|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
32-474 |
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: 910.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 32 NLEIKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLAD 111
Cdd:cd07141 1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 112 LVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLL 191
Cdd:cd07141 81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 192 MFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKE--------------------------------------VGKLI 233
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEagfppgvvnvvpgygptagaaisshpdidkvaftgsteVGKLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 234 QEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGS 313
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 314 PFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTM 393
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 394 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
.
gi 25777726 474 K 474
Cdd:cd07141 481 K 481
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
38-473 |
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: 777.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 38 TKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKLADLVERDR 117
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 118 AVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKI 197
Cdd:cd07091 83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 198 APALCCGNTVVIKPAEQTPLSALYMGALIKE--------------------------------------VGKLIQEAAGR 239
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEagfppgvvnivpgfgptagaaisshmdvdkiaftgstaVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 240 SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTT 319
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 320 EQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIER 399
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25777726 400 ANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07091 403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
35-471 |
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: 650.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 35 IKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKLADLVE 114
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGP-WPRMTGYERSRILLRFADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 115 RDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFA 194
Cdd:cd07142 80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 195 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKE--------------------------------------VGKLIQEA 236
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEaglpdgvlnivtgfgptagaaiashmdvdkvaftgsteVGKIIMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 237 AGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 316
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 317 PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 396
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25777726 397 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
30-479 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 632.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 30 TPNLEIKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKL 109
Cdd:PLN02466 50 TPPVQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGP-WPKMTAYERSRILLRF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 110 ADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFP 189
Cdd:PLN02466 129 ADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 190 LLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKE--------------------------------------VGK 231
Cdd:PLN02466 209 LLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEaglppgvlnvvsgfgptagaalashmdvdklaftgstdTGK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 232 LIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVV 311
Cdd:PLN02466 289 IVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 312 GSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFK 391
Cdd:PLN02466 369 GDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 392 TMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:PLN02466 449 DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
....*...
gi 25777726 472 TVkiPQKN 479
Cdd:PLN02466 529 VT--PLKN 534
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
38-475 |
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: 628.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 38 TKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgSVWRR-MDASERGRLLDKLADLVERD 116
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 117 RAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWK 196
Cdd:cd07143 85 LDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 197 IAPALCCGNTVVIKPAEQTPLSALYMGALIKE--------------------------------------VGKLIQEAAG 238
Cdd:cd07143 165 IAPALAAGNTIVLKPSELTPLSALYMTKLIPEagfppgvinvvsgygrtcgnaisshmdidkvaftgstlVGRKVMEAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 239 RSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 318
Cdd:cd07143 245 KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 319 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIE 398
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25777726 399 RANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 475
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
36-474 |
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: 611.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 36 KYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVER 115
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFP---AWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 116 DRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFA 194
Cdd:COG1012 81 RREELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 195 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKE--------------------------------------VGKLIQEA 236
Cdd:COG1012 160 WKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEaglpagvlnvvtgdgsevgaalvahpdvdkisftgstaVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 237 AGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 316
Cdd:COG1012 240 AAE-NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 317 PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGL-GRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 395
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 396 VIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNA-LNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVK 474
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
46-471 |
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: 607.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 46 WQNSESGRvFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMES 125
Cdd:pfam00171 1 WVDSESET-IEVINPATGEVIATVPAATAEDVDAAIAAARAAFP---AWRKTPAAERAAILRKAADLLEERKDELAELET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 126 LNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGN 205
Cdd:pfam00171 77 LENGKPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 206 TVVIKPAEQTPLSALYMGALIKE--------------------------------------VGKLIQEAAGRsNLKRVTL 247
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEaglpagvlnvvtgsgaevgealvehpdvrkvsftgstaVGRHIAEAAAQ-NLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 248 ELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDK 327
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 328 KQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGL 407
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25777726 408 VAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGlPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
38-473 |
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: 585.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 38 TKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgSVWRRMDASERGRLLDKLADLVERDR 117
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 118 AVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKI 197
Cdd:cd07144 86 DLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 198 APALCCGNTVVIKPAEQTPLSALYMGALIKE--------------------------------------VGKLIQEAAGr 239
Cdd:cd07144 166 APALAAGNTVVIKPAENTPLSLLYFANLVKEagfppgvvniipgygavagsalaehpdvdkiaftgstaTGRLVMKAAA- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 240 SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRR-VVGSPFDPT 318
Cdd:cd07144 245 QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 319 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR---KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 395
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEE 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25777726 396 VIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07144 405 AIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
41-471 |
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: 573.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPA 200
Cdd:cd07119 80 ARLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 201 LCCGNTVVIKPAEQTPLSALYMGALIKEVG---------------------------------------KLIQEAAGrsN 241
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGlpagvvnlvtgsgatvgaelaespdvdlvsftggtatgrSIMRAAAG--N 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 242 LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 321
Cdd:cd07119 237 VKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 322 GPQIDKKQYNKILELIQSGVAEGAKLECGGKGLG----RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVI 397
Cdd:cd07119 317 GPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25777726 398 ERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:cd07119 397 RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
34-476 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 566.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 34 EIKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKLADLV 113
Cdd:PLN02766 17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGP-WPRMSGFERGRIMMKFADLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 114 ERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMF 193
Cdd:PLN02766 96 EEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 194 AWKIAPALCCGNTVVIKPAEQTPLSALYMGALIK--------------------------------------EVGKLIQE 235
Cdd:PLN02766 176 FMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKlagvpdgvinvvtgfgptagaaiashmdvdkvsftgstEVGRKIMQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 236 AAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 315
Cdd:PLN02766 256 AAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 316 DPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 395
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 396 VIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 475
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
|
.
gi 25777726 476 P 476
Cdd:PLN02766 496 Y 496
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
78-473 |
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: 547.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 78 DKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKI 157
Cdd:cd07078 1 DAAVAAARAAFK---AWAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 158 HGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKE-------- 228
Cdd:cd07078 77 HGEVIPsPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEaglppgvl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 229 ------------------------------VGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQ 278
Cdd:cd07078 157 nvvtgdgdevgaalashprvdkisftgstaVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 279 GQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR-K 357
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 358 GFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYN 437
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 25777726 438 A-LNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07078 396 VgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
52-471 |
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: 543.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 52 GRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKP 131
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESG-VWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 132 FLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07112 80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 212 AEQTPLSALYMGALIKE--------------------------------------VGKLIQEAAGRSNLKRVTLELGGKS 253
Cdd:cd07112 160 AEQSPLTALRLAELALEaglpagvlnvvpgfghtagealglhmdvdalaftgsteVGRRFLEYSGQSNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 254 PNIIFADA-DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNK 332
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 333 ILELIQSGVAEGAKLECGGK--GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAA 410
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKrvLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777726 411 VFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
57-473 |
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: 532.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPF---- 132
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIretr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 133 LQAFYVdlqgvIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07114 80 AQVRYL-----AEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 212 AEQTPLSALYMGALIKE--------------------------------------VGKLIQEAAGRsNLKRVTLELGGKS 253
Cdd:cd07114 155 SEHTPASTLELAKLAEEagfppgvvnvvtgfgpetgealvehplvakiaftggteTGRHIARAAAE-NLAPVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 254 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 333
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 334 LELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVA 409
Cdd:cd07114 314 ERYVARAREEGARVLTGGErpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25777726 410 AVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07114 394 GIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
59-475 |
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: 531.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 59 NPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYV 138
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 139 DLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLS 218
Cdd:cd07115 80 DVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 219 ALYMGALIKEVG---------------------------------------KLIQEAAGrsNLKRVTLELGGKSPNIIFA 259
Cdd:cd07115 160 ALRIAELMAEAGfpagvlnvvtgfgevagaalvehpdvdkitftgstavgrKIMQGAAG--NLKRVSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 260 DADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQS 339
Cdd:cd07115 238 DADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 340 GVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKA 419
Cdd:cd07115 318 GREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 25777726 420 LTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 475
Cdd:cd07115 398 HRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
57-473 |
1.39e-180 |
|
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: 513.27 E-value: 1.39e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP---GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 137 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 216
Cdd:cd07093 78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 217 LSALYMGALIKEVG--------------------------------------KLIQEAAGRsNLKRVTLELGGKSPNIIF 258
Cdd:cd07093 158 LTAWLLAELANEAGlppgvvnvvhgfgpeagaalvahpdvdlisftgetatgRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 259 ADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQ 338
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 339 SGVAEGAKLECGGKGLG----RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTN 414
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 25777726 415 DINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
38-474 |
5.20e-180 |
|
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: 513.20 E-value: 5.20e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 38 TKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRMDASERGRLLDKLADLVERDR 117
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 118 AVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVD----GDYFTFTRHEPIGVCGQIIPWNFPLLMF 193
Cdd:cd07140 85 EELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 194 AWKIAPALCCGNTVVIKPAEQTPLSALYM--------------------GALI------------------KEVGKLIQE 235
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFaeltvkagfpkgvinilpgsGSLVgqrlsdhpdvrklgftgsTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 236 AAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 315
Cdd:cd07140 245 SCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 316 DPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT--M 393
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 394 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07140 405 DGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
.
gi 25777726 474 K 474
Cdd:cd07140 485 E 485
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
39-473 |
1.11e-173 |
|
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: 496.87 E-value: 1.11e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 39 KIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRA 118
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 119 VLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIA 198
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 199 PALCCGNTVVIKPAEQTPLSALYMGALIK-------------------------------------EVGKLIQEAAGRsN 241
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGdllpkgvvnvvtgfgseagkplashpriaklaftgstTVGRLIMQYAAE-N 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 242 LKRVTLELGGKSPNIIFADA-----DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 316
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 317 PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT 392
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGErltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 393 MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 472
Cdd:cd07559 398 EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNIL 477
|
.
gi 25777726 473 V 473
Cdd:cd07559 478 V 478
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
57-473 |
1.82e-168 |
|
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: 482.57 E-value: 1.82e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 136
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK---EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 137 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 216
Cdd:cd07090 77 RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 217 LSALYMGALIKE-------------------------------------VGKLIQEAAGrSNLKRVTLELGGKSPNIIFA 259
Cdd:cd07090 157 LTALLLAEILTEaglpdgvfnvvqgggetgqllcehpdvakvsftgsvpTGKKVMSAAA-KGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 260 DADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQS 339
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 340 GVAEGAKLECGGKGLG-----RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTN 414
Cdd:cd07090 316 AKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 25777726 415 DINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
41-473 |
1.05e-167 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 481.69 E-value: 1.05e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLV-ERDRAv 119
Cdd:PRK13252 10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK---IWAAMTAMERSRILRRAVDILrERNDE- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 120 LATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 199
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 200 ALCCGNTVVIKPAEQTPLSALYMGALIKE----------------VGKLIQE--------------------AAGRSNLK 243
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEaglpdgvfnvvqgdgrVGAWLTEhpdiakvsftggvptgkkvmAAAAASLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 244 RVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGP 323
Cdd:PRK13252 246 EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 324 QIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIER 399
Cdd:PRK13252 326 LVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIAR 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25777726 400 ANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:PRK13252 406 ANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
57-473 |
6.77e-165 |
|
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: 473.07 E-value: 6.77e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 136
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFK---TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 137 YVDLQGVIKTFRYYAGWADKIHGMTIPV-DGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQT 215
Cdd:cd07103 77 RGEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 216 PLSALYMGALIKE--------------------------------------VGK-LIQEAAgrSNLKRVTLELGGKSPNI 256
Cdd:cd07103 157 PLSALALAELAEEaglpagvlnvvtgspaeigealcasprvrkisftgstaVGKlLMAQAA--DTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 257 IFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILEL 336
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 337 IQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDI 416
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 25777726 417 NKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07103 395 ARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
41-469 |
1.04e-163 |
|
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: 470.83 E-value: 1.04e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQG---EWAAMSPMERGRILRRAADLIRERNEEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPA 200
Cdd:TIGR01804 78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 201 LCCGNTVVIKPAEQTPLSALYMGALIKEVG--------------------------------------KLIQEAAGrSNL 242
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGlpkgvfnvvqgdgaevgpllvnhpdvakvsftggvptgKKIMAAAA-GHL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 243 KRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQG 322
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 323 PQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIE 398
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777726 399 RANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVK 469
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
39-473 |
2.73e-163 |
|
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: 470.01 E-value: 2.73e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 39 KIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRA 118
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 119 VLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIA 198
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 199 PALCCGNTVVIKPAEQTPLSALYMGALIK-------------------------------------EVGKLIQEAAGRsN 241
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQdvlpkgvvnivtgkgsksgeyllnhpgldklaftgstEVGRDVAIAAAK-K 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 242 LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQ 321
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 322 GPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVI 397
Cdd:cd07117 318 GAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25777726 398 ERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07117 398 DMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
57-473 |
5.43e-162 |
|
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: 465.94 E-value: 5.43e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 136
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 137 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 216
Cdd:cd07109 78 RADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 217 LSALYMGALIKE--------------------------------------VGKLIQEAAGRsNLKRVTLELGGKSPNIIF 258
Cdd:cd07109 158 LTALRLAELAEEaglpagalnvvtglgaeagaalvahpgvdhisftgsveTGIAVMRAAAE-NVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 259 ADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVG-SPFDPttEQGPQIDKKQYNKILELI 337
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGpGLEDP--DLGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 338 QSGVAEGAKLECGG---KGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTN 414
Cdd:cd07109 315 ARARARGARIVAGGriaEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 415 DINKALTVSSAMQAGTVWINCYNALNA-QSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07109 395 DGDRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
40-472 |
2.97e-161 |
|
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: 464.67 E-value: 2.97e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 40 IFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAV 119
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP---AWSATSVEERAALLERIAEAYEARADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 120 LA---TMESlngGKPFLQAFYVDLQGVIKTFRYYAGWADKIHgMTIPVDGdyfTFTRHEPIGVCGQIIPWNFPLLMFAWK 196
Cdd:cd07138 78 LAqaiTLEM---GAPITLARAAQVGLGIGHLRAAADALKDFE-FEERRGN---SLVVREPIGVCGLITPWNWPLNQIVLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 197 IAPALCCGNTVVIKPAEQTPLSALYMGALIKE--------------------------------------VGKLIQEAAG 238
Cdd:cd07138 151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEaglpagvfnlvngdgpvvgealsahpdvdmvsftgstrAGKRVAEAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 239 RSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 318
Cdd:cd07138 231 DT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 319 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR---KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 395
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEgleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25777726 396 VIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 472
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
57-473 |
2.08e-157 |
|
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: 454.09 E-value: 2.08e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFP---SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 137 YVDLQGVIKTFRYYAGWADKIHGmtiPVDGDYF----TFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPA 212
Cdd:cd07092 78 DDELPGAVDNFRFFAGAARTLEG---PAAGEYLpghtSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 213 EQTPLSALYMGALIKEV-------------------------------------GKLIQEAAGRsNLKRVTLELGGKSPN 255
Cdd:cd07092 155 ETTPLTTLLLAELAAEVlppgvvnvvcgggasagdalvahprvrmvsltgsvrtGKKVARAAAD-TLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 256 IIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILE 335
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 336 LIqSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND 415
Cdd:cd07092 314 FV-ERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 25777726 416 INKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
60-473 |
1.06e-156 |
|
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: 452.56 E-value: 1.06e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 60 PATGEQVCEVQEADKADIDKAVQAARLAFSLGSvWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVD 139
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGP-WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 140 LQGVIKTFRYYAGWADKIHGMTIPVDG-DYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLS 218
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 219 ALYMGALIKE--------------------------------------VGKLIQEAAGRsNLKRVTLELGGKSPNIIFAD 260
Cdd:cd07118 162 TLMLAELLIEaglpagvvnivtgygatvgqamtehpdvdmvsftgstrVGKAIAAAAAR-NLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 261 ADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSG 340
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 341 VAEGAKLECGGKGL-GRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKA 419
Cdd:cd07118 321 RAEGATLLLGGERLaSAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 25777726 420 LTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
38-475 |
1.26e-156 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 453.21 E-value: 1.26e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 38 TKIFINNEWQNSEsGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDR 117
Cdd:PRK13473 3 TKLLINGELVAGE-GEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP---EWSQTTPKERAEALLKLADAIEENA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 118 AVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGmtiPVDGDY---FT-FTRHEPIGVCGQIIPWNFPLLMF 193
Cdd:PRK13473 79 DEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEG---KAAGEYlegHTsMIRRDPVGVVASIAPWNYPLMMA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 194 AWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKE-------------------------------------VGKLIQEA 236
Cdd:PRK13473 156 AWKLAPALAAGNTVVLKPSEITPLTALKLAELAADilppgvlnvvtgrgatvgdalvghpkvrmvsltgsiaTGKHVLSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 237 AGRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 316
Cdd:PRK13473 236 AADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 317 PTTEQGPQIDKKQYNKILELIQSGVAEG-AKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 395
Cdd:PRK13473 315 EDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 396 VIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 475
Cdd:PRK13473 395 AVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKH 474
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
57-472 |
4.66e-153 |
|
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: 443.33 E-value: 4.66e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP---RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 137 YvDLQGVIKTFRYYAGWADKIH---GMTIPVDGDYFT-FTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPA 212
Cdd:cd07110 78 W-DVDDVAGCFEYYADLAEQLDakaERAVPLPSEDFKaRVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 213 EQTPLSALYMGALIKE--------------------------------------VGKLIQEAAGRsNLKRVTLELGGKSP 254
Cdd:cd07110 157 ELTSLTELELAEIAAEaglppgvlnvvtgtgdeagaplaahpgidkisftgstaTGSQVMQAAAQ-DIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 255 NIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKIL 334
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 335 ELIQSGVAEGAKLECGGK--GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVF 412
Cdd:cd07110 316 SFIARGKEEGARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 413 TNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 472
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
41-471 |
2.64e-148 |
|
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: 431.67 E-value: 2.64e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQNSESGRvfPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAV 119
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 120 LATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIA 198
Cdd:cd07097 79 LARLLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 199 PALCCGNTVVIKPAEQTPLSA------------------LYMG-------ALIK-------------EVGKLIQEAAGrS 240
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAwalveileeaglpagvfnLVMGsgsevgqALVEhpdvdavsftgstAVGRRIAAAAA-A 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 241 NLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTE 320
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 321 QGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR--KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIE 398
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRpdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25777726 399 RANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNA-LNAQSPFGGFKMSGNG-REMGEFGLREYSEVKTV 471
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
57-473 |
6.88e-147 |
|
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: 427.33 E-value: 6.88e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 136
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 137 YVDLQGVIKTFRYYAGwadkihgMTIPV-----DGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07106 77 QFEVGGAVAWLRYTAS-------LDLPDeviedDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 212 AEQTPLSALYMGALIKEV------------------------------------GKLIQEAAGrSNLKRVTLELGGKSPN 255
Cdd:cd07106 150 SPFTPLCTLKLGELAQEVlppgvlnvvsggdelgpaltshpdirkisftgstatGKKVMASAA-KTLKRVTLELGGNDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 256 IIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILE 335
Cdd:cd07106 229 IVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 336 LIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND 415
Cdd:cd07106 309 LVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSD 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 25777726 416 INKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07106 389 LERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
41-467 |
1.05e-146 |
|
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: 427.97 E-value: 1.05e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIhgmtipvdgDYfTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPA 200
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLL---------DT-ELAGWKPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 201 LCCGNTVVIKPAEQTPLSALYMGALIKE-------------------------------------VGKLIQEA-AGRSnl 242
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEaglppgvlnivtgngsfgsalanhpgvdkvaftgsteVGRALRRAtAGTG-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 243 KRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQG 322
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 323 PQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANN 402
Cdd:cd07111 330 AIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANN 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25777726 403 SDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSE 467
Cdd:cd07111 410 TPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
57-471 |
1.90e-146 |
|
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: 426.66 E-value: 1.90e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRrMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 137 YVDLQGVIKTFRYYAGWADKIHG-MTIPVDGDYFTFT----RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07089 79 AMQVDGPIGHLRYFADLADSFPWeFDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 212 AEQTPLSALYMGALIKE--------------------------------------VGKLIQEAAGRsNLKRVTLELGGKS 253
Cdd:cd07089 159 APDTPLSALLLGEIIAEtdlpagvvnvvtgsdnavgealttdprvdmvsftgstaVGRRIMAQAAA-TLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 254 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 333
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 334 LELIQSGVAEGAKLECGGK---GLGrKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAA 410
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGrpaGLD-KGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777726 411 VFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:cd07089 397 VWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
82-473 |
3.15e-143 |
|
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: 415.09 E-value: 3.15e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 82 QAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKIHGMT 161
Cdd:cd06534 1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 162 IP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKE------------ 228
Cdd:cd06534 77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEaglppgvvnvvp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 229 --------------------------VGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCC 282
Cdd:cd06534 157 gggdevgaallshprvdkisftgstaVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 283 TAGSRIFVEESIYEEFVRRSVerakrrvvgspfdptteqgpqidkkqynkileliqsgvaegaklecggkglgrkgffie 362
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 363 pTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALN-A 441
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVgP 335
|
410 420 430
....*....|....*....|....*....|..
gi 25777726 442 QSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
41-471 |
3.13e-142 |
|
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: 416.28 E-value: 3.13e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA---WERLPAIERAAYLRKLADLIRENADEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFT-FTRHEPIGVCGQIIPWNFPLLMFAWKIAP 199
Cdd:cd07088 78 AKLIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENiFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 200 ALCCGNTVVIKPAEQTPLSALYMGALIKEVG--------------------------KLI----QEAAGRS-------NL 242
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGlpagvlnivtgrgsvvgdalvahpkvGMIsltgSTEAGQKimeaaaeNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 243 KRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQG 322
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 323 PQIDKKQYNKILELIQSGVAEGAKLECGGKGL-GRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERAN 401
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 402 NSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
40-473 |
1.10e-141 |
|
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: 414.66 E-value: 1.10e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 40 IFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGsVWRRMDASERGRLLDKLADLVERDRAV 119
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 120 LATMESLNGGKPFLQAFYVDLQGVIKTFRYYAG------WADKIHGMTIpvdGDyfTFTRHEPIGVCGQIIPWNFPLLMF 193
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAAlardfpFEERRPGSGG---GH--VLVRREPVGVVAAIVPWNAPLFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 194 AWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKE-------------------------------------VGKLIQEA 236
Cdd:cd07139 155 ALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEaglppgvvnvvpadrevgeylvrhpgvdkvsftgstaAGRRIAAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 237 AGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 316
Cdd:cd07139 235 CGE-RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 317 PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK---GLGRkGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTM 393
Cdd:cd07139 314 PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGrpaGLDR-GWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 394 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYnALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07139 393 DDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
26-472 |
6.96e-138 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 406.43 E-value: 6.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 26 LPSPTPNleikyTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFS--LGSVWRRMDASERG 103
Cdd:PLN02467 1 MAIPVPR-----RQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnKGKDWARTTGAVRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 104 RLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvDLQGVIKTFRYYAGWADKIHG-----MTIPVDgDYFTFTRHEPIG 178
Cdd:PLN02467 76 KYLRAIAAKITERKSELAKLETLDCGKPLDEAAW-DMDDVAGCFEYYADLAEALDAkqkapVSLPME-TFKGYVLKEPLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 179 VCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEV----------------------------- 229
Cdd:PLN02467 154 VVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVglppgvlnvvtglgteagaplashpgvdk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 230 ---------GKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVR 300
Cdd:PLN02467 234 iaftgstatGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 301 RSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK--GLGRKGFFIEPTVFSNVTDDMRIAKE 378
Cdd:PLN02467 313 KLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWRE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 379 EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMG 458
Cdd:PLN02467 393 EVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELG 472
|
490
....*....|....
gi 25777726 459 EFGLREYSEVKTVT 472
Cdd:PLN02467 473 EWGLENYLSVKQVT 486
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
41-477 |
1.79e-137 |
|
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: 404.96 E-value: 1.79e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:TIGR02299 4 FIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFK---RWAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKPFLQAfyvdLQGVIKT---FRYYAGWA-DKIHGMTIPVDgDYFTFTRHEPIGVCGQIIPWNFPLLMFAWK 196
Cdd:TIGR02299 81 AVLECLDCGQPLRQT----RQQVIRAaenFRFFADKCeEAMDGRTYPVD-THLNYTVRVPVGPVGLITPWNAPFMLSTWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 197 IAPALCCGNTVVIKPAEQTPLSALYMGALIKE--------------------------------------VGKLIQeAAG 238
Cdd:TIGR02299 156 IAPALAFGNTVVLKPAEWSPLTAARLAEIAKEaglpdgvfnlvhgfgeeagkalvahpdvkavsftgetaTGSIIM-RNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 239 RSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 318
Cdd:TIGR02299 235 ADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 319 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLG-------RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFK 391
Cdd:TIGR02299 315 TEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrgedlGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 392 TMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:TIGR02299 395 DEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNV 474
|
490
....*....|.
gi 25777726 472 TV-----KIPQ 477
Cdd:TIGR02299 475 ALalgphHIPK 485
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
57-475 |
6.02e-137 |
|
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: 402.14 E-value: 6.02e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAF 136
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP---EWRATTPLERARMLRELATRLREHAEELALIDALDCGNP-VSAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 137 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 216
Cdd:cd07107 77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 217 LSALYMGALIKEV-------------------------------------GKLIQEAAGRSnLKRVTLELGGKSPNIIFA 259
Cdd:cd07107 157 LSALRLAELAREVlppgvfnilpgdgatagaalvrhpdvkrialigsvptGRAIMRAAAEG-IKHVTLELGGKNALIVFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 260 DADLDYAVEQAHQGVFFN-QGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQ 338
Cdd:cd07107 236 DADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 339 SGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTN 414
Cdd:cd07107 316 SAKREGARLVTGGGrpegPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777726 415 DINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 475
Cdd:cd07107 396 DISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
41-473 |
1.74e-136 |
|
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: 401.73 E-value: 1.74e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQNSESGRVFPVYNPATGEQ-VCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAV 119
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEvVGTFPLSTASDVDAAVEAAREAFP---EWRKVPAPRRAEYLFRAAELLKKRKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 120 LATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIA 198
Cdd:cd07131 79 LARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 199 PALCCGNTVVIKPAEQTPLSALYM-------------------------GALIK-------------EVGKLIQEAAGRS 240
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLvelfaeaglppgvvnvvhgrgeevgEALVEhpdvdvvsftgstEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 241 NlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTE 320
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 321 QGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR----KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 396
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 397 IERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNAlNAQSPFGGFKMSGNG-REMGEFGLREYSEVKTVTV 473
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGA-EVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
57-473 |
1.94e-134 |
|
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: 395.96 E-value: 1.94e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 137 YVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTP 216
Cdd:cd07108 78 RPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 217 LSALYMG------------------------ALIK-------------EVGKLI-QEAAGRsnLKRVTLELGGKSPNIIF 258
Cdd:cd07108 158 LAVLLLAeilaqvlpagvlnvitgygeecgaALVDhpdvdkvtftgstEVGKIIyRAAADR--LIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 259 ADADLDYAVEQAHQGV-FFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELI 337
Cdd:cd07108 236 PDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 338 QSGVAE-GAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVF 412
Cdd:cd07108 316 DLGLSTsGATVLRGGPlpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25777726 413 TNDINKALTVSSAMQAGTVWIN-CYNALNAQSpFGGFKMSGNGREMG-EFGLREYSEVKTVTV 473
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNqGGGQQPGQS-YGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
55-473 |
4.36e-133 |
|
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: 392.34 E-value: 4.36e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 55 FPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGsvwRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQ 134
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM---KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 135 AfYVDLQGVIKTFRYYAGWADKIHGMTIPVDG-----DYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVI 209
Cdd:cd07149 78 A-RKEVDRAIETLRLSAEEAKRLAGETIPFDAspggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 210 KPAEQTPLSALYMG-------------------------ALIK-------------EVGKLIQEAAGrsnLKRVTLELGG 251
Cdd:cd07149 157 KPASQTPLSALKLAellleaglpkgalnvvtgsgetvgdALVTdprvrmisftgspAVGEAIARKAG---LKKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 252 KSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYN 331
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 332 KILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 411
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25777726 412 FTNDINKALTVSSAMQAGTVWINCYNALNA-QSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMINDSSTFRVdHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
41-474 |
4.03e-132 |
|
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: 390.65 E-value: 4.03e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgSVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTI------PVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFA 194
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 195 WKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEVG-----------------KLIQE------------AAGR------ 239
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGipdgvlnvvngkgavgaQLISHpdvakvsftgsvATGKkigrqa 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 240 -SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 318
Cdd:cd07113 241 aSDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 319 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIE 398
Cdd:cd07113 321 VMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQ 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25777726 399 RANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVK 474
Cdd:cd07113 401 LINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
38-471 |
7.65e-131 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 388.28 E-value: 7.65e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 38 TKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDR 117
Cdd:PLN02278 25 TQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLTASERSKILRRWYDLIIANK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 118 AVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPV-DGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWK 196
Cdd:PLN02278 102 EDLAQLMTLEQGKPLKEA-IGEVAYGASFLEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPVGVVGAITPWNFPLAMITRK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 197 IAPALCCGNTVVIKPAEQTPLSALYMGALIKE--------------------------------------VGKLIQEAAG 238
Cdd:PLN02278 181 VGPALAAGCTVVVKPSELTPLTALAAAELALQagippgvlnvvmgdapeigdallaspkvrkitftgstaVGKKLMAGAA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 239 RSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 318
Cdd:PLN02278 261 AT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 319 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIE 398
Cdd:PLN02278 340 VTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIA 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25777726 399 RANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:PLN02278 420 IANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
55-473 |
3.62e-130 |
|
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: 384.76 E-value: 3.62e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 55 FPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQ 134
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 135 AFYvDLQGVIKTFRYYAGWADKIHGMTIPVDG-DYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAE 213
Cdd:cd07150 78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSpGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 214 QTPLSALYMGALIKE--------------------------------------VGKLIQEAAGRsNLKRVTLELGGKSPN 255
Cdd:cd07150 157 ETPVIGLKIAEIMEEaglpkgvfnvvtgggaevgdelvddprvrmvtftgstaVGREIAEKAGR-HLKKITLELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 256 IIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILE 335
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 336 LIQSGVAEGAKLECGGKGLGRkgfFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND 415
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 25777726 416 INKALTVSSAMQAGTVWINCYNAL-NAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07150 393 LQRAFKLAERLESGMVHINDPTILdEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
32-471 |
5.00e-128 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 380.78 E-value: 5.00e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 32 NLEIKyTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGsVWRRMDASERGRLLDKLAD 111
Cdd:PRK09847 15 SLAIE-NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERG-DWSLSSPAKRKAVLNKLAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 112 LVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLL 191
Cdd:PRK09847 93 LMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 192 MFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKE--------------------------------------VGKLI 233
Cdd:PRK09847 173 LTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEaglpdgvlnvvtgfgheagqalsrhndidaiaftgstrTGKQL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 234 QEAAGRSNLKRVTLELGGKSPNIIFADA-DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVG 312
Cdd:PRK09847 253 LKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 313 SPFDPTTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGKGLGRKGFfIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT 392
Cdd:PRK09847 333 HPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTS 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25777726 393 MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:PRK09847 411 EEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
41-473 |
9.36e-128 |
|
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: 379.49 E-value: 9.36e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE---AWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPA 200
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 201 LCCGNTVVIKPAEQTPLSALYMGALIKE-------------------------------------VGKLIQEAAGRsNLK 243
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDllppgvvnvvngfgleagkplasskriakvaftgettTGRLIMQYASE-NII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 244 RVTLELGGKSPNIIFA------DADLDYAVEQAhqGVF-FNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 316
Cdd:cd07116 240 PVTLELGGKSPNIFFAdvmdadDAFFDKALEGF--VMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 317 PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNvTDDMRIAKEEIFGPVQEILRFKT 392
Cdd:cd07116 318 TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGErnelGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 393 MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 472
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 476
|
.
gi 25777726 473 V 473
Cdd:cd07116 477 V 477
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
76-473 |
2.30e-127 |
|
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: 376.87 E-value: 2.30e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 76 DIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWAD 155
Cdd:cd07104 1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKA-AFEVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 156 KIHGMTIPVDGD-YFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKE------ 228
Cdd:cd07104 77 RPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAEIFEeaglpk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 229 ---------------------------------VGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVF 275
Cdd:cd07104 157 gvlnvvpgggseigdalvehprvrmisftgstaVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 276 FNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKglg 355
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT--- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 356 RKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINC 435
Cdd:cd07104 313 YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 25777726 436 YNALN-AQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07104 393 QTVNDePHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
55-473 |
4.56e-125 |
|
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: 372.07 E-value: 4.56e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 55 FPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQ 134
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD---VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 135 AfYVDLQGVIKTFRYYAGWADKIHGMTIPVDG-DY----FTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVI 209
Cdd:cd07145 78 S-RVEVERTIRLFKLAAEEAKVLRGETIPVDAyEYnerrIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 210 KPAEQTPLSALYMGALIKE--------------------------------------VGKLIQEAAGRSnLKRVTLELGG 251
Cdd:cd07145 157 KPSSNTPLTAIELAKILEEaglppgvinvvtgygsevgdeivtnpkvnmisftgstaVGLLIASKAGGT-GKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 252 KSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYN 331
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 332 KILELIQSGVAEGAKLECGGKGLGrkGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAV 411
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25777726 412 FTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFRWDNlPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
41-473 |
1.73e-123 |
|
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: 368.43 E-value: 1.73e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQNSESGrVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07086 2 VIGGEWVGSGGE-TFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFK---EWRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 199
Cdd:cd07086 78 GRLVSLEMGKILPEG-LGEVQEMIDICDYAVGLSRMLYGLTIPSErPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 200 ALCCGNTVVIKPAEQTPLSALYM---------------------------GALIK--------------EVGKLIQEAAG 238
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVtkilaevleknglppgvvnlvtgggdgGELLVhdprvplvsftgstEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 239 RSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 318
Cdd:cd07086 237 RRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 319 TEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGR--KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEV 396
Cdd:cd07086 316 TLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 397 IERANNSDFGLVAAVFTNDINKALTVSSAM--QAGTVWIN--CYNAlNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 472
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAFRWLGPKgsDCGIVNVNipTSGA-EIGGAFGGEKETGGGRESGSDAWKQYMRRSTCT 474
|
.
gi 25777726 473 V 473
Cdd:cd07086 475 I 475
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
41-475 |
1.94e-123 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 368.67 E-value: 1.94e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWqnSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAfsLGSVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:TIGR03216 4 FINGAF--VESGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAA--LKGPWGKMTVAERADLLYAVADEIERRFDDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHG----MTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWK 196
Cdd:TIGR03216 80 LAAEVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTecfeMATPDGKGALNYAVRKPLGVVGVISPWNLPLLLMTWK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 197 IAPALCCGNTVVIKPAEQTPLSALYMGALIKEV---------------------------------------GKLIQEAA 237
Cdd:TIGR03216 160 VGPALACGNTVVVKPSEETPGTATLLGEVMNAVgvpkgvynvvhgfgpdsagefltrhpgvdaitftgetrtGSAIMKAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 238 GRSnLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDP 317
Cdd:TIGR03216 240 ADG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 318 TTEQGPQIDKKQYNKILELIQSGVAEGAKLECGG-----KGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT 392
Cdd:TIGR03216 319 ATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGgvpdfGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFDS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 393 MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 472
Cdd:TIGR03216 399 EEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNVC 478
|
...
gi 25777726 473 VKI 475
Cdd:TIGR03216 479 IKL 481
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
77-473 |
7.95e-120 |
|
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: 357.54 E-value: 7.95e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 77 IDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFY-VDLQGVIktFRYYAgwaD 155
Cdd:cd07100 1 IEAALDRAHAAFLA---WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEKCAWI--CRYYA---E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 156 KIHGM----TIPVDGDYfTFTRHEPIGVCGQIIPWNFPL---LMFAwkiAPALCCGNTVVIKPAEQTPLSALYMGALIKE 228
Cdd:cd07100 73 NAEAFladePIETDAGK-AYVRYEPLGVVLGIMPWNFPFwqvFRFA---APNLMAGNTVLLKHASNVPGCALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 229 VG----------------------KLIQ-------EAAGRS-------NLKRVTLELGGKSPNIIFADADLDYAVEQAHQ 272
Cdd:cd07100 149 AGfpegvfqnllidsdqveaiiadPRVRgvtltgsERAGRAvaaeagkNLKKSVLELGGSDPFIVLDDADLDKAVKTAVK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 273 GVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGK 352
Cdd:cd07100 229 GRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 353 GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVW 432
Cdd:cd07100 309 RPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVF 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 25777726 433 INCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07100 389 INGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
40-475 |
1.74e-115 |
|
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: 349.21 E-value: 1.74e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 40 IFINNEWQnsESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRA 118
Cdd:cd07124 35 LVIGGKEV--RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP---TWRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 119 VLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIA 198
Cdd:cd07124 110 ELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 199 PALCCGNTVVIKPAEQTPLSA-LYMGALI-------------------------------------KEVGKLIQEAAGR- 239
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAaKLVEILEeaglppgvvnflpgpgeevgdylvehpdvrfiaftgsREVGLRIYERAAKv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 240 ----SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 315
Cdd:cd07124 269 qpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 316 DPTTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGK--GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTM 393
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEvlELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 394 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSG-NGREMGEFGLREYSEVKT 470
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGtGSKAGGPDYLLQFMQPKT 507
|
....*
gi 25777726 471 VTVKI 475
Cdd:cd07124 508 VTENF 512
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
58-473 |
6.52e-115 |
|
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: 345.87 E-value: 6.52e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 58 YNPATGEQVCEVQEADKADIDKAVQAARLAFSlGSVWRRmDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfY 137
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFD-ETDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEA-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 138 VDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPL 217
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 218 SALYMGALIKEV---------------------------------------GKLIQEAAGrSNLKRVTLELGGKSPNIIF 258
Cdd:cd07120 159 INAAIIRILAEIpslpagvvnlftesgsegaahlvaspdvdvisftgstatGRAIMAAAA-PTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 259 ADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQ 338
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 339 SGVAEGAK-LECGGKGLGR--KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND 415
Cdd:cd07120 318 RAIAAGAEvVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 25777726 416 INKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
55-469 |
1.08e-112 |
|
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: 339.99 E-value: 1.08e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 55 FPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQ 134
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR---PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 135 AfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGD-----YFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVI 209
Cdd:cd07147 78 A-RGEVARAIDTFRIAAEEATRIYGEVLPLDISargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 210 KPAEQTPLSALYMGALIKE-------------------------------------VGKLIQEAAGRsnlKRVTLELGGK 252
Cdd:cd07147 157 KPASRTPLSALILGEVLAEtglpkgafsvlpcsrddadllvtderikllsftgspaVGWDLKARAGK---KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 253 SPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNK 332
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 333 ILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVF 412
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 25777726 413 TNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVK 469
Cdd:cd07147 391 TRDLEKALRAWDELEVGGVVINDVPTFRVDHmPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
44-474 |
8.20e-112 |
|
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: 338.12 E-value: 8.20e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 44 NEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVERDRAVLATM 123
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA---QKEWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 124 ESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIP--VDGDYFTFTRhEPIGVCGQIIPWNFPLLMFAWKIAPAL 201
Cdd:cd07151 78 LIRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPsdVPGKENRVYR-EPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 202 CCGNTVVIKPAEQTPLSALYMGALIKE---------------------------------------VGKLIQEAAGRsNL 242
Cdd:cd07151 156 ALGNAVVLKPASDTPITGGLLLAKIFEeaglpkgvlnvvvgagseigdafvehpvprlisftgstpVGRHIGELAGR-HL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 243 KRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQG 322
Cdd:cd07151 235 KKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 323 PQIDKKQYNKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANN 402
Cdd:cd07151 315 PLINESQVDGLLDKIEQAVEEGATLLVGGE---AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25777726 403 SDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALN--AQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVK 474
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVNdePHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
57-473 |
7.07e-111 |
|
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: 335.56 E-value: 7.07e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAE---NRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 137 YvDLQGVIKTFRYYAGWADKIHGMTIPVD-----GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07094 80 V-EVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 212 AEQTPLSALYMGALIKE--------------------------------------VGKLIQEAAGrsnLKRVTLELGGKS 253
Cdd:cd07094 159 ASKTPLSALELAKILVEagvpegvlqvvtgerevlgdafaadervamlsftgsaaVGEALRANAG---GKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 254 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 333
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 334 LELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 413
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777726 414 NDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNDSSAFRTDWmPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
58-473 |
1.55e-110 |
|
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: 334.57 E-value: 1.55e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 58 YNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPfLQAFY 137
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQR---AWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 138 VDLQGVIKTFRYYAGWADKI-------HGMTIPVdgdyFTFT-RHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVI 209
Cdd:cd07099 77 LEVLLALEAIDWAARNAPRVlaprkvpTGLLMPN----KKATvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 210 KPAEQTPLSALYM------------------------GALIKEV------------GKLIQEAAGRsNLKRVTLELGGKS 253
Cdd:cd07099 153 KPSEVTPLVGELLaeawaaagppqgvlqvvtgdgatgAALIDAGvdkvaftgsvatGRKVMAAAAE-RLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 254 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 333
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 334 LELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 413
Cdd:cd07099 312 RRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25777726 414 NDINKALTVSSAMQAGTVWINC--YNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07099 392 RDLARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
49-473 |
6.52e-106 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 324.91 E-value: 6.52e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 49 SESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNG 128
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA---QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 129 GKPFLQAFYvDLQGVIKTFRYYAGWADKI-----HGMTIPVDGDyfTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCC 203
Cdd:PRK09407 105 GKARRHAFE-EVLDVALTARYYARRAPKLlaprrRAGALPVLTK--TTELRQPKGVVGVISPWNYPLTLAVSDAIPALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 204 GNTVVIKPAEQTPLSALYM-------------------------GALIKEV-----------GKLIQEAAGRsNLKRVTL 247
Cdd:PRK09407 182 GNAVVLKPDSQTPLTALAAvellyeaglprdlwqvvtgpgpvvgTALVDNAdylmftgstatGRVLAEQAGR-RLIGFSL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 248 ELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDK 327
Cdd:PRK09407 261 ELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 328 KQYNKILELIQSGVAEGAKLECGGKG---LGrkGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSD 404
Cdd:PRK09407 341 AQLETVSAHVDDAVAKGATVLAGGKArpdLG--PLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTP 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25777726 405 FGLVAAVFTNDINKALTVSSAMQAGTVWIN-CYNALNA--QSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:PRK09407 419 YGLNASVWTGDTARGRAIAARIRAGTVNVNeGYAAAWGsvDAPMGGMKDSGLGRRHGAEGLLKYTESQTIAT 490
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
38-474 |
5.01e-104 |
|
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: 318.69 E-value: 5.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 38 TKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDR 117
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA---WSATPVLKRQQVMFKFRQLLEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 118 AVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWK 196
Cdd:cd07085 78 DELARLITLEHGKTLADA-RGDVLRGLEVVEFACSIPHLLKGEYLEnVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 197 IAPALCCGNTVVIKPAEQTPLSALYMGALIKE-------------------------------------VGKLIQEAAGR 239
Cdd:cd07085 157 FPMAIACGNTFVLKPSERVPGAAMRLAELLQEaglpdgvlnvvhggkeavnalldhpdikavsfvgstpVGEYIYERAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 240 SNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTT 319
Cdd:cd07085 237 NG-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 320 EQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGL----GRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 395
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 396 VIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALN-AQSPFGGFKMS--GNGREMGEFGLREYSEVKTVT 472
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPlAFFSFGGWKGSffGDLHFYGKDGVRFYTQTKTVT 475
|
..
gi 25777726 473 VK 474
Cdd:cd07085 476 SR 477
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
60-473 |
3.65e-102 |
|
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: 313.09 E-value: 3.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 60 PATGEQVCEVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYvD 139
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA---QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFE-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 140 LQGVIKTFRYYAGWADKI-----HGMTIPVdgdyFTFTR--HEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPA 212
Cdd:cd07101 79 VLDVAIVARYYARRAERLlkprrRRGAIPV----LTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 213 EQTPLSALYM-------------------------GALIKEV-----------GKLIQEAAGRsNLKRVTLELGGKSPNI 256
Cdd:cd07101 155 SQTALTALWAvellieaglprdlwqvvtgpgsevgGAIVDNAdyvmftgstatGRVVAERAGR-RLIGCSLELGGKNPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 257 IFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILEL 336
Cdd:cd07101 234 VLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 337 IQSGVAEGAKLECGGKG---LGRkgFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 413
Cdd:cd07101 314 VDDAVAKGATVLAGGRArpdLGP--YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25777726 414 NDINKALTVSSAMQAGTVWIN-CYNAL--NAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07101 392 RDGARGRRIAARLRAGTVNVNeGYAAAwaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
39-474 |
4.75e-102 |
|
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: 313.35 E-value: 4.75e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 39 KIFINNEWQNSeSGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgSVWRRMDASERGRLLDKLADLVERDRA 118
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGR--GWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 119 VLATMESLNGGKPFLQAfyvdLQGVIKT---FRYYAGWADKIHGMTIPVDGDYFT-----FTRHEPIGVCGQIIPWNFPL 190
Cdd:cd07082 80 EVANLLMWEIGKTLKDA----LKEVDRTidyIRDTIEELKRLDGDSLPGDWFPGTkgkiaQVRREPLGVVLAIGPFNYPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 191 LMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIK--------------------------------------EVGKL 232
Cdd:cd07082 156 NLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHdagfpkgvvnvvtgrgreigdplvthgridvisftgstEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 233 IQEAAGRsnlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVG 312
Cdd:cd07082 236 LKKQHPM---KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 313 SPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGrkGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT 392
Cdd:cd07082 313 MPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVND 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 393 MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:cd07082 391 IEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
...
gi 25777726 472 TVK 474
Cdd:cd07082 471 VIN 473
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
76-473 |
8.74e-101 |
|
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: 308.74 E-value: 8.74e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 76 DIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL-ATMESLNGGKPFLQAFYVDLqgVIKTFRYYAGWA 154
Cdd:cd07105 1 DADQAVEAAAAAFP---AWSKTPPSERRDILLKAADLLESRRDEFiEAMMEETGATAAWAGFNVDL--AAGMLREAASLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 155 DKIHGMTIPVD--GDYfTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMG--------- 223
Cdd:cd07105 76 TQIIGGSIPSDkpGTL-AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGrvfheaglp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 224 -------------------ALIK-------------EVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAH 271
Cdd:cd07105 155 kgvlnvvthspedapevveALIAhpavrkvnftgstRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 272 QGVFFNQGQCCTAGSRIFVEESIYEEFVrrsvERAKRRVVGSPFDPTTEqGPQIDKKQYNKILELIQSGVAEGAKLECGG 351
Cdd:cd07105 234 FGAFLNSGQICMSTERIIVHESIADEFV----EKLKAAAEKLFAGPVVL-GSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 352 KG-LGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGT 430
Cdd:cd07105 309 LAdESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 25777726 431 VWINCYNALN-AQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07105 389 VHINGMTVHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
42-472 |
4.05e-100 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 309.94 E-value: 4.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 42 INNEWQNSEsgRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:PRK03137 41 IGGERITTE--DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE---TWKKWSPEDRARILLRAAAIIRRRKHEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYA----GWADKIHgmTIPVDGDYFTFtRHEPIGVCGQIIPWNFPLLMFAWK 196
Cdd:PRK03137 116 SAWLVKEAGKPWAEA-DADTAEAIDFLEYYArqmlKLADGKP--VESRPGEHNRY-FYIPLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 197 IAPALCCGNTVVIKPAEQTPLSALYM--------------------GALI------------------KEVGKLIQEAAG 238
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFvevleeaglpagvvnfvpgsGSEVgdylvdhpktrfitftgsREVGLRIYERAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 239 RSN-----LKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGS 313
Cdd:PRK03137 272 KVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 314 PFDPTtEQGPQIDKKQYNKILELIQSGVAEGaKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTM 393
Cdd:PRK03137 352 PEDNA-YMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 394 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSG-NGREMGEFGLREYSEVKT 470
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSGtDSKAGGPDYLLLFLQAKT 509
|
..
gi 25777726 471 VT 472
Cdd:PRK03137 510 VS 511
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
63-473 |
8.44e-100 |
|
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: 306.53 E-value: 8.44e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 63 GEQVCEVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVERDRAVLATM---ESlnGGKPFLQAFYVD 139
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAA---QRAWAATPPRERAAVLRRAADLLEEHADEIADWivrES--GSIRPKAGFEVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 140 LqgVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSA 219
Cdd:cd07152 76 A--AIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 220 LYMGALIKE--------------------------------------VGKLIQEAAGRsNLKRVTLELGGKSPNIIFADA 261
Cdd:cd07152 154 GVVIARLFEeaglpagvlhvlpggadagealvedpnvamisftgstaVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 262 DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGV 341
Cdd:cd07152 233 DLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 342 AEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALT 421
Cdd:cd07152 313 AAGARLEAGGT---YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 25777726 422 VSSAMQAGTVWINCYNALN-AQSPFGGFKMSGNG-REMGEFGLREYSEVKTVTV 473
Cdd:cd07152 390 LADRLRTGMLHINDQTVNDePHNPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
57-473 |
7.77e-96 |
|
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: 296.58 E-value: 7.77e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAArlafslGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAF 136
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALA------ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 137 YvDLQGVIKTFRYYAGWADKIHGMTIPVD-----GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07146 77 Y-EVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 212 AEQTPLSALYMGALIKE--------------------------------------VGKLIQEAAGrsnLKRVTLELGGKS 253
Cdd:cd07146 156 SEKTPLSAIYLADLLYEaglppdmlsvvtgepgeigdelithpdvdlvtftggvaVGKAIAATAG---YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 254 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 333
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 334 LELIQSGVAEGAKLECGGkglGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 413
Cdd:cd07146 313 ENRVEEAIAQGARVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25777726 414 NDINKALTVSSAMQAGTVWINCYNALNAQ-SPFGGFKMSGNG-REMGEFGLREYSEVKTVTV 473
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
58-471 |
1.11e-95 |
|
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: 296.46 E-value: 1.11e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 58 YNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfy 137
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQK---GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 138 vdlQGVIKTF----RYYAGWADKIHGMTIPVDGDYFT-FTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPA 212
Cdd:cd07102 76 ---GGEIRGMleraRYMISIAEEALADIRVPEKDGFErYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 213 EQTPL------SALYMGALIKEV-------------------------------GKLIQEAAGRsNLKRVTLELGGKSPN 255
Cdd:cd07102 153 PQTPLcgerfaAAFAEAGLPEGVfqvlhlshetsaaliadpridhvsftgsvagGRAIQRAAAG-RFIKVGLELGGKDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 256 IIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILE 335
Cdd:cd07102 232 YVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 336 LIQSGVAEGAKLECGGKGLGR---KGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVF 412
Cdd:cd07102 312 QIADAIAKGARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVW 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 25777726 413 TNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:cd07102 392 TKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
41-475 |
2.80e-95 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 296.43 E-value: 2.80e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP---AWRALTAKERANILRRWFNLMMEHQDDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKPFLQAfyvdlQGVIKTFRYYAGW----ADKIHGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAW 195
Cdd:PRK11241 91 ARLMTLEQGKPLAEA-----KGEISYAASFIEWfaeeGKRIYGDTIPgHQADKRLIVIKQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 196 KIAPALCCGNTVVIKPAEQTPLSALYMGALIK--------------------------------------EVGKLIQEAA 237
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIragipagvfnvvtgsagavggeltsnplvrklsftgstEIGRQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 238 GRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDP 317
Cdd:PRK11241 246 AK-DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 318 TTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVI 397
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25777726 398 ERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKI 475
Cdd:PRK11241 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL 482
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
59-471 |
6.20e-91 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 284.32 E-value: 6.20e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 59 NPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAfYV 138
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFR---DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA-KA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 139 DLQGVIKTFRYYAgwaDKIHGMTIPVDGDYFT------FTRHEPIGVCGQIIPWNFPL---LMFAwkiAPALCCGNTVVI 209
Cdd:PRK09406 83 EALKCAKGFRYYA---EHAEALLADEPADAAAvgasraYVRYQPLGVVLAVMPWNFPLwqvVRFA---APALMAGNVGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 210 KPAEQTPLSALYMGALIKEVG--------KLI---------------------QEAAGRS-------NLKRVTLELGGKS 253
Cdd:PRK09406 157 KHASNVPQTALYLADLFRRAGfpdgcfqtLLVgsgaveailrdprvaaatltgSEPAGRAvaaiagdEIKKTVLELGGSD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 254 PNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKI 333
Cdd:PRK09406 237 PFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 334 LELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFT 413
Cdd:PRK09406 317 EKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWT 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 25777726 414 NDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:PRK09406 397 RDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
58-473 |
1.16e-87 |
|
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: 276.10 E-value: 1.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 58 YNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFY 137
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQR---EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 138 vdlqGVIKTFryyagwADKI-----HG----MTIPVDGDYFTFTR-----HEPIGVCGQIIPWNFPLLMFAWKIAPALCC 203
Cdd:cd07098 78 ----GEILVT------CEKIrwtlkHGekalRPESRPGGLLMFYKrarveYEPLGVVGAIVSWNYPFHNLLGPIIAALFA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 204 GNTVVIKPAEQTPLSALYMGALIKE-----------------------------------------VGKLIQEAAGRSnL 242
Cdd:cd07098 148 GNAIVVKVSEQVAWSSGFFLSIIREclaacghdpdlvqlvtclpetaealtshpvidhitfigsppVGKKVMAAAAES-L 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 243 KRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQG 322
Cdd:cd07098 227 TPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 323 PQIDKKQYNKILELIQSGVAEGAKLECGGK----GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIE 398
Cdd:cd07098 307 AMISPARFDRLEELVADAVEKGARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVE 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25777726 399 RANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCY--NALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTV 473
Cdd:cd07098 387 IANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFgvNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
106-471 |
5.27e-83 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 262.36 E-value: 5.27e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 106 LDKLADLVERDRAVLATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD---GDYFTFTRhePIGVCGQ 182
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSDrpgENILLFKR--ALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 183 IIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEV--------------------------------- 229
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIglpkgvfnlvlgrgetvgqelagnpkvamvsmt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 230 -----GKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVE 304
Cdd:PRK10090 158 gsvsaGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 305 RAKRRVVGSPFD-PTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGP 383
Cdd:PRK10090 237 AMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 384 VQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLR 463
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLH 396
|
....*...
gi 25777726 464 EYSEVKTV 471
Cdd:PRK10090 397 EYLQTQVV 404
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
59-471 |
1.69e-72 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 236.68 E-value: 1.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 59 NPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGrllDKLADLVE--RDRA-VLATMESLNGGKPFLQA 135
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFR---DWRETNIDYRA---QKLRDIGKalRARSeEMAQMITREMGKPINQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 136 fyvdLQGVIKTFRYYAGWADKIHGMTIP----VDGDYfTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:PRK13968 87 ----RAEVAKSANLCDWYAEHGPAMLKAeptlVENQQ-AVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 212 AEQTPLSALYMGALIKEV-------------------------------------GKLIQEAAGRSnLKRVTLELGGKSP 254
Cdd:PRK13968 162 APNVMGCAQLIAQVFKDAgipqgvygwlnadndgvsqmindsriaavtvtgsvraGAAIGAQAGAA-LKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 255 NIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKIL 334
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 335 ELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTN 414
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 25777726 415 DINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:PRK13968 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
43-473 |
1.70e-72 |
|
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: 236.72 E-value: 1.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 43 NNEWQnsESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLAT 122
Cdd:cd07130 4 DGEWG--GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK---EWRDVPAPKRGEIVRQIGDALRKKKEALGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 123 MESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPAL 201
Cdd:cd07130 79 LVSLEMGKILPEG-LGEVQEMIDICDFAVGLSRQLYGLTIPSErPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 202 CCGNTVVIKPAEQTPLSALYMGALIKEV-----------------------------------------GKLI-QEAAGR 239
Cdd:cd07130 158 VCGNVVVWKPSPTTPLTAIAVTKIVARVleknglpgaiaslvcggadvgealvkdprvplvsftgstavGRQVgQAVAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 240 snLKRVTLELGGKSPNIIFADADLDYAVeqahQGVFF----NQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPF 315
Cdd:cd07130 238 --FGRSLLELGGNNAIIVMEDADLDLAV----RAVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 316 DPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSnVTDDMRIAKEEIFGPVQEILRFKTMDE 395
Cdd:cd07130 312 DDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 396 VIERANNSDFGLVAAVFTNDINKALTVSSAMQA--GTVWINC-YNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVT 472
Cdd:cd07130 391 AIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVNIgTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCT 470
|
.
gi 25777726 473 V 473
Cdd:cd07130 471 I 471
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
57-454 |
6.42e-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: 235.01 E-value: 6.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWrrMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAf 136
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 137 YVDLQGVIKTFRYYAGWADKIHGMTIPVD-----GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKP 211
Cdd:cd07148 80 KVEVTRAIDGVELAADELGQLGGREIPMGltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 212 AEQTPLSALYMGALIKEVG-------KLIQEAAG-------------------------RSNLK---RVTLELGGKSPNI 256
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGlpegwcqAVPCENAVaeklvtdprvaffsfigsarvgwmlRSKLApgtRCALEHGGAAPVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 257 IFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILEL 336
Cdd:cd07148 240 VDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 337 IQSGVAEGAKLECGGKGLGRKGFfiEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDI 416
Cdd:cd07148 320 VNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDL 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 25777726 417 NKALTVSSAMQAGTVWINCYNALNAQ-SPFGGFKMSGNG 454
Cdd:cd07148 398 DVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
173-471 |
7.08e-69 |
|
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: 226.34 E-value: 7.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 173 RHEPIGVCGQIIPWNFPL-LMFAwKIAPALCCGNTVVIKPAEQTPLSALYMGALIKE----------------------- 228
Cdd:cd07134 97 RYEPKGVCLIISPWNYPFnLAFG-PLVSAIAAGNTAILKPSELTPHTSAVIAKIIREafdedevavfegdaevaqallel 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 229 ------------VGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYE 296
Cdd:cd07134 176 pfdhifftgspaVGKIVMAAAAK-HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 297 EFVRRsVERAKRRVVGSpfDPTTEQGPQ----IDKKQYNKILELIQSGVAEGAKLECGGKgLGRKGFFIEPTVFSNVTDD 372
Cdd:cd07134 255 AFVEH-LKAEIEKFYGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGGQ-FDAAQRYIAPTVLTNVTPD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 373 MRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND---INKALTVSSamqAGTVWIN--CYNALNAQSPFGG 447
Cdd:cd07134 331 MKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDkanVNKVLARTS---SGGVVVNdvVLHFLNPNLPFGG 407
|
330 340
....*....|....*....|....
gi 25777726 448 FKMSGNGREMGEFGLREYSEVKTV 471
Cdd:cd07134 408 VNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
40-472 |
1.73e-67 |
|
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: 224.38 E-value: 1.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 40 IFINNEWqnSESGRVFPVYNP-ATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRA 118
Cdd:cd07083 21 LVIGGEW--VDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFK---TWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 119 VLATMESLNGGKPFLQAFyVDLQGVIKTFRYYAGWADKIHG---MTIPVDG-DYFTFTRhePIGVCGQIIPWNFPLLMFA 194
Cdd:cd07083 96 ELIATLTYEVGKNWVEAI-DDVAEAIDFIRYYARAALRLRYpavEVVPYPGeDNESFYV--GLGAGVVISPWNFPVAIFT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 195 WKIAPALCCGNTVVIKPAEQTPL-------------------------SALYMGALIK-------------EVGKLIQEA 236
Cdd:cd07083 173 GMIVAPVAVGNTVIAKPAEDAVVvgykvfeifheagfppgvvqflpgvGEEVGAYLTEherirginftgslETGKKIYEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 237 AGR-----SNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVV 311
Cdd:cd07083 253 AARlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 312 GSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGaKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFK 391
Cdd:cd07083 333 GPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 392 TMD--EVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSGNGREMGEFG-LREYS 466
Cdd:cd07083 412 DDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkITGALVGVQPFGGFKLSGTNAKTGGPHyLRRFL 491
|
....*.
gi 25777726 467 EVKTVT 472
Cdd:cd07083 492 EMKAVA 497
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
29-478 |
5.06e-65 |
|
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: 218.60 E-value: 5.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 29 PTPNLEIKYTKI--FINNEWQNS--------ESGRVFPVYNPATGEQV-CEVQEADKADIDKAVQAARLAFSlgsVWRRM 97
Cdd:cd07125 12 LEVPLEALADALkaFDEKEWEAIpiingeetETGEGAPVIDPADHERTiGEVSLADAEDVDAALAIAAAAFA---GWSAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 98 DASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFyVDLQGVIKTFRYYAGWADK-IHGMTIPVDGDYFTFTRHEP 176
Cdd:cd07125 89 PVEERAEILEKAADLLEANRGELIALAAAEAGKTLADAD-AEVREAIDFCRYYAAQARElFSDPELPGPTGELNGLELHG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 177 IGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSA-------------------LYMG------ALIK---- 227
Cdd:cd07125 168 RGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAaravellheagvprdvlqlVPGDgeeigeALVAhpri 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 228 ---------EVGKLIQEAagRSNLKRVTL----ELGGKspNIIFAD--ADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEE 292
Cdd:cd07125 248 dgviftgstETAKLINRA--LAERDGPILpliaETGGK--NAMIVDstALPEQAVKDVVQSAFGSAGQRCSALRLLYLQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 293 SIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEgAKLECGGKGLGRKGFFIEPTVFSNVTDD 372
Cdd:cd07125 324 EIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 373 MRiaKEEIFGPVQEILRFK--TMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNA----QsPFG 446
Cdd:cd07125 403 DL--TTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN-RNITGAivgrQ-PFG 478
|
490 500 510
....*....|....*....|....*....|....*
gi 25777726 447 GFKMSGNGREMGefG---LREYSEVKTVTVKIPQK 478
Cdd:cd07125 479 GWGLSGTGPKAG--GpnyLLRFGNEKTVSLNTTAA 511
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
39-474 |
1.56e-61 |
|
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: 208.20 E-value: 1.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 39 KIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRA 118
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFL---TWGQTSLAQRTSVLLRYQALLKEHRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 119 VLATMESLNGGKPFLQAFYVDLQGvIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKI 197
Cdd:TIGR01722 79 EIAELITAEHGKTHSDALGDVARG-LEVVEHACGVNSLLKGETSTqVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 198 APALCCGNTVVIKPAEQTPLSALYMGALIKE-------------------------------------VGKLIQEAAGRS 240
Cdd:TIGR01722 158 PIAIACGNTFVLKPSEKVPSAAVKLAELFSEagapdgvlnvvhgdkeavdrllehpdvkavsfvgstpIGRYIHTTGSAH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 241 NlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSR-IFVEESiyEEFVRRSVERAKRRVVGSPFDPTT 319
Cdd:TIGR01722 238 G-KRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAaVLVGAA--DEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 320 EQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGF----FIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDE 395
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 396 VIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCynALNAQSP---FGGFKMS--GNGREMGEFGLREYSEVKT 470
Cdd:TIGR01722 395 AIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV--PIPVPLPyfsFTGWKDSffGDHHIYGKQGTHFYTRGKT 472
|
....
gi 25777726 471 VTVK 474
Cdd:TIGR01722 473 VTTR 476
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
94-471 |
2.44e-60 |
|
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: 203.53 E-value: 2.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 94 WRRmdasergRLLDKLADLV-ERDRAVLATMES-LngGKPFLQAFYVDLQGVIKTFRYY----AGWADKIHGMTIPVDGD 167
Cdd:cd07087 21 WRK-------AQLKALKRMLtENEEEIAAALYAdL--GKPPAEAYLTEIAVVLGEIDHAlkhlKKWMKPRRVSVPLLLQP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 168 YFTFTRHEPIGVCGQIIPWNFPLLMfawKIAP---ALCCGNTVVIKPAEQTP-LSAL-------YM---------G---- 223
Cdd:cd07087 92 AKAYVIPEPLGVVLIIGPWNYPLQL---ALAPligAIAAGNTVVLKPSELAPaTSALlaklipkYFdpeavavveGgvev 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 224 --ALIKE------------VGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIF 289
Cdd:cd07087 169 atALLAEpfdhifftgspaVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 290 VEESIYEEFvrrsVERAKRRVV---GSPFDPTTEQGPQIDKKQYNKILELIQSGvaegaKLECGGkGLGRKGFFIEPTVF 366
Cdd:cd07087 248 VHESIKDEL----IEELKKAIKefyGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGG-QVDKEERYIAPTIL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 367 SNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSP 444
Cdd:cd07087 318 DDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvLLHAAIPNLP 397
|
410 420
....*....|....*....|....*..
gi 25777726 445 FGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:cd07087 398 FGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
39-454 |
4.25e-60 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 204.99 E-value: 4.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 39 KIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRLLDKLADLVERDRA 118
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA---WAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 119 VLATMESLNGGKPFLQAF-----------YVDLQGViktfrYYAGWADKIHGMTIPVDG-DYFTFTRHEPIGVCGQIIPW 186
Cdd:PLN00412 94 PIAECLVKEIAKPAKDAVtevvrsgdlisYTAEEGV-----RILGEGKFLVSDSFPGNErNKYCLTSKIPLGVVLAIPPF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 187 NFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEVG---KLIQEAAGRS-------------NLKRVT---- 246
Cdd:PLN00412 169 NYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGfpkGLISCVTGKGseigdfltmhpgvNCISFTggdt 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 247 --------------LELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVG 312
Cdd:PLN00412 249 giaiskkagmvplqMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 313 SPFDpTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKglgRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKT 392
Cdd:PLN00412 329 PPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWK---REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINS 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25777726 393 MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQS-PFGGFKMSGNG 454
Cdd:PLN00412 405 VEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHfPFQGLKDSGIG 467
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
98-471 |
7.63e-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: 189.23 E-value: 7.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 98 DASERGRLLDKLADLVERDRAVLAtmESLN---GGKPFLQAFYVDLQGVIKTFRYY----AGW--ADKIHGMtipvdgdy 168
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALA--EAISadfGHRSRHETLLAEILPSIAGIKHArkhlKKWmkPSRRHVG-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 169 FTFT------RHEPIGVCGQIIPWNFPL-LMFAWKIApALCCGNTVVIKPAEQTP-LSALyMGALIKE------------ 228
Cdd:cd07133 88 LLFLpakaevEYQPLGVVGIIVPWNYPLyLALGPLIA-ALAAGNRVMIKPSEFTPrTSAL-LAELLAEyfdedevavvtg 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 229 -----------------------VGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAG 285
Cdd:cd07133 166 gadvaaafsslpfdhllftgstaVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 286 SRIFVEESIYEEFVRRSVERAKRRVvgspfdPTTEQGPQ----IDKKQYNKILELIQSGVAEGAKL-ECGGKG----LGR 356
Cdd:cd07133 245 DYVLVPEDKLEEFVAAAKAAVAKMY------PTLADNPDytsiINERHYARLQGLLEDARAKGARViELNPAGedfaATR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 357 KgffIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND---INKAL--TVSsamqaGTV 431
Cdd:cd07133 319 K---LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDkaeQDRVLrrTHS-----GGV 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 25777726 432 WIN--CYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:cd07133 391 TINdtLLHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
41-455 |
3.13e-54 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 189.01 E-value: 3.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQnSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:PRK09457 4 WINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFP---AWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKPFLQAFY--------VDLQgvIKTFRYYAGwaDKIHGMtipvdGDYFTFTRHEPIGVCGQIIPWNFPLLM 192
Cdd:PRK09457 80 AEVIARETGKPLWEAATevtaminkIAIS--IQAYHERTG--EKRSEM-----ADGAAVLRHRPHGVVAVFGPYNFPGHL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 193 FAWKIAPALCCGNTVVIKPAEQTPLSA------------------LYMGAliKEVGK----------------------L 232
Cdd:PRK09457 151 PNGHIVPALLAGNTVVFKPSELTPWVAeltvklwqqaglpagvlnLVQGG--RETGKalaahpdidgllftgsantgylL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 233 IQEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIY-EEFVRRSVERAKRRVV 311
Cdd:PRK09457 229 HRQFAGQPE-KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 312 GSPF-DPTTEQGPQIDKKQYNKILELIQSGVAEGAK----LECGGKGLGrkgfFIEPTVFsNVTDDMRIAKEEIFGPVQE 386
Cdd:PRK09457 308 GRWDaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKslleMTQLQAGTG----LLTPGII-DVTGVAELPDEEYFGPLLQ 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 387 ILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTV-WINCYNALNAQSPFGGFKMSGNGR 455
Cdd:PRK09457 383 VVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGNHR 452
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
75-471 |
1.22e-53 |
|
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: 186.27 E-value: 1.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 75 ADIDKAVQAARLAFSLGsvwRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAG-- 152
Cdd:cd07135 5 DEIDSIHSRLRATFRSG---KTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKnl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 153 --WA--DKIHGMTIPvdgdYF---TFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGAL 225
Cdd:cd07135 82 kkWAkdEKVKDGPLA----FMfgkPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 226 IKE-----------------------------------VGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQA 270
Cdd:cd07135 158 VPKyldpdafqvvqggvpettalleqkfdkifytgsgrVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAAKRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 271 HQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSvERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSgvaEGAKLECG 350
Cdd:cd07135 237 LWGKFGNAGQICVAPDYVLVDPSVYDEFVEEL-KKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT---TKGKVVIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 351 GKgLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGT 430
Cdd:cd07135 313 GE-MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGG 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 25777726 431 VWIN-------CYNAlnaqsPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:cd07135 392 VVINdtlihvgVDNA-----PFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
76-455 |
1.34e-53 |
|
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: 185.94 E-value: 1.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 76 DIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFY--------VDLQgvIKTF 147
Cdd:cd07095 1 QVDAAVAAARAAFP---GWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDIS--IKAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 148 RYYAGwaDKIHGMtipvdGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMG---- 223
Cdd:cd07095 76 HERTG--ERATPM-----AQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVelwe 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 224 --------------------ALIK-------------EVGKLI-QEAAGRSNlKRVTLELGGKSPNIIFADADLDYAVEQ 269
Cdd:cd07095 149 eaglppgvlnlvqggretgeALAAhegidgllftgsaATGLLLhRQFAGRPG-KILALEMGGNNPLVVWDVADIDAAAYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 270 AHQGVFFNQGQCCTAGSRIFVEESIY-EEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLE 348
Cdd:cd07095 228 IVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 349 CGGKGLGRKGFFIEPTVFsNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQA 428
Cdd:cd07095 308 LAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRA 386
|
410 420 430
....*....|....*....|....*....|
gi 25777726 429 GTVWINcyNALNAQS---PFGGFKMSGNGR 455
Cdd:cd07095 387 GIVNWN--RPTTGASstaPFGGVGLSGNHR 414
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
26-472 |
2.59e-53 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 189.19 E-value: 2.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 26 LPSPTPNLeikytkifINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLgsvWRRMDASERGRL 105
Cdd:PLN02419 110 MPPRVPNL--------IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL---WRNTPITTRQRV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 106 LDKLADLVERDRAVLATMESLNGGKPfLQAFYVDLQGVIKTFRYYAGWADKIHGMTIP-VDGDYFTFTRHEPIGVCGQII 184
Cdd:PLN02419 179 MLKFQELIRKNMDKLAMNITTEQGKT-LKDSHGDIFRGLEVVEHACGMATLQMGEYLPnVSNGVDTYSIREPLGVCAGIC 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 185 PWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEVG---------------------------------- 230
Cdd:PLN02419 258 PFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGlpdgvlnivhgtndtvnaicddediravsfvgsn 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 231 ----KLIQEAAGRSnlKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRI-FVEESiyEEFVRRSVER 305
Cdd:PLN02419 338 tagmHIYARAAAKG--KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVvFVGDA--KSWEDKLVER 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 306 AKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGL----GRKGFFIEPTVFSNVTDDMRIAKEEIF 381
Cdd:PLN02419 414 AKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIF 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 382 GPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCynALNAQSPFGGF-----KMSGNGRE 456
Cdd:PLN02419 494 GPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPFFSFtgnkaSFAGDLNF 571
|
490
....*....|....*.
gi 25777726 457 MGEFGLREYSEVKTVT 472
Cdd:PLN02419 572 YGKAGVDFFTQIKLVT 587
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
175-471 |
6.91e-53 |
|
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: 184.24 E-value: 6.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 175 EPIGVCGQIIPWNFPLLMfawKIAP---ALCCGNTVVIKPAEQTPLSALYMGALIKE----------------------- 228
Cdd:cd07136 99 EPYGVVLIIAPWNYPFQL---ALAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEEtfdeeyvavveggveenqelldq 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 229 ------------VGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYE 296
Cdd:cd07136 176 kfdyifftgsvrVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 297 EFVRRSVERAKRRVVGSPFDptTEQGPQI-DKKQYNKILELIQSGvaegaKLECGGKGlGRKGFFIEPTVFSNVTDDMRI 375
Cdd:cd07136 255 KFIKELKEEIKKFYGEDPLE--SPDYGRIiNEKHFDRLAGLLDNG-----KIVFGGNT-DRETLYIEPTILDNVTWDDPV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 376 AKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcyNAL----NAQSPFGGFKMS 451
Cdd:cd07136 327 MQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN--DTImhlaNPYLPFGGVGNS 404
|
330 340
....*....|....*....|
gi 25777726 452 GNGREMGEFGLREYSEVKTV 471
Cdd:cd07136 405 GMGSYHGKYSFDTFSHKKSI 424
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
170-474 |
1.46e-46 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 168.28 E-value: 1.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 170 TFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIK---------------------- 227
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTkyldpsyvrvieggvevttell 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 228 -------------EVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESI 294
Cdd:PTZ00381 183 kepfdhifftgspRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 295 YEEFVrRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSgvaEGAKLECGGKgLGRKGFFIEPTVFSNVTDDMR 374
Cdd:PTZ00381 262 KDKFI-EALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE-VDIENKYVAPTIIVNPDLDSP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 375 IAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSG 452
Cdd:PTZ00381 337 LMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGVGNSG 416
|
330 340
....*....|....*....|..
gi 25777726 453 NGREMGEFGLREYSEVKTVTVK 474
Cdd:PTZ00381 417 MGAYHGKYGFDTFSHPKPVLNK 438
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
48-454 |
1.75e-46 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 173.20 E-value: 1.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 48 NSESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESL 126
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFP---AWSATPVEERAAILERAADLLEAHRAELMALLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 127 NGGKPFL-------QAfyVDlqgviktF-RYYAGWADKIHGMTipvdgdyftfTRHEPIGVCGQIIPWNFPLLMFAWKIA 198
Cdd:COG4230 642 EAGKTLPdaiaevrEA--VD-------FcRYYAAQARRLFAAP----------TVLRGRGVFVCISPWNFPLAIFTGQVA 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 199 PALCCGNTVVIKPAEQTPLSALYM-------------------------GALIK-------------EVGKLIQEA-AGR 239
Cdd:COG4230 703 AALAAGNTVLAKPAEQTPLIAARAvrllheagvpadvlqllpgdgetvgAALVAdpriagvaftgstETARLINRTlAAR 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 240 SNlKRVTL--ELGGKspNIIFADADldyA-VEQAHQGV----FFNQGQCCTAgSRI-FVEESIYEEFVRRSVERAKRRVV 311
Cdd:COG4230 783 DG-PIVPLiaETGGQ--NAMIVDSS---AlPEQVVDDVlasaFDSAGQRCSA-LRVlCVQEDIADRVLEMLKGAMAELRV 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 312 GSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKL-ECGGKGLGRKGFFIEPTVFSnvTDDMRIAKEEIFGPVQEILRF 390
Cdd:COG4230 856 GDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLIE--IDSISDLEREVFGPVLHVVRY 933
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25777726 391 K--TMDEVIERANNSDFGLVAAVFT-NDiNKALTVSSAMQAGTVWINcYNALNA----QsPFGGFKMSGNG 454
Cdd:COG4230 934 KadELDKVIDAINATGYGLTLGVHSrID-ETIDRVAARARVGNVYVN-RNIIGAvvgvQ-PFGGEGLSGTG 1001
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
52-458 |
2.29e-46 |
|
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: 168.17 E-value: 2.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 52 GRVFPVYNPAT-GEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGK 130
Cdd:TIGR01238 50 GEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFP---TWNATPAKERAAKLDRLADLLELHMPELMALCVREAGK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 131 PFLQAFyVDLQGVIKTFRYYAGWADkihgmtipvdgDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIK 210
Cdd:TIGR01238 127 TIHNAI-AEVREAVDFCRYYAKQVR-----------DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 211 PAEQTPLSALYMGALIKEVG--------------------------------------KLIQEAAGRSNLKRVTL--ELG 250
Cdd:TIGR01238 195 PAEQTSLIAYRAVELMQEAGfpagtiqllpgrgadvgaaltsdpriagvaftgstevaQLINQTLAQREDAPVPLiaETG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 251 GKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQY 330
Cdd:TIGR01238 275 GQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 331 NKILELIQSGVAEG---AKLECGGKGLGRKGFFIEPTVFSnvTDDMRIAKEEIFGPVQEILRFKT--MDEVIERANNSDF 405
Cdd:TIGR01238 355 QNLLAHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGY 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 25777726 406 GLVAAVFTNDINKALTVSSAMQAGTVWIN--CYNALNAQSPFGGFKMSGNGREMG 458
Cdd:TIGR01238 433 GLTMGVHSRIETTYRWIEKHARVGNCYVNrnQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
41-475 |
3.37e-46 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 172.31 E-value: 3.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQN----SESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVER 115
Cdd:PRK11904 546 FLEKQWQAgpiiNGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFP---AWSRTPVEERAAILERAADLLEA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 116 DRAVLATMESLNGGKPfLQ--------AfyVDlqgviktF-RYYAGWADKIHGMTIPVDGdyftFT------RHEPIGV- 179
Cdd:PRK11904 623 NRAELIALCVREAGKT-LQdaiaevreA--VD-------FcRYYAAQARRLFGAPEKLPG----PTgesnelRLHGRGVf 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 180 -CgqIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPL----------------SALYM---------GALIK------ 227
Cdd:PRK11904 689 vC--ISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLiaaeavkllheagipkDVLQLlpgdgatvgAALTAdpriag 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 228 -------EVGKLIQEA-AGRSNlKRVTL--ELGGKspNIIFADAD------LDYAVEQAhqgvFFNQGQCCTAGSRIFVE 291
Cdd:PRK11904 767 vaftgstETARIINRTlAARDG-PIVPLiaETGGQ--NAMIVDSTalpeqvVDDVVTSA----FRSAGQRCSALRVLFVQ 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 292 ESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEG---AKLECGgkGLGRKGFFIEPTVFSn 368
Cdd:PRK11904 840 EDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLP--AGTENGHFVAPTAFE- 916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 369 vTDDMRIAKEEIFGPVQEILRFKT--MDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNA----Q 442
Cdd:PRK11904 917 -IDSISQLEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-RNQIGAvvgvQ 994
|
490 500 510
....*....|....*....|....*....|....*.
gi 25777726 443 sPFGGFKMSGNGREMGefG---LREYSEVKTVTVKI 475
Cdd:PRK11904 995 -PFGGQGLSGTGPKAG--GphyLLRFATEKTVTVNT 1027
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
41-473 |
4.78e-45 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 164.62 E-value: 4.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQnsESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAArlaFSLGSVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:PLN02315 24 YVGGEWR--ANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRAC---EEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKpFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVD-GDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAP 199
Cdd:PLN02315 99 GRLVSLEMGK-ILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSErPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 200 ALCCGNTVVIKPAEQTPLSALYMGALIKEV-----------------------------------------GKLIQEAAg 238
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknnlpgaiftsfcggaeigeaiakdtriplvsftgsskvGLMVQQTV- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 239 RSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 318
Cdd:PLN02315 257 NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 319 TEQGP---QIDKKQYNKILELIQSgvaEGAKLECGGKGLGRKGFFIEPTVFSnVTDDMRIAKEEIFGPVQEILRFKTMDE 395
Cdd:PLN02315 337 TLLGPlhtPESKKNFEKGIEIIKS---QGGKILTGGSAIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 396 VIERANNSDFGLVAAVFTND---INKALTVSSAmQAGTVWINC-YNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:PLN02315 413 AIEINNSVPQGLSSSIFTRNpetIFKWIGPLGS-DCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
..
gi 25777726 472 TV 473
Cdd:PLN02315 492 TI 493
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
49-454 |
6.21e-44 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 165.81 E-value: 6.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 49 SESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAFSlgsVWRRMDASERGRLLDKLADLVERDRAVLATMESLN 127
Cdd:PRK11905 563 DVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFP---EWSATPAAERAAILERAADLMEAHMPELFALAVRE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 128 GGKPFLQAF-----YVDlqgviktF-RYYAGWADkihgmtipvdgDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPAL 201
Cdd:PRK11905 640 AGKTLANAIaevreAVD-------FlRYYAAQAR-----------RLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAAL 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 202 CCGNTVVIKPAEQTPLSALY----M---------------------GALIK-------------EVGKLIQEA-AGRSNl 242
Cdd:PRK11905 702 VAGNTVLAKPAEQTPLIAARavrlLheagvpkdalqllpgdgrtvgAALVAdpriagvmftgstEVARLIQRTlAKRSG- 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 243 KRVTL--ELGGKSPNIIFADAdldyAVEQAHQGV----FFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFD 316
Cdd:PRK11905 781 PPVPLiaETGGQNAMIVDSSA----LPEQVVADViasaFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWR 856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 317 PTTEQGPQIDKKQYNKILELIQSGVAEGAKL-ECGGKGLGRKGFFIEPTVFSnvTDDMRIAKEEIFGPVQEILRFKT--M 393
Cdd:PRK11905 857 LSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhQLPLPAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKAdeL 934
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25777726 394 DEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINcYNALNA----QsPFGGFKMSGNG 454
Cdd:PRK11905 935 DRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN-RNIIGAvvgvQ-PFGGEGLSGTG 997
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
57-452 |
1.71e-42 |
|
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: 157.75 E-value: 1.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 57 VYNPATGEQVC---------EVQEADKADIDKAVQAARLAfslGSVWRRMDASERGRLLDKLADLVE---RDRAVLATMe 124
Cdd:cd07123 42 VRTGNTGKQVMphdhahvlaTYHYADAALVEKAIEAALEA---RKEWARMPFEDRAAIFLKAADLLSgkyRYELNAATM- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 125 sLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTiPVDGDYFTFTR--HEPI-GVCGQIIPWNFPLLMFAWKIAPAL 201
Cdd:cd07123 118 -LGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQ-PLSSPAGVWNRleYRPLeGFVYAVSPFNFTAIGGNLAGAPAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 202 CcGNTVVIKPAEQTPLSALYMGALIKEVG-------------KLIQEAAGRS---------------------------- 240
Cdd:cd07123 196 M-GNVVLWKPSDTAVLSNYLVYKILEEAGlppgvinfvpgdgPVVGDTVLASphlaglhftgstptfkslwkqigenldr 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 241 --NLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPT 318
Cdd:cd07123 275 yrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 319 TEQGPQIDKKQYNKILELIQSGVAE-GAKLECGGKGLGRKGFFIEPTVFsnVTDD--MRIAKEEIFGPVQEILRFKTMD- 394
Cdd:cd07123 355 NFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVI--ETTDpkHKLMTEEIFGPVLTVYVYPDSDf 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25777726 395 -EVIERANN-SDFGLVAAVFTND---INKALTVSSaMQAGTVWIN--CYNALNAQSPFGGFKMSG 452
Cdd:cd07123 433 eETLELVDTtSPYALTGAIFAQDrkaIREATDALR-NAAGNFYINdkPTGAVVGQQPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
79-474 |
2.47e-40 |
|
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: 150.45 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 79 KAVQAARLAFSLGsvwRRMDASERGRLLDKLADLVE--RDRAVLATMESLNggKPFLQAFYVDLQGVIKTFRY----YAG 152
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEFRIQQLEALLRMLEenEDEIVEALAKDLR--KPKFEAVLSEILLVKNEIKYaisnLPE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 153 WADkihgmTIPVDGDYFT-----FTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALI- 226
Cdd:cd07132 77 WMK-----PEPVKKNLATllddvYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 227 ----------------------------------KEVGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQ 272
Cdd:cd07132 152 kyldkecypvvlggveettellkqrfdyifytgsTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCDIDVAARRIAW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 273 GVFFNQGQCCTAGSRIFVEESIYEEFvrrsVERAKRRVV---GSpfDPTTEQ--GPQIDKKQYNKILELIQSG-VA---E 343
Cdd:cd07132 231 GKFINAGQTCIAPDYVLCTPEVQEKF----VEALKKTLKefyGE--DPKESPdyGRIINDRHFQRLKKLLSGGkVAiggQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 344 GAKLECggkglgrkgfFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTND---INKAL 420
Cdd:cd07132 305 TDEKER----------YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNkkvINKIL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 25777726 421 TVSSamqAGTVwinCYNALNAQS-----PFGGFKMSGNGREMGEFGLREYSEVKTVTVK 474
Cdd:cd07132 375 SNTS---SGGV---CVNDTIMHYtldslPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
17-454 |
8.02e-36 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 141.65 E-value: 8.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 17 AALMASLHLLPSPTPNLEikytkifinnewQNSESGRVFPVYNPA-TGEQVCEVQEADKADIDKAVQAARLAfslGSVWR 95
Cdd:PRK11809 635 SALLASAHQKWQAAPMLE------------DPVAAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNA---APIWF 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 96 RMDASERGRLLDKLADLVErdravlATMESLNG------GKPFLQAF-----YVDLqgviktFRYYAGWADkihgmtipv 164
Cdd:PRK11809 700 ATPPAERAAILERAADLME------AQMQTLMGllvreaGKTFSNAIaevreAVDF------LRYYAGQVR--------- 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 165 dgDYFTFTRHEPIG--VCgqIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYM-------------------- 222
Cdd:PRK11809 759 --DDFDNDTHRPLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAvrilleagvpagvvqllpgr 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 223 -----GALIK-------------EVGKLIQEA-AGR-SNLKRVT---LELGGKSPNIIFADADLDYAVEQAHQGVFFNQG 279
Cdd:PRK11809 835 getvgAALVAdarvrgvmftgstEVARLLQRNlAGRlDPQGRPIpliAETGGQNAMIVDSSALTEQVVADVLASAFDSAG 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 280 QCCTAGSRIFVEESIYEefvrRSVERAK----RRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAK---LECGGK 352
Cdd:PRK11809 915 QRCSALRVLCLQDDVAD----RTLKMLRgamaECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPvfqAARENS 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 353 GLGRKGFFIEPTVFS-NVTDDMriaKEEIFGPVQEILRFK--TMDEVIERANNSDFGLVAAVFTN-DINKALTVSSAmQA 428
Cdd:PRK11809 991 EDWQSGTFVPPTLIElDSFDEL---KREVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRiDETIAQVTGSA-HV 1066
|
490 500 510
....*....|....*....|....*....|
gi 25777726 429 GTVWINcYNALNA----QsPFGGFKMSGNG 454
Cdd:PRK11809 1067 GNLYVN-RNMVGAvvgvQ-PFGGEGLSGTG 1094
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
81-471 |
6.50e-32 |
|
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: 126.76 E-value: 6.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 81 VQAARLAFSLGsvwRRMDASERGRLLDKLADLV-ERDRAVLATMESlNGGKPFLQAFYVDLQGVIKT----FRYYAGWAD 155
Cdd:cd07137 5 VRELRETFRSG---RTRSAEWRKSQLKGLLRLVdENEDDIFAALRQ-DLGKPSAESFRDEVSVLVSScklaIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 156 ----KIHGMTIPVDGDYFTftrhEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKE--- 228
Cdd:cd07137 81 pekvKTPLTTFPAKAEIVS----EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEyld 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 229 --------------------------------VGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVF- 275
Cdd:cd07137 157 tkaikvieggvpettalleqkwdkifftgsprVGRIIMAAAAK-HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWg 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 276 FNQGQCCTAGSRIFVEESIYEEFVRrsverAKRRVVGSPF--DP-TTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGk 352
Cdd:cd07137 236 CNNGQACIAPDYVLVEESFAPTLID-----ALKNTLEKFFgeNPkESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGG- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 353 GLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNdiNKALT--VSSAMQAGT 430
Cdd:cd07137 310 ERDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTK--NKELKrrIVAETSSGG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 25777726 431 VWIN--CYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTV 471
Cdd:cd07137 388 VTFNdtVVQYAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
41-463 |
4.02e-27 |
|
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: 113.90 E-value: 4.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQnSESGRVFPVYNPATGEQVCEVQeADKADIDKAVQAARLAFslGSVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:cd07128 4 YVAGQWH-AGTGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYAREKG--GPALRALTFHERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKpfLQAFYVDLQGVIKTFRYYAGWADK--------IHGMTIPVDGDYFTFTRH--EPI-GVCGQIIPWNFP 189
Cdd:cd07128 80 YALSAATGAT--RRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLSKDGTFVGQHilTPRrGVAVHINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 190 llmfAW----KIAPALCCGNTVVIKPAEQTPLSALYMGALIKEVGKL----IQEAAG--RSNLKRVT----------LEL 249
Cdd:cd07128 158 ----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLLpegaLQLICGsvGDLLDHLGeqdvvaftgsAAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 250 GGK---SPNII------FADAD-LDYAV--EQAHQG-----VFFNQ---------GQCCTAGSRIFVEESIYEEFVRRSV 303
Cdd:cd07128 234 AAKlraHPNIVarsirfNAEADsLNAAIlgPDATPGtpefdLFVKEvaremtvkaGQKCTAIRRAFVPEARVDAVIEALK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 304 ERAKRRVVGSPFDPTTEQGPQIDKKQYN----KILELIQSG-VAEGAKLECGGKGLGR-KGFFIEPTVF-SNVTDDMRIA 376
Cdd:cd07128 314 ARLAKVVVGDPRLEGVRMGPLVSREQREdvraAVATLLAEAeVVFGGPDRFEVVGADAeKGAFFPPTLLlCDDPDAATAV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 377 KE-EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQA--GTVWINcyNALNAQ------SPF-- 445
Cdd:cd07128 394 HDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVL--NRDSAKestghgSPLpq 471
|
490 500
....*....|....*....|.
gi 25777726 446 ---GGFKMSGNGREMGefGLR 463
Cdd:cd07128 472 lvhGGPGRAGGGEELG--GLR 490
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
41-463 |
4.61e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 114.03 E-value: 4.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQnSESGRVFPVYNPATGEQVCEVqEADKADIDKAVQAARLafSLGSVWRRMDASERGRLLDKLADLVERDRAVL 120
Cdd:PRK11903 8 YVAGRWQ-AGSGAGTPLFDPVTGEELVRV-SATGLDLAAAFAFARE--QGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 121 ATMESLNGGKPFLQAfYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPI----------GVCGQIIPWNFPl 190
Cdd:PRK11903 84 YDIATANSGTTRNDS-AVDIDGGIFTLGYYAKLGAALGDARLLRDGEAVQLGKDPAFqgqhvlvptrGVALFINAFNFP- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 191 lmfAW----KIAPALCCGNTVVIKPAEQTPLSALYMGALIKEVGKL------------------IQE------------- 235
Cdd:PRK11903 162 ---AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGILpagalsvvcgssaglldhLQPfdvvsftgsaeta 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 236 AAGRSNLK------RVTLELGGKSPNIIFADAD-----LDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVE 304
Cdd:PRK11903 239 AVLRSHPAvvqrsvRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 305 RAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQsGVAEGAKLECGGKGLG------RKGFFIEPTVF-SNVTDDMRIAK 377
Cdd:PRK11903 319 RLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLgASDPDAATAVH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 378 E-EIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDI--------------NKALTVSSAMQA-----GTVWincyn 437
Cdd:PRK11903 398 DvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAaflaaaaleladshGRVHVISPDVAAlhtghGNVM----- 472
|
490 500
....*....|....*....|....*.
gi 25777726 438 alnAQSPFGGFKMSGNGREMGefGLR 463
Cdd:PRK11903 473 ---PQSLHGGPGRAGGGEELG--GLR 493
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
82-454 |
5.01e-25 |
|
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: 107.32 E-value: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 82 QAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFyvDLQGVIKTFRYYA--GWADKIHG 159
Cdd:cd07084 3 RALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE--NICGDQVQLRARAfvIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 160 MTIPVDGDYFTFTRHE---PIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEVGKLIQE- 235
Cdd:cd07084 81 EPGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPEd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 236 --------------------------------AAGRSNLK--RVTLELGGKSPNIIFADAD-LDYAVEQAHQGVFFNQGQ 280
Cdd:cd07084 161 vtlingdgktmqalllhpnpkmvlftgssrvaEKLALDAKqaRIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 281 CCTAGSRIFVEESIY-EEFVRRSVERAKRRVVGspfdpTTEQGPQidkkQYNKILELIQSGVAE-GAKLECGGKGLGRK- 357
Cdd:cd07084 241 KCTAQSMLFVPENWSkTPLVEKLKALLARRKLE-----DLLLGPV----QTFTTLAMIAHMENLlGSVLLFSGKELKNHs 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 358 -----GFFIEPTVFSNVTDDMRIAK---EEIFGPVQEILRFK-----TMDEVIERANNSdfgLVAAVFTNDInkalTVSS 424
Cdd:cd07084 312 ipsiyGACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKkdqlaLVLELLERMHGS---LTAAIYSNDP----IFLQ 384
|
410 420 430
....*....|....*....|....*....|
gi 25777726 425 AMqAGTVWINCYNALNAQSPFGGFKMSGNG 454
Cdd:cd07084 385 EL-IGNLWVAGRTYAILRGRTGVAPNQNHG 413
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
175-472 |
1.06e-21 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 97.49 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 175 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALI---------------------------- 226
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIpkyldskavkvieggpavgeqllqhkwd 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 227 -------KEVGKLIQEAAGRsNLKRVTLELGGKSPNI---IFADADLDYAVEQAHQGVFFN-QGQCCTAGSRIFVEEsiy 295
Cdd:PLN02203 187 kifftgsPRVGRIIMTAAAK-HLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEE--- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 296 eEFVRRSVERAK---RRVVGSPFDPTTEQGPQIDKKQYNKILEL-----IQSGVAEGAKLEcggkglgRKGFFIEPTVFS 367
Cdd:PLN02203 263 -RFAPILIELLKstiKKFFGENPRESKSMARILNKKHFQRLSNLlkdprVAASIVHGGSID-------EKKLFIEPTILL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 368 NVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN---CYNALNAqSP 444
Cdd:PLN02203 335 NPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNdaiIQYACDS-LP 413
|
330 340
....*....|....*....|....*...
gi 25777726 445 FGGFKMSGNGREMGEFGLREYSEVKTVT 472
Cdd:PLN02203 414 FGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
175-471 |
2.29e-20 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 93.57 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 175 EPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKE-------------------------- 228
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQyldssavrvvegavtettalleqkwd 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 229 ---------VGKLIQEAAGRsNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVF-FNQGQCCTAGSRIFVEESiYEEF 298
Cdd:PLN02174 191 kifytgsskIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKE-YAPK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 299 VRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELI-QSGVAEgaKLECGGKGlGRKGFFIEPTVFSNVTDDMRIAK 377
Cdd:PLN02174 269 VIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLdEKEVSD--KIVYGGEK-DRENLKIAPTILLDVPLDSLIMS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 378 EEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWIN---CYNALNAQsPFGGFKMSGNG 454
Cdd:PLN02174 346 EEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiaVHLALHTL-PFGGVGESGMG 424
|
330
....*....|....*..
gi 25777726 455 REMGEFGLREYSEVKTV 471
Cdd:PLN02174 425 AYHGKFSFDAFSHKKAV 441
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
41-417 |
6.22e-11 |
|
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: 64.44 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 41 FINNEWQNSESGRVFPvyNPATGEQVCEVQEADKADIDKAVQAARlAFSLGSVWRRMDASER----GRLLDKLADLVERD 116
Cdd:cd07126 2 LVAGKWKGASNYTTLL--DPLNGDKFISVPDTDEDEINEFVDSLR-QCPKSGLHNPLKNPERyllyGDVSHRVAHELRKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 117 RA--VLATMESLNGGKPFLQAfyvdLQGVIKTFRYYAGWA-DKIHGMT--IPVDGDYFTFTRHE---PIGVCGQIIPWNF 188
Cdd:cd07126 79 EVedFFARLIQRVAPKSDAQA----LGEVVVTRKFLENFAgDQVRFLArsFNVPGDHQGQQSSGyrwPYGPVAIITPFNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 189 PLLMFAWKIAPALCCGNTVVIKP-------AEQTPLSALYMGA------LI----KEVGKLIQEAAGRSNL--------K 243
Cdd:cd07126 155 PLEIPALQLMGALFMGNKPLLKVdskvsvvMEQFLRLLHLCGMpatdvdLIhsdgPTMNKILLEANPRMTLftgsskvaE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 244 RVTLELGGKspnIIFADA------------DLDYAVEQAHQGVFFNQGQCCTAGSRIFVEES-IYEEFVRRSVERAKRR- 309
Cdd:cd07126 235 RLALELHGK---VKLEDAgfdwkilgpdvsDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALAEQRk 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 310 ----VVGSPFDPTTEqgpqidkkqynKILELIQSGVA-EGAKLECGGKGLGRKGF-----FIEPT-VF-----SNVTDDM 373
Cdd:cd07126 312 ledlTIGPVLTWTTE-----------RILDHVDKLLAiPGAKVLFGGKPLTNHSIpsiygAYEPTaVFvpleeIAIEENF 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 25777726 374 RIAKEEIFGPVQEILRFK--TMDEVIERANNSDFGLVAAVFTNDIN 417
Cdd:cd07126 381 ELVTTEVFGPFQVVTEYKdeQLPLVLEALERMHAHLTAAVVSNDIR 426
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
171-310 |
3.34e-03 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 39.73 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 171 FTRHEPIGVCGQIIPWNFPLLMFaWKIAPALCCGNTVVIKPAEQTP----------------------LSALYMGALIKE 228
Cdd:pfam05893 83 YEKAFPPGLVFHVLSGNVPLLPV-MSILMGLLVKNVNLLKVSSSDPftaaallasfadldpthpladsLSVVYWDGGSTQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25777726 229 VGKLIQEAA-------GRSNLKRVTLELGGKSPNIIFA----------DADLDYAVEQ-AHQGVFFNQgQCCTAGSRIFV 290
Cdd:pfam05893 162 LEDLIVANAdvviawgGEDAINAIRECLKPGKQWIDFGakisfavvdrEAALDKAAERaADDICVFDQ-QACLSPQTVFV 240
|
170 180
....*....|....*....|....*.
gi 25777726 291 E---ESIYEEFVRR---SVERAKRRV 310
Cdd:pfam05893 241 EsddKITPDEFAERlaaALAKRARIL 266
|
|
| |
