 125
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPA--WAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 126 DLDTIASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTGST-HFSYTVREPLGVCGQIIPWNFPLLMWAW 204
Cdd:COG1012 81 RREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPgTRAYVRREPLGVVGAITPWNFPLALAAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 205 KIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNA 284
Cdd:COG1012 161 KLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 285 GVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAE 364
Cdd:COG1012 241 AENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 365 TFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERI-GDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELI 443
Cdd:COG1012 321 TDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 444 EKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYN---DFHHcvPFGGFNASGIGREMGSEALDNYTQVKAVRVK 520
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTtgaVPQA--PFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
.
gi 50310159 521 L 521
Cdd:COG1012 479 L 479
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
49-520 |
0e+00 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 662.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 49 TGLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSG-VWSKVDPLVRSQCLSKLADYIEKDL 127
Cdd:cd07141 7 TKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGsPWRTMDASERGRLLNKLADLIERDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 128 DTIASIESLDNGKAIS-SAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKI 206
Cdd:cd07141 87 AYLASLETLDNGKPFSkSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 207 APALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAG- 285
Cdd:cd07141 167 APALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGk 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 286 VNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAET 365
Cdd:cd07141 247 SNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 366 FQGAQTSQNQLDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEK 445
Cdd:cd07141 327 EQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIER 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50310159 446 ANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRVK 520
Cdd:cd07141 407 ANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
42-521 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 658.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 42 GISYEQPTGLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgVWSKVDPLVRSQCLSKLAD 121
Cdd:cd07144 1 GKSYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 122 YIEKDLDTIASIESLDNGKAISS-AKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLL 200
Cdd:cd07144 80 LVEKNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 201 MWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHI 280
Cdd:cd07144 160 MAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 281 YQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKS-ASEALKVGD 359
Cdd:cd07144 240 MKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEhVKQNYKVGS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 360 PFDAETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGE---RIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKF 436
Cdd:cd07144 320 PFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEkapEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 437 KTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKA 516
Cdd:cd07144 400 KTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKA 479
|
....*
gi 50310159 517 VRVKL 521
Cdd:cd07144 480 VHINL 484
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
47-517 |
0e+00 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 611.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 47 QPTGLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGVWSKVDPLVRSQCLSKLADYIEKD 126
Cdd:cd07142 2 KHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 127 LDTIASIESLDNGKAISSAK-GDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWK 205
Cdd:cd07142 82 ADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 206 IAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAG 285
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 286 -VNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAE 364
Cdd:cd07142 242 kSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 365 TFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIE 444
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50310159 445 KANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
68-517 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 609.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 68 VLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGVWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKG 147
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 148 DVQLVVNYLRSAAGYADKVDGRVI--DTGStHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTP 225
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIpvDKGD-YLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 226 LSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFA 305
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 306 DANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEI 385
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 386 GKNEGATLITGGERIG----DKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSN 461
Cdd:cd07114 320 AREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 50310159 462 INTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
89-519 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 594.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 89 DAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDG 168
Cdd:cd07078 1 DAAVAAARAAFKA--WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 169 RVIDTGST-HFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNI 247
Cdd:cd07078 79 EVIPSPDPgELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 248 VSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEV 327
Cdd:cd07078 159 VTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 328 CCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERI-GDKGYF 406
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeGGKGYF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 407 VRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDF- 485
Cdd:cd07078 319 VPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGa 398
|
410 420 430
....*....|....*....|....*....|....
gi 50310159 486 HHCVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07078 399 EPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
52-522 |
0e+00 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 594.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 52 FINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGVWSKVDPLVRSQCLSKLADYIEKDLDTIA 131
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 132 SIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALA 211
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 212 TGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKV 291
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 292 TLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQT 371
Cdd:cd07119 241 ALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 372 SQNQLDKILKYVEIGKNEGATLITGGERIGD----KGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKAN 447
Cdd:cd07119 321 SAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLAN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50310159 448 DSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRVKLE 522
Cdd:cd07119 401 DTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLS 475
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
50-515 |
0e+00 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 584.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 50 GLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDT 129
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 130 IASIESLDNGKAISSAKG-DVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAP 208
Cdd:cd07559 80 LAVAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 209 ALATGNTVVLKTAESTPLSALYVSQYIPKAgIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNL 288
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 289 KKVTLELGGKSPNVVFADA-----NLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDA 363
Cdd:cd07559 239 IPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 364 ETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERI----GDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTI 439
Cdd:cd07559 319 ETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50310159 440 DELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVK 515
Cdd:cd07559 399 EEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
68-521 |
0e+00 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 584.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 68 VLSPSTEEEITHVYEGREEDVDAAVEAADKAFKsgVWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKG 147
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE--AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 148 -DVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPL 226
Cdd:cd07115 79 lDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 227 SALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFAD 306
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 307 ANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIG 386
Cdd:cd07115 239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 387 KNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAI 466
Cdd:cd07115 319 REEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 50310159 467 QVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRVKL 521
Cdd:cd07115 399 RVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
40-517 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 579.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 40 PNGISYEQptgLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGVWSKVDPLVRSQCLSKL 119
Cdd:PLN02466 52 PVQVSYTQ---LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 120 ADYIEKDLDTIASIESLDNGKAIS-SAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFP 198
Cdd:PLN02466 129 ADLLEKHNDELAALETWDNGKPYEqSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 199 LLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGR 278
Cdd:PLN02466 209 LLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 279 HIYQNAG-VNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKeiKSASEALK- 356
Cdd:PLN02466 289 IVLELAAkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVE--KAKARALKr 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 357 -VGDPFDAETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTK 435
Cdd:PLN02466 367 vVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILK 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 436 FKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVK 515
Cdd:PLN02466 447 FKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
..
gi 50310159 516 AV 517
Cdd:PLN02466 527 AV 528
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
63-517 |
0e+00 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 574.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 63 GKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGVWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAI 142
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 143 S-SAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTA 221
Cdd:cd07112 81 SdALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 222 ESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAG-VNLKKVTLELGGKSP 300
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 301 NVVFADA-NLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKI 379
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 380 LKYVEIGKNEGATLITGGER--IGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGI 457
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 458 HTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
49-517 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 574.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 49 TGLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGVWSKVDPLVRSQCLSKLADYIEKDLD 128
Cdd:PLN02766 21 TKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 129 TIASIESLDNGKAISSAKG-DVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIA 207
Cdd:PLN02766 101 ELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 208 PALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGV- 286
Cdd:PLN02766 181 PALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATs 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 287 NLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETF 366
Cdd:PLN02766 261 NLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 367 QGAQTSQNQLDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKA 446
Cdd:PLN02766 341 QGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKA 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50310159 447 NDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:PLN02766 421 NNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
68-519 |
0e+00 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 561.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 68 VLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAK- 146
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG--WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 147 GDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPL 226
Cdd:cd07093 79 RDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 227 SALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFAD 306
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 307 ANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIG 386
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 387 KNEGATLITGGERIG----DKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNI 462
Cdd:cd07093 319 RAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 50310159 463 NTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
50-521 |
0e+00 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 529.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 50 GLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDT 129
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 130 IASIESLDNGKAISSAKG-DVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAP 208
Cdd:cd07117 80 LAMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 209 ALATGNTVVLKTAESTPLSALYVSQYIPKAgIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNL 288
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 289 KKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQG 368
Cdd:cd07117 239 IPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 369 AQTSQNQLDKILKYVEIGKNEGATLITGGERIG----DKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIE 444
Cdd:cd07117 319 AQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTenglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50310159 445 KANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRVKL 521
Cdd:cd07117 399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
69-519 |
0e+00 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 523.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 69 LSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGVWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGD 148
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 149 VQLVVNYLRSAAGYADKVDGRVIDT-GSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLS 227
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNlGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 228 ALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADA 307
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 308 NLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGK 387
Cdd:cd07118 242 DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 388 NEGATLITGGERIGD-KGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAI 466
Cdd:cd07118 322 AEGATLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 50310159 467 QVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07118 402 TVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
51-521 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 518.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 51 LFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKsgVWSKVDPLVRSQCLSKLADYIEKDLDTI 130
Cdd:PRK13252 9 LYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK--IWAAMTAMERSRILRRAVDILRERNDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 131 ASIESLDNGKAISSAkgdvqLVVNYLRSA------AGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAW 204
Cdd:PRK13252 87 AALETLDTGKPIQET-----SVVDIVTGAdvleyyAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 205 KIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKiVGEAITTHPKIKKVAFTGSTATGRHIYQNA 284
Cdd:PRK13252 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 285 GVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAE 364
Cdd:PRK13252 241 AASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 365 TFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERI----GDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTID 440
Cdd:PRK13252 321 TNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLteggFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDED 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 441 ELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRVK 520
Cdd:PRK13252 401 EVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVE 480
|
.
gi 50310159 521 L 521
Cdd:PRK13252 481 M 481
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
52-515 |
1.78e-179 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 512.82 E-value: 1.78e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 52 FINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFksGVWSKVDPLVRSQCLSKLADYIEKDLDTIA 131
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 132 SIESLDNGKAIS-SAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPAL 210
Cdd:TIGR01804 79 KLETLDTGKTLQeTIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 211 ATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKK 290
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 291 VTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQ 370
Cdd:TIGR01804 239 VTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 371 TSQNQLDKILKYVEIGKNEGATLITGGERIG----DKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKA 446
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRPEnvglQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50310159 447 NDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVK 515
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
48-520 |
2.49e-178 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 510.50 E-value: 2.49e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 48 PTGLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGVWSKVDPLVRSQCLSKLADYIEKDL 127
Cdd:cd07140 5 PHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 128 DTIASIESLDNGKAISSA-KGDVQLVVNYLRSAAGYADKVDGRVIDTGSTH----FSYTVREPLGVCGQIIPWNFPLLMW 202
Cdd:cd07140 85 EELATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARpnrnLTLTKREPIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 203 AWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQ 282
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 283 NAGV-NLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPF 361
Cdd:cd07140 245 SCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 362 DAETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKT--I 439
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 440 DELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
.
gi 50310159 520 K 520
Cdd:cd07140 485 E 485
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
68-519 |
2.18e-177 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 506.84 E-value: 2.18e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 68 VLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKG 147
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE--WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 148 DVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLS 227
Cdd:cd07090 79 DIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 228 ALYVSQYIPKAGIPDGVVNIVSGFGKiVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADA 307
Cdd:cd07090 159 ALLLAEILTEAGLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 308 NLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGK 387
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 388 NEGATLITGGERIG-----DKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNI 462
Cdd:cd07090 318 QEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 50310159 463 NTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
68-517 |
3.84e-177 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 505.81 E-value: 3.84e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 68 VLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKG 147
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKT--WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 148 DVQLVVNYLRSAAGYADKVDGRVIDTGS-THFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPL 226
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIPSPApGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 227 SALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFAD 306
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 307 ANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIG 386
Cdd:cd07103 239 ADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 387 KNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAI 466
Cdd:cd07103 319 VAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 50310159 467 QVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07103 399 RVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
51-517 |
3.59e-175 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 501.65 E-value: 3.59e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 51 LFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTI 130
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WSATSVEERAALLERIAEAYEARADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 131 ASIESLDNGKAISSAKGD-VQLVVNYLRSAAGYADKVDGRvIDTGSTHFsytVREPLGVCGQIIPWNFPLLMWAWKIAPA 209
Cdd:cd07138 79 AQAITLEMGAPITLARAAqVGLGIGHLRAAADALKDFEFE-ERRGNSLV---VREPIGVCGLITPWNWPLNQIVLKVAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 210 LATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLK 289
Cdd:cd07138 155 LAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 290 KVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGA 369
Cdd:cd07138 235 RVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 370 QTSQNQLDKILKYVEIGKNEGATLITGG----ERIgDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEK 445
Cdd:cd07138 315 LASAAQFDRVQGYIQKGIEEGARLVAGGpgrpEGL-ERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAI 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50310159 446 ANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINtYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07138 394 ANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
48-522 |
1.03e-174 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 500.59 E-value: 1.03e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 48 PTGLFINNQFVPSkQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDL 127
Cdd:PRK13473 2 QTKLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAIEENA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 128 DTIASIESLDNGKAISSAKGD-VQLVVNYLRSAAGYADKVDGRVidTG---STHFSYTVREPLGVCGQIIPWNFPLLMWA 203
Cdd:PRK13473 79 DEFARLESLNCGKPLHLALNDeIPAIVDVFRFFAGAARCLEGKA--AGeylEGHTSMIRRDPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 204 WKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAgIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQN 283
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 284 AGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDA 363
Cdd:PRK13473 236 AADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 364 ETFQGAQTSQNQLDKILKYVEIGKNEG-ATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDEL 442
Cdd:PRK13473 316 DTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 443 IEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRVKLE 522
Cdd:PRK13473 396 VRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKHT 475
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
68-519 |
9.06e-173 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 494.83 E-value: 9.06e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 68 VLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKG 147
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESG-WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 148 DVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLS 227
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 228 ALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADA 307
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 308 NLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGdPFDAETFQGAQTSQNQLDKILKYVEIGK 387
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 388 NEGATLITGGERIGD---KGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINT 464
Cdd:cd07109 319 ARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 50310159 465 AIQVSNRLNAGTVWINTYNDFHHC-VPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07109 399 ALRVARRLRAGQVFVNNYGAGGGIeLPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
68-517 |
2.53e-172 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 493.58 E-value: 2.53e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 68 VLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKG 147
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 148 DVQLVVNYLRSAAGYADKVdgRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLS 227
Cdd:cd07106 79 EVGGAVAWLRYTASLDLPD--EVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 228 ALYVSQYIPKAgIPDGVVNIVSGfGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADA 307
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 308 NLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGK 387
Cdd:cd07106 235 DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 388 NEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQ 467
Cdd:cd07106 315 AKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEA 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 50310159 468 VSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07106 395 VARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
51-517 |
2.56e-171 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 492.09 E-value: 2.56e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 51 LFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGVWSKVDPLVRSQCLSKLADYIEKDLDTI 130
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 131 ASIESLDNGKAIS-SAKGDVQLVVNYLRSAAGYADK---VDGRVIDTGSThfSYTVREPLGVCGQIIPWNFPLLMWAWKI 206
Cdd:cd07139 81 ARLWTAENGMPISwSRRAQGPGPAALLRYYAALARDfpfEERRPGSGGGH--VLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 207 APALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGfGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGV 286
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 287 NLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETF 366
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 367 QGAQTSQNQLDKILKYVEIGKNEGATLITGGERIG--DKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIE 444
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50310159 445 KANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTY-NDFHhcVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFrLDFG--APFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
50-511 |
8.99e-171 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 491.14 E-value: 8.99e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 50 GLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDT 129
Cdd:cd07111 23 GHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 130 IASIESLDNGKAI-SSAKGDVQLVVNYLRSAAGYADKVDgrvidtgsthFSYTVREPLGVCGQIIPWNFPLLMWAWKIAP 208
Cdd:cd07111 101 FAVLESLDNGKPIrESRDCDIPLVARHFYHHAGWAQLLD----------TELAGWKPVGVVGQIVPWNFPLLMLAWKICP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 209 ALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKiVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNL 288
Cdd:cd07111 171 ALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAGTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 289 KKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQG 368
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 369 AQTSQNQLDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKAND 448
Cdd:cd07111 330 AIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANN 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50310159 449 SEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNY 511
Cdd:cd07111 410 TPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
68-519 |
1.12e-170 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 489.53 E-value: 1.12e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 68 VLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKG 147
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 148 D-VQLVVNYLRSAAGYADKVDGRVidTGS---THFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAES 223
Cdd:cd07092 79 DeLPGAVDNFRFFAGAARTLEGPA--AGEylpGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 224 TPLSALYVSQyIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVV 303
Cdd:cd07092 157 TPLTTLLLAE-LAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 304 FADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYV 383
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 384 EiGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNIN 463
Cdd:cd07092 316 E-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 50310159 464 TAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07092 395 RAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
50-521 |
2.17e-169 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 487.78 E-value: 2.17e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 50 GLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDT 129
Cdd:TIGR02299 2 GHFIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKR--WAELKAAERKRYLHKIADLIEQHADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 130 IASIESLDNGKAISSAKgdvQLVVnylRSAAG---YADK----VDGRVIDTgSTHFSYTVREPLGVCGQIIPWNFPLLMW 202
Cdd:TIGR02299 80 IAVLECLDCGQPLRQTR---QQVI---RAAENfrfFADKceeaMDGRTYPV-DTHLNYTVRVPVGPVGLITPWNAPFMLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 203 AWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQ 282
Cdd:TIGR02299 153 TWKIAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 283 NAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFD 362
Cdd:TIGR02299 233 NGADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 363 AETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERIGD-------KGYFVRPTIFADVEESMRIVKEEIFGPVVTVTK 435
Cdd:TIGR02299 313 PETEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPTfrgedlgRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 436 FKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVK 515
Cdd:TIGR02299 393 FKDEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETK 472
|
....*.
gi 50310159 516 AVRVKL 521
Cdd:TIGR02299 473 NVALAL 478
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
68-517 |
1.21e-167 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 482.24 E-value: 1.21e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 68 VLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKG 147
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 148 DVQLVVNYLRSAAGYADKVD---GRVIDTGSTHFS-YTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAES 223
Cdd:cd07110 79 DVDDVAGCFEYYADLAEQLDakaERAVPLPSEDFKaRVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 224 TPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVV 303
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 304 FADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYV 383
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 384 EIGKNEGATLITGGER--IGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSN 461
Cdd:cd07110 319 ARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 50310159 462 INTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07110 399 AERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
68-517 |
2.32e-166 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 479.05 E-value: 2.32e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 68 VLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGVWSkVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKG 147
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 148 -DVQLVVNYLRSAAGYADKVDGRVI-----DTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTA 221
Cdd:cd07089 80 mQVDGPIGHLRYFADLADSFPWEFDlpvpaLRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 222 ESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPN 301
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 302 VVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILK 381
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 382 YVEIGKNEGATLITGGERI--GDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHT 459
Cdd:cd07089 320 YIARGRDEGARLVTGGGRPagLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 50310159 460 SNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07089 400 ADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
52-517 |
1.29e-165 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 477.51 E-value: 1.29e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 52 FINNQFVPSkqGKTFEVLSPSTEEEITHVY-EGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTI 130
Cdd:cd07097 4 YIDGEWVAG--GDGEENRNPSDTSDVVGKYaRASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 131 ASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDtgSTH---FSYTVREPLGVCGQIIPWNFPLLMWAWKIA 207
Cdd:cd07097 80 ARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLP--STRpgvEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 208 PALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVN 287
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 288 LKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQ 367
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 368 GAQTSQNQLDKILKYVEIGKNEGATLITGGERI--GDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEK 445
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50310159 446 ANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWIN---TYNDFHhcVPFGGFNASGIG-REMGSEALDNYTQVKAV 517
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlptAGVDYH--VPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
52-517 |
9.38e-165 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 475.22 E-value: 9.38e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 52 FINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIA 131
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 132 SIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFS-YTVREPLGVCGQIIPWNFPLLMWAWKIAPAL 210
Cdd:cd07088 79 KLIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENiFIFKVPIGVVAGILPWNFPFFLIARKLAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 211 ATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKK 290
Cdd:cd07088 159 VTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 291 VTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQ 370
Cdd:cd07088 239 VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 371 TSQNQLDKILKYVEIGKNEGATLITGGERI-GDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDS 449
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDS 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50310159 450 EYGLAAGIHTSNINTAIQVSNRLNAGTVWIN-----TYNDFHHcvpfgGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07088 399 EYGLTSYIYTENLNTAMRATNELEFGETYINrenfeAMQGFHA-----GWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
52-519 |
1.05e-162 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 470.40 E-value: 1.05e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 52 FINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIA 131
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 132 SIESLDNGKAISSAKG-DVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPAL 210
Cdd:cd07116 82 VAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 211 ATGNTVVLKTAESTPLSALYVSQYIPKAgIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKK 290
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 291 VTLELGGKSPNVVFA------DANLKSAVQNSLLgIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAE 364
Cdd:cd07116 241 VTLELGGKSPNIFFAdvmdadDAFFDKALEGFVM-FALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 365 TFQGAQTSQNQLDKILKYVEIGKNEGATLITGGER-----IGDKGYFVRPTIFADveESMRIVKEEIFGPVVTVTKFKTI 439
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelggLLGGGYYVPTTFKGG--NKMRIFQEEIFGPVLAVTTFKDE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 440 DELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07116 398 EEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
68-519 |
2.30e-162 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 468.76 E-value: 2.30e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 68 VLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAI-SSAK 146
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPE--WAATPARERGKLLARIADALEARSEELARLLALETGNALrTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 147 GDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPL 226
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 227 SALYVSQyIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFAD 306
Cdd:cd07108 159 AVLLLAE-ILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 307 ANLKSAVQNSLLGI-YYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEI 385
Cdd:cd07108 238 ADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 386 GKNE-GATLITGG----ERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTS 460
Cdd:cd07108 318 GLSTsGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 461 NINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEA-LDNYTQVKAVRV 519
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTVNI 457
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
93-517 |
1.55e-161 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 463.24 E-value: 1.55e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 93 EAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDG-RVI 171
Cdd:cd06534 1 AAARAAFKA--WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGpELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 172 DTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGF 251
Cdd:cd06534 79 SPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 252 GKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAG 331
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 332 SRLYVEESIYDDFLKEIKsasealkvgdpfdaetfqgaqtsqnqldkilkyveigknegatlitggerigdkgyfvrpTI 411
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV------------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 412 FADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHC-VP 490
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPeAP 338
|
410 420
....*....|....*....|....*..
gi 50310159 491 FGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLEEYTRTKTV 365
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
52-519 |
1.70e-157 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 457.19 E-value: 1.70e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 52 FINNQFVPSKQGKTFEVLSPSTEEEITHVY-EGREEDVDAAVEAADKAFksGVWSKVDPLVRSQCLSKLADYIEKDLDTI 130
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVVGTFpLSTASDVDAAVEAAREAF--PEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 131 ASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTG-STHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPA 209
Cdd:cd07131 80 ARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 210 LATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLK 289
Cdd:cd07131 160 LVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 290 KVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGA 369
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 370 QTSQNQLDKILKYVEIGKNEGATLITGGERI----GDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEK 445
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50310159 446 ANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWIN--TYNDFHHcVPFGGFNASGIG-REMGSEALDNYTQVKAVRV 519
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGAEVH-LPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
23-522 |
1.51e-155 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 452.81 E-value: 1.51e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 23 HALRYYSHLPLKVKVDlpngisyeqpTGLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSG 102
Cdd:PRK09847 4 HHLAYWQDKALSLAIE----------NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 103 VWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAIS-SAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYT 181
Cdd:PRK09847 74 DWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRhSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 182 VREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITT 261
Cdd:PRK09847 154 VREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 262 HPKIKKVAFTGSTATGRHIYQNAG-VNLKKVTLELGGKSPNVVFADA-NLKSAVQNSLLGIYYNSGEVCCAGSRLYVEES 339
Cdd:PRK09847 234 HNDIDAIAFTGSTRTGKQLLKDAGdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 340 IYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGKNEGaTLITGGERIGDKGYfVRPTIFADVEESM 419
Cdd:PRK09847 314 IADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-IGPTIFVDVDPNA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 420 RIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGI 499
Cdd:PRK09847 392 SLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGN 471
|
490 500
....*....|....*....|...
gi 50310159 500 GREMGSEALDNYTQVKAVRVKLE 522
Cdd:PRK09847 472 GRDKSLHALEKFTELKTIWISLE 494
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
50-517 |
2.82e-154 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 449.95 E-value: 2.82e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 50 GLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAF---KSGVWSKVDPLVRSQCLSKLADYIEKD 126
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnKGKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 127 LDTIASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRV---IDTGSTHF-SYTVREPLGVCGQIIPWNFPLLMW 202
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQkapVSLPMETFkGYVLKEPLGVVGLITPWNYPLLMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 203 AWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQ 282
Cdd:PLN02467 169 TWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 283 NAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFD 362
Cdd:PLN02467 249 AAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 363 AETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERIGD--KGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTID 440
Cdd:PLN02467 329 EGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTED 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50310159 441 ELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:PLN02467 409 EAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
87-519 |
2.68e-153 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 444.67 E-value: 2.68e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 87 DVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASI---ESldnGKAISSAKGDVQLVVNYLRSAAGYA 163
Cdd:cd07104 1 DVDRAYAAAAAAQKA--WAATPPQERAAILRKAAEILEERRDEIADWlirES---GSTRPKAAFEVGAAIAILREAAGLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 164 DKVDGRVIDTGST-HFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLS-ALYVSQYIPKAGIP 241
Cdd:cd07104 76 RRPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 242 DGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIY 321
Cdd:cd07104 156 KGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 322 YNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERig 401
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 402 dKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWIN- 480
Cdd:cd07104 314 -EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINd 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 50310159 481 -TYNDFHHcVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07104 393 qTVNDEPH-VPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
50-520 |
3.48e-153 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 446.12 E-value: 3.48e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 50 GLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGvWSKVDPLVRSQCLSKLADYIEKDLDT 129
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSA-WAKTTPAERGRILLRLADLIEQHGEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 130 IASIESLDNGKAISSAKG-DVQLVVNYLRSAAGYADKVDGRVID------TGSTHFSYTVREPLGVCGQIIPWNFPLLMW 202
Cdd:cd07113 80 LAQLETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLApsipsmQGERYTAFTRREPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 203 AWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKiVGEAITTHPKIKKVAFTGSTATGRHIYQ 282
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 283 NAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFD 362
Cdd:cd07113 239 QAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 363 AETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDEL 442
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50310159 443 IEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRVK 520
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
66-519 |
8.91e-150 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 436.38 E-value: 8.91e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 66 FEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSA 145
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPA--WAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 146 KGDVQLVVNYLRSAAGYADKVDGRVIDTGST-HFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAEST 224
Cdd:cd07150 79 WFETTFTPELLRAAAGECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 225 PLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVF 304
Cdd:cd07150 159 PVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 305 ADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVE 384
Cdd:cd07150 239 ADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 385 IGKNEGATLITGGERigdKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINT 464
Cdd:cd07150 319 DAVAKGAKLLTGGKY---DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 50310159 465 AIQVSNRLNAGTVWIN--TYNDFHHcVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07150 396 AFKLAERLESGMVHINdpTILDEAH-VPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
68-521 |
2.10e-148 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 432.95 E-value: 2.10e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 68 VLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKG 147
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE--WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 148 DVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLS 227
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 228 ALYVSQYIPKAgIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADA 307
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 308 NLKSAVQNSLLGIYYN-SGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIG 386
Cdd:cd07107 238 DPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 387 KNEGATLITGGER----IGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNI 462
Cdd:cd07107 318 KREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 50310159 463 NTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRVKL 521
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
66-517 |
3.02e-144 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 422.39 E-value: 3.02e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 66 FEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGvwSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSA 145
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM--KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 146 KGDVQLVVNYLRSAAGYADKVDGRVIDT-----GSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKT 220
Cdd:cd07149 79 RKEVDRAIETLRLSAEEAKRLAGETIPFdaspgGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 221 AESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGvnLKKVTLELGGKSP 300
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 301 NVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKIL 380
Cdd:cd07149 237 VIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 381 KYVEIGKNEGATLITGGERIGDkgyFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTS 460
Cdd:cd07149 317 EWVEEAVEGGARLLTGGKRDGA---ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTN 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 461 NINTAIQVSNRLNAGTVWINTYNDF---HhcVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07149 394 DLQKALKAARELEVGGVMINDSSTFrvdH--MPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
69-517 |
1.42e-143 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 420.60 E-value: 1.42e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 69 LSPSTEEEITHVYEGREEDVDAAVEAADKAFKSGVWSkVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGD 148
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 149 VQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSA 228
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 229 LYVSQYIPKA-GIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADA 307
Cdd:cd07120 161 AAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 308 NLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGK 387
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 388 NEGATLITGGERIGD---KGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINT 464
Cdd:cd07120 321 AAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLAR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 50310159 465 AIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07120 401 AMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
52-519 |
2.22e-139 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 410.80 E-value: 2.22e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 52 FINNQFVPSKqGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKsgVWSKVDPLVRSQCLSKLADYIEKDLDTIA 131
Cdd:cd07086 2 VIGGEWVGSG-GETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFK--EWRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 132 SIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTG-STHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPAL 210
Cdd:cd07086 79 RLVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 211 ATGNTVVLKTAESTPLSALYVSQYIPKA----GIPDGVVNIVSGFGKiVGEAITTHPKIKKVAFTGSTATGRHIYQNAGV 286
Cdd:cd07086 159 VCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 287 NLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETF 366
Cdd:cd07086 238 RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 367 QGAQTSQNQLDKILKYVEIGKNEGATLITGGERI--GDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIE 444
Cdd:cd07086 318 VGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 445 KANDSEYGLAAGIHTSNINTAIQ-VSNR-LNAGTVWINTYN---DFHhcVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07086 398 INNDVPQGLSSSIFTEDLREAFRwLGPKgSDCGIVNVNIPTsgaEIG--GAFGGEKETGGGRESGSDAWKQYMRRSTCTI 475
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
66-515 |
1.24e-138 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 408.27 E-value: 1.24e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 66 FEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKsgVWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSA 145
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD--VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 146 KGDVQLVVNYLRSAAGYADKVDGRVI-----DTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKT 220
Cdd:cd07145 79 RVEVERTIRLFKLAAEEAKVLRGETIpvdayEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 221 AESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSP 300
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 301 NVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKIL 380
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERME 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 381 KYVEIGKNEGATLITGGERIGdkGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTS 460
Cdd:cd07145 319 NLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTN 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 50310159 461 NINTAIQVSNRLNAGTVWINTYNDFH-HCVPFGGFNASGIGREMGSEALDNYTQVK 515
Cdd:cd07145 397 DINRALKVARELEAGGVVINDSTRFRwDNLPFGGFKKSGIGREGVRYTMLEMTEEK 452
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
52-517 |
3.01e-135 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 400.99 E-value: 3.01e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 52 FINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIA 131
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPS--WSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 132 SIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIdtgSTHFS----YTVREPLGVCGQIIPWNFPLLMWAWKIA 207
Cdd:PLN02278 106 QLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDII---PSPFPdrrlLVLKQPVGVVGAITPWNFPLAMITRKVG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 208 PALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVN 287
Cdd:PLN02278 183 PALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 288 LKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQ 367
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 368 GAQTSQNQLDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKAN 447
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAN 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 448 DSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:PLN02278 423 DTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
55-520 |
1.42e-132 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 392.82 E-value: 1.42e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 55 NQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIE 134
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKE--WAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 135 SLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDT---GSTHFSYtvREPLGVCGQIIPWNFPLLMWAWKIAPALA 211
Cdd:cd07151 79 IRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSdvpGKENRVY--REPLGVVGVISPWNFPLHLSMRSVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 212 TGNTVVLKTAESTPLSA-LYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKK 290
Cdd:cd07151 157 LGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 291 VTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQ 370
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 371 TSQNQLDKILKYVEIGKNEGATLITGGERigdKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSE 450
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50310159 451 YGLAAGIHTSNINTAIQVSNRLNAGTVWIN--TYNDFHHcVPFGGFNASGIGREMGSEALDNYTQVKAVRVK 520
Cdd:cd07151 394 YGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVNDEPH-VPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
19-517 |
7.69e-131 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 390.04 E-value: 7.69e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 19 AAFAHALRyyshlplKVKVDLpnGISYeqptGLFINNQFVPSkqGKTFEVLSPS-TEEEITHVYEGREEDVDAAVEAADK 97
Cdd:cd07124 16 AAFRAALA-------RVREEL--GREY----PLVIGGKEVRT--EEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 98 AFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTH 177
Cdd:cd07124 81 AFPT--WRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 178 FSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGE 257
Cdd:cd07124 159 DNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 258 AITTHPKIKKVAFTGSTATGRHIYQNAGV------NLKKVTLELGGKSPNVVFADANLKSAVQnsllGIYYN----SGEV 327
Cdd:cd07124 239 YLVEHPDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAE----GIVRSafgfQGQK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 328 CCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGKNEGaTLITGGERIGD--KGY 405
Cdd:cd07124 315 CSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELaaEGY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 406 FVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYN-- 483
Cdd:cd07124 394 FVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKItg 473
|
490 500 510
....*....|....*....|....*....|....*...
gi 50310159 484 ---DFHhcvPFGGFNASGIG-REMGSEALDNYTQVKAV 517
Cdd:cd07124 474 alvGRQ---PFGGFKMSGTGsKAGGPDYLLQFMQPKTV 508
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
88-519 |
2.99e-129 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 382.96 E-value: 2.99e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 88 VDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGDVQLVVNYLRSaagYADKVD 167
Cdd:cd07100 1 IEAALDRAHAAFLA--WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRY---YAENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 168 G----RVIDTGSTHfSYTVREPLGVCGQIIPWNFPLlmwaWKI----APALATGNTVVLKTAESTPLSALYVSQYIPKAG 239
Cdd:cd07100 76 AfladEPIETDAGK-AYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 240 IPDGV-VNIVSGFGKIvgEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLL 318
Cdd:cd07100 151 FPEGVfQNLLIDSDQV--EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 319 GIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGE 398
Cdd:cd07100 229 GRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 399 RIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVW 478
Cdd:cd07100 309 RPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVF 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 50310159 479 INTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07100 389 INGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
49-517 |
4.32e-129 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 384.56 E-value: 4.32e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 49 TGLFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLD 128
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSATPVLKRQQVMFKFRQLLEENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 129 TIASIESLDNGKAISSAKGDVQL---VVNYLRSAA----GYADKVDGRVIDTgsthfsYTVREPLGVCGQIIPWNFPLLM 201
Cdd:cd07085 79 ELARLITLEHGKTLADARGDVLRgleVVEFACSIPhllkGEYLENVARGIDT------YSYRQPLGVVAGITPFNFPAMI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 202 WAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGfGKIVGEAITTHPKIKKVAFTGSTATGRHIY 281
Cdd:cd07085 153 PLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 282 QNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPF 361
Cdd:cd07085 232 ERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 362 DAETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERI----GDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFK 437
Cdd:cd07085 312 DPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 438 TIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINtyndfhhcVP---------FGGFNAS--GIGREMGSE 506
Cdd:cd07085 392 TLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN--------VPipvplaffsFGGWKGSffGDLHFYGKD 463
|
490
....*....|.
gi 50310159 507 ALDNYTQVKAV 517
Cdd:cd07085 464 GVRFYTQTKTV 474
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
69-517 |
1.08e-123 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 369.63 E-value: 1.08e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 69 LSPSTEEEITHVYEGREEDVDAAVEAADKAFKsgVWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGD 148
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQR--AWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 149 VQLVVNYLRSAAGYADKV-DGRVIDTGS---THFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAEST 224
Cdd:cd07099 79 VLLALEAIDWAARNAPRVlAPRKVPTGLlmpNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 225 PLSALYVSQYIPKAGIPDGVVNIVSGFGKiVGEAITTHpKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVF 304
Cdd:cd07099 159 PLVGELLAEAWAAAGPPQGVLQVVTGDGA-TGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 305 ADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVE 384
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 385 IGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINT 464
Cdd:cd07099 317 DAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 50310159 465 AIQVSNRLNAGTVWIN--TYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07099 397 AEAIARRLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
67-517 |
3.37e-121 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 363.29 E-value: 3.37e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 67 EVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKsgVWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAK 146
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAE--NRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 147 GDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFS-----YTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTA 221
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRGEEIPLDATQGSdnrlaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 222 ESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGvnLKKVTLELGGKSPN 301
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 302 VVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILK 381
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 382 YVEIGKNEGATLITGGERigdKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSN 461
Cdd:cd07094 318 WVEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 50310159 462 INTAIQVSNRLNAGTVWINTYNDFHH-CVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07094 395 LNVAFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
86-513 |
2.14e-117 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 353.14 E-value: 2.14e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 86 EDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADK 165
Cdd:cd07152 13 ADVDRAAARAAAAQRA--WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 166 VDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYV-SQYIPKAGIPDGV 244
Cdd:cd07152 91 PQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVViARLFEEAGLPAGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 245 VNIVSGfGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNS 324
Cdd:cd07152 171 LHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 325 GEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERigdKG 404
Cdd:cd07152 250 GQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTY---DG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 405 YFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWIN--TY 482
Cdd:cd07152 327 LFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINdqTV 406
|
410 420 430
....*....|....*....|....*....|..
gi 50310159 483 NDFHHcVPFGGFNASGIGREMGSEA-LDNYTQ 513
Cdd:cd07152 407 NDEPH-NPFGGMGASGNGSRFGGPAnWEEFTQ 437
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
87-519 |
2.46e-117 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 352.65 E-value: 2.46e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 87 DVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKV 166
Cdd:cd07105 1 DADQAVEAAAAAFPA--WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 167 DGRVI-DTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVV 245
Cdd:cd07105 79 IGGSIpSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 246 NIVS----GFGKIVgEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIY 321
Cdd:cd07105 159 NVVThspeDAPEVV-EALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 322 YNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDpfdaeTFQGAQTSQNQLDKILKYVEIGKNEGATLITGG-ERI 400
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGlADE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 401 GDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWIN 480
Cdd:cd07105 313 SPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 50310159 481 --TYNDfHHCVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07105 393 gmTVHD-EPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
58-517 |
3.10e-116 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 353.03 E-value: 3.10e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 58 VPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLD 137
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRA--WAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 138 NGKAISSAKGDVQLVVN----YLRSAAGY--ADKVDGRV-IDTGSTHfsytVREPLGVCGQIIPWNFPLLMWAWKIAPAL 210
Cdd:PRK09407 104 TGKARRHAFEEVLDVALtaryYARRAPKLlaPRRRAGALpVLTKTTE----LRQPKGVVGVISPWNYPLTLAVSDAIPAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 211 ATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHpkIKKVAFTGSTATGRHIYQNAGVNLKK 290
Cdd:PRK09407 180 LAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 291 VTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQ 370
Cdd:PRK09407 258 FSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 371 TSQNQLDKILKYVEIGKNEGATLITGGERIGDKG-YFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDS 449
Cdd:PRK09407 338 ISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDT 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50310159 450 EYGLAAGIHTSNINTAIQVSNRLNAGTVWIN-----TY--NDfhhcVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:PRK09407 418 PYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWgsVD----APMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
51-517 |
4.54e-116 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 352.31 E-value: 4.54e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 51 LFINNQFVPSKqgKTFEVLSPS-TEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDT 129
Cdd:PRK03137 39 LIIGGERITTE--DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFET--WKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 130 IASIESLDNGKAISSAKGDVQLVVNYL----RSAAGYADKVDgrVIDTGSTHFSYtVREPLGVCGQIIPWNFPLLMWAWK 205
Cdd:PRK03137 115 FSAWLVKEAGKPWAEADADTAEAIDFLeyyaRQMLKLADGKP--VESRPGEHNRY-FYIPLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 206 IAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAG 285
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 286 VN------LKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGD 359
Cdd:PRK03137 272 KVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 360 PFDAeTFQGAQTSQNQLDKILKYVEIGKNEGaTLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTI 439
Cdd:PRK03137 352 PEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 440 DELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINtyndfHHCV-------PFGGFNASGIGREMGS-EALDNY 511
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN-----RGCTgaivgyhPFGGFNMSGTDSKAGGpDYLLLF 504
|
....*.
gi 50310159 512 TQVKAV 517
Cdd:PRK03137 505 LQAKTV 510
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
52-517 |
3.28e-115 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 348.79 E-value: 3.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 52 FINNQFVPSKqGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLV-RSQCLSKLADYIEKDLDTI 130
Cdd:cd07082 5 LINGEWKESS-GKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRG--WWPTMPLEeRIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 131 ASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFS-----YTVREPLGVCGQIIPWNFPLLMWAWK 205
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTkgkiaQVRREPLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 206 IAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAG 285
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 286 VnlKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAET 365
Cdd:cd07082 242 M--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 366 FQGAQTSQNQLDKILKYVEIGKNEGATLITGGERIGdkGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEK 445
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50310159 446 ANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYN----DFHhcvPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCqrgpDHF---PFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
66-515 |
1.27e-114 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 346.54 E-value: 1.27e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 66 FEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSA 145
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRP--MRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 146 KGDVQLVVNYLRSAAGYADKVDGRVID-----TGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKT 220
Cdd:cd07147 79 RGEVARAIDTFRIAAEEATRIYGEVLPldisaRGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 221 AESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIvGEAITTHPKIKKVAFTGSTATGRHIYQNAGVnlKKVTLELGGKSP 300
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 301 NVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKIL 380
Cdd:cd07147 236 VIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 381 KYVEIGKNEGATLITGGERigdKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTS 460
Cdd:cd07147 316 GWVNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 50310159 461 NINTAIQVSNRLNAGTVWIN---TYNDFHhcVPFGGFNASGIGREMGSEALDNYTQVK 515
Cdd:cd07147 393 DLEKALRAWDELEVGGVVINdvpTFRVDH--MPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
70-519 |
6.37e-112 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 339.67 E-value: 6.37e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 70 SPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGDV 149
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 150 QLVVN----YLRSAAGY-ADKVDGRVID--TGSTHFsytvREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAE 222
Cdd:cd07101 80 LDVAIvaryYARRAERLlKPRRRRGAIPvlTRTTVN----RRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 223 STPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIkkVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNV 302
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 303 VFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKY 382
Cdd:cd07101 234 VLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 383 VEIGKNEGATLITGGERIGDKG-YFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSN 461
Cdd:cd07101 314 VDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50310159 462 INTAIQVSNRLNAGTVWIN-----TYNDFHhcVPFGGFNASGIGREMGSEALDNYTQVKAVRV 519
Cdd:cd07101 394 GARGRRIAARLRAGTVNVNegyaaAWASID--APMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
116-517 |
3.70e-111 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 336.32 E-value: 3.70e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 116 LSKLADYIEKDLDTIASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDT---GSTHFSYtvREPLGVCGQI 192
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSdrpGENILLF--KRALGVTTGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 193 IPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTG 272
Cdd:PRK10090 79 LPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 273 STATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSAS 352
Cdd:PRK10090 159 SVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 353 EALKVGDPFDAETFQ-GAQTSQNQLDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVV 431
Cdd:PRK10090 239 QAVQFGNPAERNDIAmGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 432 TVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTYN-----DFHhcvpfGGFNASGIGREMGSE 506
Cdd:PRK10090 319 PVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENfeamqGFH-----AGWRKSGIGGADGKH 393
|
410
....*....|.
gi 50310159 507 ALDNYTQVKAV 517
Cdd:PRK10090 394 GLHEYLQTQVV 404
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
67-515 |
9.07e-109 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 331.63 E-value: 9.07e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 67 EVLSPSTEEEITHVYEGREEDVDAAVEAAdkafkSGVWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAK 146
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALA-----ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 147 GDVQLVVNYLRSAAGYADKVDGRVID-----TGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTA 221
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFScdltaNGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 222 ESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGvnLKKVTLELGGKSPN 301
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 302 VVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILK 381
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 382 YVEIGKNEGATLITGGERigdKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSN 461
Cdd:cd07146 315 RVEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 50310159 462 INTAIQVSNRLNAGTVWINTYNDFH-HCVPFGGFNASGIG-REMGSEALDNYTQVK 515
Cdd:cd07146 392 LDTIKRLVERLDVGTVNVNEVPGFRsELSPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
69-517 |
7.57e-106 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 323.81 E-value: 7.57e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 69 LSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGD 148
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG--WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 149 VQLVVNYLRSAAGYADKV--DGRVIDTGSTHfSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPL 226
Cdd:cd07102 79 IRGMLERARYMISIAEEAlaDIRVPEKDGFE-RYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 227 SALYVSQYIPKAGIPDGVVNIVSGFGKiVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFAD 306
Cdd:cd07102 158 CGERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 307 ANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIG 386
Cdd:cd07102 237 ADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 387 KNEGATLITGGER---IGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNIN 463
Cdd:cd07102 317 IAKGARALIDGALfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 50310159 464 TAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07102 397 RAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
52-515 |
5.00e-105 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 323.01 E-value: 5.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 52 FINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKsgVWSKVDPLVRSQCLSKLADYIEKDLDTIA 131
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--AWRALTAKERANILRRWFNLMMEHQDDLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 132 SIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTV-REPLGVCGQIIPWNFPLLMWAWKIAPAL 210
Cdd:PRK11241 92 RLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIViKQPIGVTAAITPWNFPAAMITRKAGPAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 211 ATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKK 290
Cdd:PRK11241 172 AAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 291 VTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQ 370
Cdd:PRK11241 252 VSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 371 TSQNQLDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSE 450
Cdd:PRK11241 332 IDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTE 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50310159 451 YGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVK 515
Cdd:PRK11241 412 FGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
51-517 |
2.18e-99 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 309.49 E-value: 2.18e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 51 LFINNQFVPSkQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTI 130
Cdd:TIGR01237 35 LVINGERVET-ENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEA--WKKTDPEERAAILFKAAAIVRRRRHEF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 131 ASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDT---GSTH-FSYTvrePLGVCGQIIPWNFPLLMWAWKI 206
Cdd:TIGR01237 112 SALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNsreGETNqYVYT---PTGVTVVISPWNFPFAIMVGMT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 207 APALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGV 286
Cdd:TIGR01237 189 VAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 287 ------NLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDP 360
Cdd:TIGR01237 269 vqpgqkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPP 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 361 FDAETFQGAQTSQNQLDKILKYVEIGKNEGaTLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTID 440
Cdd:TIGR01237 349 DSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFD 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 441 ELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINtyndfHHCV-------PFGGFNASGIGREMGS-EALDNYT 512
Cdd:TIGR01237 428 EALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFN-----RNITgaivgyqPFGGFKMSGTDSKAGGpDYLALFM 502
|
....*
gi 50310159 513 QVKAV 517
Cdd:TIGR01237 503 QAKTV 507
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
71-517 |
1.71e-97 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 303.07 E-value: 1.71e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 71 PSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKA-ISSAKGDV 149
Cdd:cd07098 3 PATGQHLGSVPADTPEDVDEAIAAARAAQRE--WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 150 QLVVNYLRSAAGYADKV---DGRVIDTGSTHFSYTVR-EPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTP 225
Cdd:cd07098 81 LVTCEKIRWTLKHGEKAlrpESRPGGLLMFYKRARVEyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 226 LSALYVSQYIPKA----GIPDGVVNIVSGFGKiVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPN 301
Cdd:cd07098 161 WSSGFFLSIIREClaacGHDPDLVQLVTCLPE-TAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 302 VVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILK 381
Cdd:cd07098 240 IVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 382 YVEIGKNEGATLITGGERIGD----KGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGI 457
Cdd:cd07098 320 LVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50310159 458 HTSNINTAIQVSNRLNAGTVWINTYNDFHHCV--PFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07098 400 FGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGRFAGEEGLRGLCNPKSV 461
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
61-511 |
5.57e-87 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 276.01 E-value: 5.57e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 61 KQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKsgVWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGK 140
Cdd:cd07130 9 GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK--EWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 141 AISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTG-STHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLK 219
Cdd:cd07130 87 ILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSErPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 220 TAESTPLSALYVSQYIPKA----GIPDGVVNIVSGfGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLEL 295
Cdd:cd07130 167 PSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 296 GGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQ 375
Cdd:cd07130 246 GGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 376 LDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIfADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAA 455
Cdd:cd07130 326 VDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSS 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50310159 456 GIHTSNINTAIQVSNRLNA--GTVWINtyndfhhcVP---------FGGFNASGIGREMGSEALDNY 511
Cdd:cd07130 405 SIFTTDLRNAFRWLGPKGSdcGIVNVN--------IGtsgaeiggaFGGEKETGGGRESGSDAWKQY 463
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
64-517 |
2.25e-86 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 273.92 E-value: 2.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 64 KTFEVLSpsteeeithvyegrEEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAIS 143
Cdd:PRK09406 15 KTFTALT--------------DDEVDAAIARAHARFRD--YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 144 SAKGDVQLVVNYLRSAAGYADKV----DGRVIDTGSTHfSYTVREPLGVCGQIIPWNFPLlmwaWKI----APALATGNT 215
Cdd:PRK09406 79 SAKAEALKCAKGFRYYAEHAEALladePADAAAVGASR-AYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 216 VVLKTAESTPLSALYVSQYIPKAGIPDGV-VNIVSGFGKIvgEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLE 294
Cdd:PRK09406 154 GLLKHASNVPQTALYLADLFRRAGFPDGCfQTLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 295 LGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQN 374
Cdd:PRK09406 232 LGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 375 QLDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLA 454
Cdd:PRK09406 312 GRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50310159 455 AGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:PRK09406 392 SNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
36-504 |
2.04e-85 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 273.30 E-value: 2.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 36 KVDLPNGISYEQPTGLFINNQfvPSKQGKTFEVLSPSTEEEIT-HVYEGREEDVDAAVEAADKAFksGVWSKVDPLVRSQ 114
Cdd:cd07125 20 ADALKAFDEKEWEAIPIINGE--ETETGEGAPVIDPADHERTIgEVSLADAEDVDAALAIAAAAF--AGWSATPVEERAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 115 CLSKLADYIEKDLDTIASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVR-EPLGVCGQII 193
Cdd:cd07125 96 ILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLElHGRGVFVCIS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 194 PWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGS 273
Cdd:cd07125 176 PWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 274 TATGRHIYQ-NAGVNLKKVTL--ELGGKspNVVFAD--ANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEI 348
Cdd:cd07125 256 TETAKLINRaLAERDGPILPLiaETGGK--NAMIVDstALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEML 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 349 KSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGKNEgATLITGGERIGDKGYFVRPTIFADVeeSMRIVKEEIFG 428
Cdd:cd07125 334 KGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 429 PVVTVTKFK--TIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTyNDFHHCV---PFGGFNASGIGREM 503
Cdd:cd07125 411 PILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINR-NITGAIVgrqPFGGWGLSGTGPKA 489
|
.
gi 50310159 504 G 504
Cdd:cd07125 490 G 490
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
51-504 |
3.82e-85 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 272.14 E-value: 3.82e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 51 LFINNQFVPSKQGKTfeVLSPSTEEEI--THVYEGREEdVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLD 128
Cdd:cd07083 21 LVIGGEWVDTKERMV--SVSPFAPSEVvgTTAKADKAE-AEAALEAAWAAFKT--WKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 129 TIASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVID----TGSTHFSYTVrePLGVCGQIIPWNFPLLMWAW 204
Cdd:cd07083 96 ELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEvvpyPGEDNESFYV--GLGAGVVISPWNFPVAIFTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 205 KIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNA 284
Cdd:cd07083 174 MIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 285 GVNL------KKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVG 358
Cdd:cd07083 254 ARLApgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 359 DPFDAETFQGAQTSQNQLDKILKYVEIGKNEGaTLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKT 438
Cdd:cd07083 334 PPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKD 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50310159 439 ID--ELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTyNDFHHCV---PFGGFNASGIGREMG 504
Cdd:cd07083 413 DDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINR-KITGALVgvqPFGGFKLSGTNAKTG 482
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
69-517 |
1.23e-83 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 267.11 E-value: 1.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 69 LSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGD 148
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 149 VQlvvnylRSAA---GYAD------KVDGRVIDTGSTHFSYtvrEPLGVCGQIIPWNFPLlmwaWKI----APALATGNT 215
Cdd:PRK13968 90 VA------KSANlcdWYAEhgpamlKAEPTLVENQQAVIEY---RPLGTILAIMPWNFPL----WQVmrgaVPILLAGNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 216 VVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITThPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLEL 295
Cdd:PRK13968 157 YLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAIGAQAGAALKKCVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 296 GGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQ 375
Cdd:PRK13968 236 GGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 376 LDKILKYVEIGKNEGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAA 455
Cdd:PRK13968 316 RDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50310159 456 GIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:PRK13968 396 TIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
87-509 |
3.64e-76 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 246.41 E-value: 3.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 87 DVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGDVQLVVNYLR-SAAGYADK 165
Cdd:cd07095 1 QVDAAVAAARAAFPG--WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDiSIKAYHER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 166 VDGRVIDTGSTHFSYTVRePLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVV 245
Cdd:cd07095 79 TGERATPMAQGRAVLRHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 246 NIVSGfGKIVGEAITTHPKIKKVAFTGSTATGRHIYQN-AGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNS 324
Cdd:cd07095 158 NLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 325 GEVCCAGSRLYVEESIY-DDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERIGDK 403
Cdd:cd07095 237 GQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 404 GYFVRPTIFaDVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTV-WINTY 482
Cdd:cd07095 317 TAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVnWNRPT 395
|
410 420
....*....|....*....|....*..
gi 50310159 483 NDFHHCVPFGGFNASGIGREMGSEALD 509
Cdd:cd07095 396 TGASSTAPFGGVGLSGNHRPSAYYAAD 422
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
51-517 |
3.90e-76 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 247.87 E-value: 3.90e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 51 LFINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTI 130
Cdd:TIGR01722 3 HWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLT--WGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 131 ASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFS-YTVREPLGVCGQIIPWNFPLLMWAWKIAPA 209
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDvYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 210 LATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGfGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLK 289
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 290 KVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSrLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGA 369
Cdd:TIGR01722 240 RVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS-AAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 370 QTSQNQLDKILKYVEIGKNEGATLITGGERIGDKGY----FVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEK 445
Cdd:TIGR01722 319 LITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIAL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 446 ANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINtyndfhhcVP---------FGGFNASGIG--REMGSEALDNYTQV 514
Cdd:TIGR01722 399 INASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN--------VPipvplpyfsFTGWKDSFFGdhHIYGKQGTHFYTRG 470
|
...
gi 50310159 515 KAV 517
Cdd:TIGR01722 471 KTV 473
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
67-508 |
4.11e-72 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 236.55 E-value: 4.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 67 EVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKS-GVWskVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSA 145
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 146 KGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHFS-----YTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKT 220
Cdd:cd07148 80 KVEVTRAIDGVELAADELGQLGGREIPMGLTPASagriaFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 221 AESTPLSALYVSQYIPKAGIPDGVVNIVSGfGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNlKKVTLELGGKSP 300
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEGWCQAVPC-ENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 301 NVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKIL 380
Cdd:cd07148 238 VIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 381 KYVEIGKNEGATLITGGERIGDKGYfvRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTS 460
Cdd:cd07148 318 EWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTK 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 50310159 461 NINTAIQVSNRLNAGTVWINTYNDFH-HCVPFGGFNASGIG--------REMGSEAL 508
Cdd:cd07148 396 DLDVALKAVRRLDATAVMVNDHTAFRvDWMPFAGRRQSGYGtggipytmHDMTQEKM 452
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
63-500 |
1.57e-70 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 243.57 E-value: 1.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 63 GKTFEVLSPS-TEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKA 141
Cdd:PRK11904 561 GEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPA--WSRTPVEERAAILERAADLLEANRAELIALCVREAGKT 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 142 ISSAKGDVQLVVNYLRSAAGYADKVDGRVID----TGSTHFSYtvREPLGV--CgqIIPWNFPLLMWAWKIAPALATGNT 215
Cdd:PRK11904 639 LQDAIAEVREAVDFCRYYAAQARRLFGAPEKlpgpTGESNELR--LHGRGVfvC--ISPWNFPLAIFLGQVAAALAAGNT 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 216 VVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQN-AGVNLKKVTL- 293
Cdd:PRK11904 715 VIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTlAARDGPIVPLi 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 294 -ELGGKspNVVFADAN-LKSAVQNSLLGIYYNS-GEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQ 370
Cdd:PRK11904 795 aETGGQ--NAMIVDSTaLPEQVVDDVVTSAFRSaGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPV 872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 371 TSQNQLDKILKYVEIGKNEGATLITGGERIG-DKGYFVRPTIFadvE-ESMRIVKEEIFGPVVTVTKFKT--IDELIEKA 446
Cdd:PRK11904 873 IDAEAKANLDAHIERMKREARLLAQLPLPAGtENGHFVAPTAF---EiDSISQLEREVFGPILHVIRYKAsdLDKVIDAI 949
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 50310159 447 NDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTyNDFHHCV---PFGGFNASGIG 500
Cdd:PRK11904 950 NATGYGLTLGIHSRIEETADRIADRVRVGNVYVNR-NQIGAVVgvqPFGGQGLSGTG 1005
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
60-500 |
4.15e-69 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 240.54 E-value: 4.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 60 SKQGKTFEVLSPSTEEEIT-HVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDT---IASIES 135
Cdd:PRK11905 563 DVDGGTRPVLNPADHDDVVgTVTEASAEDVERALAAAQAAFPE--WSATPAAERAAILERAADLMEAHMPElfaLAVREA 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 136 ldnGKAISSAKGDVQLVVNYLRSaagYADkvdgRVIDTgsthFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNT 215
Cdd:PRK11905 641 ---GKTLANAIAEVREAVDFLRY---YAA----QARRL----LNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNT 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 216 VVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKK-VTL- 293
Cdd:PRK11905 707 VLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpVPLi 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 294 -ELGGKS---------PNVVFADAnLKSAVQnsllgiyyNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDA 363
Cdd:PRK11905 787 aETGGQNamivdssalPEQVVADV-IASAFD--------SAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRL 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 364 ETFQGAQTSQNQLDKILKYVEIGKNEGATLitggERIG-----DKGYFVRPTIFadvE-ESMRIVKEEIFGPVVTVTKFK 437
Cdd:PRK11905 858 STDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPlpaetEKGTFVAPTLI---EiDSISDLEREVFGPVLHVVRFK 930
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50310159 438 T--IDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTyNDFHHCV---PFGGFNASGIG 500
Cdd:PRK11905 931 AdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNR-NIIGAVVgvqPFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
63-500 |
4.89e-68 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 237.53 E-value: 4.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 63 GKTFEVLSPS-TEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKA 141
Cdd:COG4230 569 GEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA--WSATPVEERAAILERAADLLEAHRAELMALLVREAGKT 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 142 ISSAKGDVQLVVNYLRSaagYADKVdgrvidtgSTHFSY-TVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKT 220
Cdd:COG4230 647 LPDAIAEVREAVDFCRY---YAAQA--------RRLFAApTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKP 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 221 AESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQN-AGVNLKKVTL--ELGG 297
Cdd:COG4230 716 AEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTlAARDGPIVPLiaETGG 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 298 KspNVVFADAN----------LKSAVQNsllgiyynsgevccAGSR------LYVEESIYDDFLKEIKSASEALKVGDPF 361
Cdd:COG4230 796 Q--NAMIVDSSalpeqvvddvLASAFDS--------------AGQRcsalrvLCVQEDIADRVLEMLKGAMAELRVGDPA 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 362 DAETFQGAQTSQNQLDKILKYVEIGKNEGATLITGG-ERIGDKGYFVRPTIFadvE-ESMRIVKEEIFGPVVTVTKFK-- 437
Cdd:COG4230 860 DLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPlPEECANGTFVAPTLI---EiDSISDLEREVFGPVLHVVRYKad 936
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50310159 438 TIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINtyNDFHHCV----PFGGFNASGIG 500
Cdd:COG4230 937 ELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN--RNIIGAVvgvqPFGGEGLSGTG 1001
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
49-498 |
1.08e-66 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 223.30 E-value: 1.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 49 TGLFINNQFVPSkQGKTFEVLSPSTEEEIthvYEGR---EEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEK 125
Cdd:PRK09457 1 MTLWINGDWIAG-QGEAFESRNPVSGEVL---WQGNdatAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 126 DLDTIASIESLDNGKAISSAKGDVQLVVNYLR-SAAGYADKVDGRVIDTGSThfSYTVR-EPLGVCGQIIPWNFPLLMWA 203
Cdd:PRK09457 75 NKEELAEVIARETGKPLWEAATEVTAMINKIAiSIQAYHERTGEKRSEMADG--AAVLRhRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 204 WKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGfGKIVGEAITTHPKIKKVAFTGSTATGRHIYQN 283
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 284 -AGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDD-FLKEIKSASEALKVGDPF 361
Cdd:PRK09457 232 fAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 362 -DAETFQGAQTSQNQLDKILK-YVEIGKNEGATLITGGERIGDKGyFVRPTIFaDVEESMRIVKEEIFGPVVTVTKFKTI 439
Cdd:PRK09457 312 aEPQPFMGAVISEQAAQGLVAaQAQLLALGGKSLLEMTQLQAGTG-LLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDF 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 440 DELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTV-WINTYNDFHHCVPFGGFNASG 498
Cdd:PRK09457 390 DEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASG 449
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
59-515 |
2.68e-66 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 222.48 E-value: 2.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 59 PSKQGKTFEVLSPSTEEEIT-HVYEGREEDVDAAVEAADKAFKsgVWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLD 137
Cdd:TIGR01238 46 YKADGEAQPVTNPADRRDIVgQVFHANLAHVQAAIDSAQQAFP--TWNATPAKERAAKLDRLADLLELHMPELMALCVRE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 138 NGKAISSAKGDVQLVVNYLRSAAGYADKVdgrvidtgsthFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVV 217
Cdd:TIGR01238 124 AGKTIHNAIAEVREAVDFCRYYAKQVRDV-----------LGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 218 LKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQN---AGVNLKKVTLE 294
Cdd:TIGR01238 193 AKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTlaqREDAPVPLIAE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 295 LGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQG----AQ 370
Cdd:TIGR01238 273 TGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGpvidAE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 371 TSQNQLDKILKYVEIGKNEgATLITGGERIGDKGYFVRPTIFAdvEESMRIVKEEIFGPVVTVTKFKT--IDELIEKAND 448
Cdd:TIGR01238 353 AKQNLLAHIEHMSQTQKKI-AQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQ 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50310159 449 SEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTyNDFHHCV---PFGGFNASGIG-REMGSEALDNYTQVK 515
Cdd:TIGR01238 430 TGYGLTMGVHSRIETTYRWIEKHARVGNCYVNR-NQVGAVVgvqPFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
52-517 |
2.36e-65 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 222.70 E-value: 2.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 52 FINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKsgVWSKVDPLVRSQCLSKLADYIEKDLDTIA 131
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP--LWRNTPITTRQRVMLKFQELIRKNMDKLA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 132 SIESLDNGKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHF-SYTVREPLGVCGQIIPWNFPLLMWAWKIAPAL 210
Cdd:PLN02419 195 MNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVdTYSIREPLGVCAGICPFNFPAMIPLWMFPVAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 211 ATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVgEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKK 290
Cdd:PLN02419 275 TCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 291 VTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYV--EESIYDDFLKEiksASEALKV--GDPFDAETf 366
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgDAKSWEDKLVE---RAKALKVtcGSEPDADL- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 367 qGAQTSQNQLDKILKYVEIGKNEGATLITGGERI----GDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDEL 442
Cdd:PLN02419 430 -GPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 443 IEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTynDFHHCVPFGGF--NASGIGREM---GSEALDNYTQVKAV 517
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPFFSFtgNKASFAGDLnfyGKAGVDFFTQIKLV 586
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
63-511 |
6.78e-65 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 218.94 E-value: 6.78e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 63 GKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAI 142
Cdd:PLN02315 33 GPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI--WMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 143 SSAKGDVQLVVNYLRSAAGYADKVDGRVIDTGS-THFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTA 221
Cdd:PLN02315 111 AEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 222 ESTPLSALYVSQYIP----KAGIPDGVVNIVSGfGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGG 297
Cdd:PLN02315 191 PTTPLITIAMTKLVAevleKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 298 KSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLD 377
Cdd:PLN02315 270 NNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 378 KILKYVEIGKNEGATLITGGERIGDKGYFVRPTIfADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGI 457
Cdd:PLN02315 350 NFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSI 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 50310159 458 HTSNINTAIQVSNRL--NAGTVWINT-YNDFHHCVPFGGFNASGIGREMGSEALDNY 511
Cdd:PLN02315 429 FTRNPETIFKWIGPLgsDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQY 485
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
179-517 |
8.56e-65 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 216.62 E-value: 8.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 179 SYTVREPLGVCGQIIPWNFPLLMwawKIAP---ALATGNTVVLKTAESTPLSALYVSQYIPKAgIPDGVVNIVSGFGKiV 255
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYPLQL---ALAPligAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE-V 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 256 GEAITTHPkIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLY 335
Cdd:cd07087 169 ATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 336 VEESIYDDFLKEIKSASEALKVGDPFDAETFqGAQTSQNQLDKILKYVeigknEGATLITGGERIGDKGYFVrPTIFADV 415
Cdd:cd07087 248 VHESIKDELIEELKKAIKEFYGEDPKESPDY-GRIINERHFDRLASLL-----DDGKVVIGGQVDKEERYIA-PTILDDV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 416 EESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVwinTYND-FHHCV----P 490
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGV---CVNDvLLHAAipnlP 397
|
330 340
....*....|....*....|....*..
gi 50310159 491 FGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07087 398 FGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
52-522 |
7.77e-63 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 213.46 E-value: 7.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 52 FINNQFVPSKQGKTFEVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIA 131
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA--WAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 132 SIESLDNGKAISSAKGDVqlvvnyLRSA--AGYADKVDGRVIDTGS------------THFSYTVREPLGVCGQIIPWNF 197
Cdd:PLN00412 97 ECLVKEIAKPAKDAVTEV------VRSGdlISYTAEEGVRILGEGKflvsdsfpgnerNKYCLTSKIPLGVVLAIPPFNY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 198 PLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTaTG 277
Cdd:PLN00412 171 PVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 278 RHIYQNAGvnLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKV 357
Cdd:PLN00412 250 IAISKKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 358 GDPFDAETFQgAQTSQNQLDKILKYVEIGKNEGATLITGGERigdKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFK 437
Cdd:PLN00412 328 GPPEDDCDIT-PVVSESSANFIEGLVMDAKEKGATFCQEWKR---EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRIN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 438 TIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTY-----NDFhhcvPFGGFNASGIGREMGSEALDNYT 512
Cdd:PLN00412 404 SVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApargpDHF----PFQGLKDSGIGSQGITNSINMMT 479
|
490
....*....|
gi 50310159 513 QVKAVRVKLE 522
Cdd:PLN00412 480 KVKSTVINLP 489
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
61-505 |
6.44e-62 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 211.95 E-value: 6.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 61 KQGKTFEVLSPSTEE-EITHVYEGREEDVDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIE-KDLDTIASIESLDN 138
Cdd:TIGR01236 43 DSNERIPQVNPHNHQaVLAKATNATEEDAMKAVEAALDAKKD--WSNLPFYDRAAIFLKAADLLSgPYRYEILAATMLGQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 139 GKAISSAKGD-VQLVVNYLRSAAGYADKVDGRVIDTGSTHFSYTVREPL-GVCGQIIPWNFPLLMWAWKIAPALaTGNTV 216
Cdd:TIGR01236 121 SKTVYQAEIDaVAELIDFFRFNVKYARELYAQQPISAPGEWNRTEYRPLeGFVYAISPFNFTAIAGNLAGAPAL-MGNTV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 217 VLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLKK------ 290
Cdd:TIGR01236 200 VWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRyhnfpr 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 291 VTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQ 370
Cdd:TIGR01236 280 IVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 371 TSQNQLDKILKYVEIGKN--EGATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTV-----TKFKTIDELI 443
Cdd:TIGR01236 360 IDEQSFDKIVKYIEDAKKdpEALTILYGGKYDDSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVyvypdDKYKEILDLV 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50310159 444 EKAndSEYGLAAGIHTSN---INTAIQVSnRLNAGTVWINTyndfhHCV-------PFGGFNASGIGREMGS 505
Cdd:TIGR01236 440 DST--SQYGLTGAVFAKDrkaILEADKKL-RFAAGNFYIND-----KCTgavvgqqPFGGARMSGTNDKAGG 503
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
63-498 |
5.64e-60 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 206.28 E-value: 5.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 63 GKTFEVLSPSTEEE-ITHVYEGREEDVDAAVEAADKAFKsgVWSKVDPLVRSQCLSKLADYIE-KDLDTIASIESLDNGK 140
Cdd:cd07123 45 GNTGKQVMPHDHAHvLATYHYADAALVEKAIEAALEARK--EWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 141 AISSAKGDVQL-VVNYLRSAAGYADKV-DGRVIDTGSTHFSYTVREPL-GVCGQIIPWNFPLLMWAWKIAPALaTGNTVV 217
Cdd:cd07123 123 NVWQAEIDAACeLIDFLRFNVKYAEELyAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNFTAIGGNLAGAPAL-MGNVVL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 218 LKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNLK------KV 291
Cdd:cd07123 202 WKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtypRI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 292 TLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQT 371
Cdd:cd07123 282 VGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 372 SQNQLDKILKYVEIGKNE-GATLITGGERIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTV-----TKFKTIDELIEK 445
Cdd:cd07123 362 DEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVyvypdSDFEETLELVDT 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50310159 446 AndSEYGLAAGIHTSN---INTAIQVSnRLNAGTVWINTyndfhHCV-------PFGGFNASG 498
Cdd:cd07123 442 T--SPYALTGAIFAQDrkaIREATDAL-RNAAGNFYIND-----KPTgavvgqqPFGGARASG 496
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
176-517 |
3.74e-59 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 202.35 E-value: 3.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 176 THF---SYTVREPLGVCGQIIPWNFPLLMwawKIAP---ALATGNTVVLKTAESTPLSALYVSQYIPKAgIPDGVVNIVS 249
Cdd:cd07136 88 LNFpskSYIYYEPYGVVLIIAPWNYPFQL---ALAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 250 GfGKIVGEAITtHPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCC 329
Cdd:cd07136 164 G-GVEENQELL-DQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 330 AGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFqGAQTSQNQLDKILKYVEIGKnegatLITGGErIGDKGYFVRP 409
Cdd:cd07136 242 APDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDY-GRIINEKHFDRLAGLLDNGK-----IVFGGN-TDRETLYIEP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 410 TIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWIntyND--FH- 486
Cdd:cd07136 315 TILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCI---NDtiMHl 391
|
330 340 350
....*....|....*....|....*....|...
gi 50310159 487 --HCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07136 392 anPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
179-504 |
8.97e-57 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 195.52 E-value: 8.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 179 SYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVnIVSGfGKIVGEA 258
Cdd:cd07134 94 SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEG-DAEVAQA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 259 ITTHPkIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEE 338
Cdd:cd07134 172 LLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 339 SIYDDFLKEIKSASEAlkvgdpFDAETFQGAQTS-------QNQLDKILKYVEIGKNEGATLITGGErIGDKGYFVRPTI 411
Cdd:cd07134 251 SVKDAFVEHLKAEIEK------FYGKDAARKASPdlarivnDRHFDRLKGLLDDAVAKGAKVEFGGQ-FDAAQRYIAPTV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 412 FADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINtyndfhHCV-- 489
Cdd:cd07134 324 LTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN------DVVlh 397
|
330 340
....*....|....*....|.
gi 50310159 490 ------PFGGFNASGIGREMG 504
Cdd:cd07134 398 flnpnlPFGGVNNSGIGSYHG 418
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
86-517 |
4.24e-56 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 193.59 E-value: 4.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 86 EDVDAAVEAADKAFKSGvwsKVDPL-VRSQCLSKLADYIEKDLDTIASIESLDNGKA--------ISSAKGDVQLVVNYL 156
Cdd:cd07135 5 DEIDSIHSRLRATFRSG---KTKDLeYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPpfetllteVSGVKNDILHMLKNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 157 RSAAGyadkvDGRVIDTGSTHFSYTVR---EPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQ 233
Cdd:cd07135 82 KKWAK-----DEKVKDGPLAFMFGKPRirkEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 234 YIPKAgIPDGVVNIVSGfgkivGEAITT---HPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLK 310
Cdd:cd07135 157 LVPKY-LDPDAFQVVQG-----GVPETTallEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 311 SAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFqGAQTSQNQLDKILKYVEigkNEG 390
Cdd:cd07135 231 LAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDY-TRIVNPRHFNRLKSLLD---TTK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 391 ATLITGGERIGDKgYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSN 470
Cdd:cd07135 307 GKVVIGGEMDEAT-RFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILT 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 50310159 471 RLNAGTVwinTYND--FH---HCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07135 386 RTRSGGV---VINDtlIHvgvDNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
179-517 |
1.17e-55 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 194.09 E-value: 1.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 179 SYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAgIPDGVVNIVSGfGKIVGEA 258
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 259 ITTHPkIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEE 338
Cdd:PTZ00381 181 LLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 339 SIYDDFLKEIKsasEALKvgdpfdaeTFQGAQTS-QNQLDKIL------KYVEIGKNEGATLITGGErIGDKGYFVRPTI 411
Cdd:PTZ00381 260 SIKDKFIEALK---EAIK--------EFFGEDPKkSEDYSRIVnefhtkRLAELIKDHGGKVVYGGE-VDIENKYVAPTI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 412 FADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINtyndfhHCV-- 489
Cdd:PTZ00381 328 IVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN------DCVfh 401
|
330 340 350
....*....|....*....|....*....|....
gi 50310159 490 ------PFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:PTZ00381 402 llnpnlPFGGVGNSGMGAYHGKYGFDTFSHPKPV 435
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
179-517 |
2.85e-55 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 191.54 E-value: 2.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 179 SYTVREPLGVCGQIIPWNFPLLMwawKIAP---ALATGNTVVLKTAESTP-LSALyVSQYIPKAGIPDgVVNIVSGfGKI 254
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYL---ALGPliaALAAGNRVMIKPSEFTPrTSAL-LAELLAEYFDED-EVAVVTG-GAD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 255 VGEAITTHPkIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRL 334
Cdd:cd07133 169 VAAAFSSLP-FDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 335 YVEESIYDDFLKEIKSASEALkVGDPFDAETFqgaqTS---QNQLDKILKYVEIGKNEGATLIT---GGERIGDKGYFVr 408
Cdd:cd07133 248 LVPEDKLEEFVAAAKAAVAKM-YPTLADNPDY----TSiinERHYARLQGLLEDARAKGARVIElnpAGEDFAATRKLP- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 409 PTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVwinTYND--FH 486
Cdd:cd07133 322 PTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGV---TINDtlLH 398
|
330 340 350
....*....|....*....|....*....|....
gi 50310159 487 ---HCVPFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07133 399 vaqDDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
59-500 |
1.66e-54 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 198.27 E-value: 1.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 59 PSKQGKTFEVLSPSTEEEIT-HVYEGREEDVDAAVEAADKAfkSGVWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLD 137
Cdd:PRK11809 654 PVAAGEMSPVINPADPRDIVgYVREATPAEVEQALESAVNA--APIWFATPPAERAAILERAADLMEAQMQTLMGLLVRE 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 138 NGKAISSAKGDVQLVVNYLRSaagYADKVDGrvidtgstHFSYTVREPLG--VCgqIIPWNFPLLMWAWKIAPALATGNT 215
Cdd:PRK11809 732 AGKTFSNAIAEVREAVDFLRY---YAGQVRD--------DFDNDTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNS 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 216 VVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAGVNL----KKV 291
Cdd:PRK11809 799 VLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqgRPI 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 292 TL--ELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDP--------- 360
Cdd:PRK11809 879 PLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPdrlstdigp 958
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 361 -FDAETFQGaqtsqnqldkILKYVEIGKNEGATlITGGERIGD----KGYFVRPTIfadVE-ESMRIVKEEIFGPVVTVT 434
Cdd:PRK11809 959 vIDAEAKAN----------IERHIQAMRAKGRP-VFQAARENSedwqSGTFVPPTL---IElDSFDELKREVFGPVLHVV 1024
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50310159 435 KFK--TIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWINTyNDFHHCV---PFGGFNASGIG 500
Cdd:PRK11809 1025 RYNrnQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTG 1094
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
90-520 |
7.64e-45 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 163.55 E-value: 7.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 90 AAVEAADKAFKSGVWSKVDplVRSQCLSKLADYIEKDLDTIASIESLDNGKA--------ISSAKGDVQLVVNYLRS--- 158
Cdd:cd07132 2 EAVRRAREAFSSGKTRPLE--FRIQQLEALLRMLEENEDEIVEALAKDLRKPkfeavlseILLVKNEIKYAISNLPEwmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 159 ----AAGYADKVDGRVIdtgsthfsytVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQY 234
Cdd:cd07132 80 pepvKKNLATLLDDVYI----------YKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 235 IPKAGIPDgVVNIVSGfgkivGEAITT---HPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKS 311
Cdd:cd07132 150 IPKYLDKE-CYPVVLG-----GVEETTellKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 312 AVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFqGAQTSQNQLDKILKYVEIGKnega 391
Cdd:cd07132 224 AARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDY-GRIINDRHFQRLKKLLSGGK---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 392 tLITGGErIGDKGYFVRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNR 471
Cdd:cd07132 299 -VAIGGQ-TDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSN 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 50310159 472 LNAGTVwinTYND--FH---HCVPFGGFNASGIGREMGSEALDNYTQVKAVRVK 520
Cdd:cd07132 377 TSSGGV---CVNDtiMHytlDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
182-517 |
4.24e-44 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 161.42 E-value: 4.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 182 VREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAgIPDGVVNIVSGfGKIVGEAITT 261
Cdd:cd07137 98 VSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 262 HpKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIY-YNSGEVCCAGSRLYVEESI 340
Cdd:cd07137 176 Q-KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESF 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 341 YDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQ--LDKILKYVEIgkneGATLITGGERIGDKGYfVRPTIFADVEES 418
Cdd:cd07137 255 APTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFqrLSRLLDDPSV----ADKIVHGGERDEKNLY-IEPTILLDPPLD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 419 MRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVwinTYND--FH---HCVPFGG 493
Cdd:cd07137 330 SSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGV---TFNDtvVQyaiDTLPFGG 406
|
330 340
....*....|....*....|....
gi 50310159 494 FNASGIGREMGSEALDNYTQVKAV 517
Cdd:cd07137 407 VGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
182-517 |
2.62e-32 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 129.46 E-value: 2.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 182 VREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAgIPDGVVNIVSGfGKIVGEAITT 261
Cdd:PLN02203 105 VPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLLQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 262 HpKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVV---FADANLKSAVqNSLLGIYYNS--GEVCCAGSRLYV 336
Cdd:PLN02203 183 H-KWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAV-NRIVGGKWGScaGQACIAIDYVLV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 337 EESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQN--QLDKILKYVEIgkneGATLITGGErIGDKGYFVRPTIFAD 414
Cdd:PLN02203 261 EERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHfqRLSNLLKDPRV----AASIVHGGS-IDEKKLFIEPTILLN 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 415 VEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVwinTYNDF---HHC--V 489
Cdd:PLN02203 336 PPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDAiiqYACdsL 412
|
330 340
....*....|....*....|....*...
gi 50310159 490 PFGGFNASGIGREMGSEALDNYTQVKAV 517
Cdd:PLN02203 413 PFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
88-508 |
6.70e-31 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 124.66 E-value: 6.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 88 VDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGK----AISSAKGDVQLVvnyLRSAAGYA 163
Cdd:cd07084 1 PERALLAADISTKA--ARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKgwmfAENICGDQVQLR---ARAFVIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 164 DKVDGRVIDTGSTHFSYT---VREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGI 240
Cdd:cd07084 76 YRIPHEPGNHLGQGLKQQshgYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 241 -PDGVVNIVSGFGKiVGEAITTHPKIKKVAFTGSTATGRHIYQNAgvNLKKVTLELGGKSPNVVFADANLKSAV-QNSLL 318
Cdd:cd07084 156 lPPEDVTLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQAVDYVaWQCVQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 319 GIYYNSGEVCCAGSRLYVEESIY-DDFLKEIKSASEALKVGDpfdaeTFQGAQTSQNQLDKIlkyVEIGKNEGATLITGG 397
Cdd:cd07084 233 DMTACSGQKCTAQSMLFVPENWSkTPLVEKLKALLARRKLED-----LLLGPVQTFTTLAMI---AHMENLLGSVLLFSG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 398 ERIGDK------GYFVRPTIFADVEESMR---IVKEEIFGPVVTVTKFK-----TIDELIEKANDSeygLAAGIHTSN-- 461
Cdd:cd07084 305 KELKNHsipsiyGACVASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKkdqlaLVLELLERMHGS---LTAAIYSNDpi 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 50310159 462 ------INTAIQ---VSNRLNAGTVWINTYNdfhhcvpFGGFNASGIGREMG-SEAL 508
Cdd:cd07084 382 flqeliGNLWVAgrtYAILRGRTGVAPNQNH-------GGGPAADPRGAGIGgPEAI 431
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
182-517 |
4.24e-30 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 123.23 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 182 VREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLKTAESTPLSALYVSQYIPKAgIPDGVVNIVSGfgKIVGEAITT 261
Cdd:PLN02174 109 VSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEG--AVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 262 HPKIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIY-YNSGEVCCAGSRLYVEESI 340
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEY 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 341 YDDFLKEIKSASEALKVGDPFDAETFQGAQTSqNQLDKILKYVEiGKNEGATLITGGERiGDKGYFVRPTIFADVEESMR 420
Cdd:PLN02174 266 APKVIDAMKKELETFYGKNPMESKDMSRIVNS-THFDRLSKLLD-EKEVSDKIVYGGEK-DRENLKIAPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 421 IVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQVSNRLNAGTVWIN--TYNDFHHCVPFGGFNASG 498
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiAVHLALHTLPFGGVGESG 422
|
330
....*....|....*....
gi 50310159 499 IGREMGSEALDNYTQVKAV 517
Cdd:PLN02174 423 MGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
88-460 |
7.15e-27 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 113.02 E-value: 7.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 88 VDAAVEAADKAFKSgvWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAKGDVQLVVNYLRSAAGYADK-- 165
Cdd:cd07129 1 VDAAAAAAAAAFES--YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 166 VDGRVIDTGSTHFSYTVRE-------PLGVCGQIIPWNFPLlmwAWKI-----APALATGNTVVLK-------TAEstpL 226
Cdd:cd07129 79 WLDARIDPADPDRQPLPRPdlrrmlvPLGPVAVFGASNFPL---AFSVaggdtASALAAGCPVVVKahpahpgTSE---L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 227 SALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQ--NAGVNLKKVTLELGGKSPNVVF 304
Cdd:cd07129 153 VARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDaaAARPEPIPFYAELGSVNPVFIL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 305 -------ADANLKSAVQNSLLGiyynSGEVC-CAGSRLYVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQL 376
Cdd:cd07129 233 pgalaerGEAIAQGFVGSLTLG----AGQFCtNPGLVLVPAGPAGDAFIAALAEALAAAPAQTMLTPGIAEAYRQGVEAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 377 dkilkyveiGKNEGATLITGGERiGDKGYFVRPTIFA-DVEESMR--IVKEEIFGPVVTVTKFKTIDELIEKANDSEYGL 453
Cdd:cd07129 309 ---------AAAPGVRVLAGGAA-AEGGNQAAPTLFKvDAAAFLAdpALQEEVFGPASLVVRYDDAAELLAVAEALEGQL 378
|
....*..
gi 50310159 454 AAGIHTS 460
Cdd:cd07129 379 TATIHGE 385
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
187-468 |
1.40e-18 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 88.48 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 187 GVCGQIIPWNFPllmwAW----KIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGI-PDGVVNIVSGFGKIVGEAITT 261
Cdd:cd07128 146 GVAVHINAFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHLGE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 262 HpkiKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPN--VVFADANLKSA-----VQNSLLGIYYNSGEVCCAGSRL 334
Cdd:cd07128 222 Q---DVVAFTGSAATAAKLRAHPNIVARSIRFNAEADSLNaaILGPDATPGTPefdlfVKEVAREMTVKAGQKCTAIRRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 335 YVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGKNEGATLITGGERI------GDKGYFVR 408
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFevvgadAEKGAFFP 378
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50310159 409 PTIF--ADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSNINTAIQV 468
Cdd:cd07128 379 PTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFAREL 440
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
187-461 |
3.52e-18 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 87.45 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 187 GVCGQIIPWNFPllmwAW----KIAPALATGNTVVLKTAESTPLSALYVSQYIPKAGI-PDGVVNIVSGFGKIVGEAITT 261
Cdd:PRK11903 150 GVALFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 262 hpkIKKVAFTGSTATGRHIYQNAGVNLKKVTLELGGKSPN--VVFADANLKSAVQNSLLG-----IYYNSGEVCCAGSRL 334
Cdd:PRK11903 226 ---FDVVSFTGSAETAAVLRSHPAVVQRSVRVNVEADSLNsaLLGPDAAPGSEAFDLFVKevvreMTVKSGQKCTAIRRI 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 335 YVEESIYDDFLKEIKSASEALKVGDPFDAETFQGAQTSQNQLDKILKYVEIGKnEGATLITGGERIG------DKGYFVR 408
Cdd:PRK11903 303 FVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALR-AQAEVLFDGGGFAlvdadpAVAACVG 381
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 50310159 409 PTIF--ADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGLAAGIHTSN 461
Cdd:PRK11903 382 PTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
189-486 |
4.15e-14 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 74.82 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 189 CGQIIPWN-FPLLMwawkiaPALATGNTVVLKTAESTPLS-ALYVS---QYIPKAGI-PDGVVNIVSGFGKIVGEAITTH 262
Cdd:cd07127 202 CSTFPTWNgYPGLF------ASLATGNPVIVKPHPAAILPlAITVQvarEVLAEAGFdPNLVTLAADTPEEPIAQTLATR 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 263 PKIKKVAFTGSTATGRHIYQNAGvnLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNSGEVCCAGSRLYV------ 336
Cdd:cd07127 276 PEVRIIDFTGSNAFGDWLEANAR--QAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgiq 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 337 ---EESIYDDFLKEIKSASEALkVGDPFDAETFQGAQTSQNQLDKILKYVEIGKnegatLITGGERIGDKGY---FVR-P 409
Cdd:cd07127 354 tddGRKSFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIAEARQLGE-----VLLASEAVAHPEFpdaRVRtP 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 410 TIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDS--EYG-LAAGIHTSN-----------INTAIQVSNRLNAG 475
Cdd:cd07127 428 LLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESvrEHGaMTVGVYSTDpevvervqeaaLDAGVALSINLTGG 507
|
330
....*....|....
gi 50310159 476 tVWIN---TYNDFH 486
Cdd:cd07127 508 -VFVNqsaAFSDFH 520
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
67-476 |
8.97e-12 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 67.14 E-value: 8.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 67 EVLSPSTEEEITHVYEGREEDVDAAVEAADKAFKSG----------------VWSKVDPLVRsqcLSKLADYIEKDLDTI 130
Cdd:cd07126 15 TLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGlhnplknperyllygdVSHRVAHELR---KPEVEDFFARLIQRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 131 ASiesldngKAISSAKGDVQLVVNYLRSAAGYADKVDGRVIDTGSTHF---SYTVREPLGVCGQIIPWNFPLLMWAWKIA 207
Cdd:cd07126 92 AP-------KSDAQALGEVVVTRKFLENFAGDQVRFLARSFNVPGDHQgqqSSGYRWPYGPVAIITPFNFPLEIPALQLM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 208 PALATGNTVVLKTAESTPLSALYVSQYIPKAGIPDGVVNIVSGFGKIVGEAIT-THPKIkkVAFTGSTATGRHIyqnAGV 286
Cdd:cd07126 165 GALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANPRM--TLFTGSSKVAERL---ALE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 287 NLKKVTLELGG-----KSPNVVFADANLKSAVQNSllgiYYNSGEVCCAGSRLYVEESIYD-DFLKEIKSASEALKVGD- 359
Cdd:cd07126 240 LHGKVKLEDAGfdwkiLGPDVSDVDYVAWQCDQDA----YACSGQKCSAQSILFAHENWVQaGILDKLKALAEQRKLEDl 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 360 ---PFDAETfqgAQTSQNQLDKILKYveigknEGATLITGGERIGDKGY-----FVRPT-IF-----ADVEESMRIVKEE 425
Cdd:cd07126 316 tigPVLTWT---TERILDHVDKLLAI------PGAKVLFGGKPLTNHSIpsiygAYEPTaVFvpleeIAIEENFELVTTE 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 50310159 426 IFGPVVTVTKFK--TIDELIEKANDSEYGLAAGIHTSNINTAIQV-SNRLNAGT 476
Cdd:cd07126 387 VFGPFQVVTEYKdeQLPLVLEALERMHAHLTAAVVSNDIRFLQEVlANTVNGTT 440
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
83-470 |
7.58e-11 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 64.18 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 83 GREEDVDAAVEAADKAFKsgVWSKVDPLVRSQCLSKLADYIEKDLDTIASIESLDNGKaissakGDVQLVVNYLRSAA-- 160
Cdd:cd07121 1 GVFATVDDAVAAAKAAQK--QYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGM------GRVEDKIAKNHLAAek 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 161 --GYAD-KVDGRVIDTGSTHFSYTvrePLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVLktaeSTPLSALYVSQY--- 234
Cdd:cd07121 73 tpGTEDlTTTAWSGDNGLTLVEYA---PFGVIGAITPSTNPTETIINNSISMLAAGNAVVF----NPHPGAKKVSAYave 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 235 -----IPKAGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAgvnlKKVTLELGGKSPNVVFADANL 309
Cdd:cd07121 146 linkaIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSG----KKAIGAGAGNPPVVVDETADI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 310 KSAVQNSLLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASeALKVGDPfdaetfqgaQTSQnQLDKILKYVE----- 384
Cdd:cd07121 222 EKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQRNG-AYVLNDE---------QAEQ-LLEVVLLTNKgatpn 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 385 ---IGKNEGATLITGGERIGDKgyfvRPTIFADVEESMRIVKEEIFGPVVTVTKFKTIDELIEKANDSEYGL--AAGIHT 459
Cdd:cd07121 291 kkwVGKDASKILKAAGIEVPAD----IRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHS 366
|
410 420
....*....|....*....|.
gi 50310159 460 SNI----------NTAIQVSN 470
Cdd:cd07121 367 KNVenltkmaramQTTIFVKN 387
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
109-505 |
1.12e-10 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 63.40 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 109 PLVRSQCLSKLADYIEKDLDTIASIESLDNGKAISSAK-------GDVQLVVNYLRSAAGYADKVDGRVID--TGSTHFS 179
Cdd:cd07077 15 DEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIanwiammGCSESKLYKNIDTERGITASVGHIQDvlLPDNGET 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 180 YTVREPLGVCGQIIPWNFPLLMwAWKIAPALATGNTVVLKTAESTPLS--ALYVS-QYIPKAGIPDGVVNIVSGFGKIVG 256
Cdd:cd07077 95 YVRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTnrALALLfQAADAAHGPKILVLYVPHPSDELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 257 EAITTHPKIKKVAFTGSTATGRHIYQNAgvNLKKVTLELGGKSPNVVFADANLKSAVQNSLLGIYYNsGEVCCAGSRLYV 336
Cdd:cd07077 174 EELLSHPKIDLIVATGGRDAVDAAVKHS--PHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 337 EESIYDDFLKEIKsasealkvgdpfdaetfqgaqtsqnqldkiLKYVEIGKNEGA-TLITGGERIGDKGYFVRptifadv 415
Cdd:cd07077 251 VDDVLDPLYEEFK------------------------------LKLVVEGLKVPQeTKPLSKETTPSFDDEAL------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 416 EESMRIVkeeifgPVVTVTKFKTIDELIEKANDSE-YGLAAGIHTSNINTAIQVSNRLNAGTVWINTYNDFHHCVPFGGF 494
Cdd:cd07077 294 ESMTPLE------CQFRVLDVISAVENAWMIIESGgGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKG 367
|
410
....*....|.
gi 50310159 495 NASGIGREMGS 505
Cdd:cd07077 368 VERIVTSGMNN 378
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
162-474 |
4.35e-10 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 61.90 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 162 YADKVDGRVIDTGSTHFSYTVREPLGVCGQIIPWNFPLLMWAWKIAPALATGNTVVL----KTAESTPLSALYVSQYIPK 237
Cdd:cd07081 72 YKDEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFsphpRAKKVTQRAATLLLQAAVA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 238 AGIPDGVVNIVSGFGKIVGEAITTHPKIKKVAFTGSTATGRHIYQNAgvnlkKVTLELG-GKSPNVVFADANLKSAVQNS 316
Cdd:cd07081 152 AGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSG-----KPAIGVGaGNTPVVIDETADIKRAVQSI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 317 LLGIYYNSGEVCCAGSRLYVEESIYDDFLKEIKSASealkvgdpfdAETFQGAQTSQNQlDKILKYVE-----IGKNEGA 391
Cdd:cd07081 227 VKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQG----------AYKLTAEELQQVQ-PVILKNGDvnrdiVGQDAYK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50310159 392 TLITGGERIGD--KGYFVRPTIFADVEESMrivkEEIFGPVVTVTKFKTIDELIEKA----NDSEYGLAAGIHTSNINTA 465
Cdd:cd07081 296 IAAAAGLKVPQetRILIGEVTSLAEHEPFA----HEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAI 371
|
....*....
gi 50310159 466 IQVSNRLNA 474
Cdd:cd07081 372 ENMNQFANA 380
|
|
| |
