|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
27-435 |
0e+00 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 668.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 27 SYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTMD 106
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 107 IPRSVQNFRFFASSSLHHTSECTQMDHlGCMHYTVR-------------------------------------------- 142
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDG-GALNYVLRqpvgvaglitpwnlplmlltwkiapalafgntvvlkpsewtplt 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 143 APVGVGVPPGV------VNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDA 216
Cdd:cd07093 160 AWLLAELANEAglppgvVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 217 NLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRAL 296
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 297 AEGAQIWCGEGVDKLSlpaRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSS 376
Cdd:cd07093 320 AEGATILTGGGRPELP---DLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 301500698 377 NVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
10-437 |
7.39e-174 |
|
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: 495.42 E-value: 7.39e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 10 LENFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEF 87
Cdd:COG1012 6 YPLFIGGEWVAAASgeTFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 88 AQAESKDQGKTLALARtMDIPRSVQNFRFFASSSLHHTSECTQMDHLGCMHYTVR------------------------- 142
Cdd:COG1012 86 AALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRReplgvvgaitpwnfplalaawklap 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 143 ------------APVGVGVPPGVV-------------NIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC 197
Cdd:COG1012 165 alaagntvvlkpAEQTPLSALLLAelleeaglpagvlNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 198 KKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIG 277
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 278 ALISKAHLEKVRSYVKRALAEGAQIWCGeGVdklslPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEE 357
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGAELLTG-GR-----RPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 358 VIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLI-RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITVK 436
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
.
gi 301500698 437 H 437
Cdd:COG1012 479 L 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
20-433 |
1.01e-164 |
|
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: 471.25 E-value: 1.01e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 20 PCSSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTL 99
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 100 ALARTmDIPRSVQNFRFFASSSLHHTSECTQMDHlGCMHYTVR------------------------------------- 142
Cdd:pfam00171 84 AEARG-EVDRAIDVLRYYAGLARRLDGETLPSDP-GRLAYTRReplgvvgaitpwnfplllpawkiapalaagntvvlkp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 143 APVGVGVPPGVV-------------NIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNP 209
Cdd:pfam00171 162 SELTPLTALLLAelfeeaglpagvlNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 210 AIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVR 289
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 290 SYVKRALAEGAQIWCGeGvdklslPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGL 369
Cdd:pfam00171 322 KYVEDAKEEGAKLLTG-G------EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301500698 370 AATVWSSNVGRVHRVAKKLQSGLVWTNCWLI-RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTgDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
48-435 |
1.91e-144 |
|
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: 418.92 E-value: 1.91e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 48 EAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTmDIPRSVQNFRFFASSSLHHTSE 127
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 128 CTQMDHLGCMHYTVR-------------------------------------APVGVGVPPGVV-------------NIV 157
Cdd:cd07078 80 VIPSPDPGELAIVRReplgvvgaitpwnfplllaawklapalaagntvvlkpSELTPLTALLLAellaeaglppgvlNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 158 FGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEIC 237
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 238 LCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDKlslparN 317
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLE------G 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 318 QAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNC 397
Cdd:cd07078 314 GKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIND 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 301500698 398 WLI-RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07078 394 YSVgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
27-435 |
3.84e-134 |
|
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: 393.45 E-value: 3.84e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 27 SYDPSTGEVYCRVPNSGKDEIEAAVKAAREAF--PSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALART 104
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 105 MdIPRSVQNFRFFASSSLHHTSECTQMDHLGCMHYTVR------------------------------------------ 142
Cdd:cd07114 81 Q-VRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRReplgvvaaitpwnspllllakklapalaagntvvlkpsehtp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 143 APVGVGVPPGVV--------NIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFE 214
Cdd:cd07114 160 ASTLELAKLAEEagfppgvvNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 215 DANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKR 294
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 295 ALAEGAQIWCGEGVDKLslpARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVW 374
Cdd:cd07114 320 AREEGARVLTGGERPSG---ADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIW 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301500698 375 SSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07114 397 TRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
13-435 |
1.02e-133 |
|
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: 393.11 E-value: 1.02e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSR--SPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07091 7 FINNEFVDSVSgkTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRkmDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESKDQGKTLALARTMDIPRSVQNFRFFA-----------SSSLHH--------------------------------- 124
Cdd:cd07091 87 ALESLDNGKPLEESAKGDVALSIKCLRYYAgwadkiqgktiPIDGNFlaytrrepigvcgqiipwnfpllmlawklapal 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 125 ---------TSECTQMDHLgcmhYTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA- 194
Cdd:cd07091 167 aagntvvlkPAEQTPLSAL----YLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 195 PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLV 274
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 275 SIGALISKAHLEKVRSYVKRALAEGAQIWCGEGvdklslpARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 354
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGE-------RHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 355 EEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 434
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
|
.
gi 301500698 435 V 435
Cdd:cd07091 476 I 476
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
28-435 |
6.69e-131 |
|
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: 384.86 E-value: 6.69e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARtMDI 107
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 108 PRSVQNFRFFA------------SSSLHHT------------------------------------------SECTQMdh 133
Cdd:cd07103 81 DYAASFLEWFAeearriygrtipSPAPGKRilvikqpvgvvaaitpwnfpaamitrkiapalaagctvvlkpAEETPL-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 134 lgCMHYTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIF 213
Cdd:cd07103 159 --SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 214 EDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVK 293
Cdd:cd07103 237 DDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 294 RALAEGAQIWCGEGVDKLslparnqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATV 373
Cdd:cd07103 317 DAVAKGAKVLTGGKRLGL-------GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301500698 374 WSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07103 390 FTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
28-435 |
1.67e-125 |
|
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: 371.25 E-value: 1.67e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARtMDI 107
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 108 PRSVQNFRFFA--SSSLHhtSECTQMDHlGCMHYTVR------------------------------------------- 142
Cdd:cd07090 81 DSSADCLEYYAglAPTLS--GEHVPLPG-GSFAYTRReplgvcagigawnypiqiaswksapalacgnamvykpspftpl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 143 -------APVGVGVPPGVVNIVFGTGpRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFED 215
Cdd:cd07090 158 talllaeILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 216 ANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRA 295
Cdd:cd07090 237 ADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 296 LAEGAQIWCGEGVDKLSLPARNqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWS 375
Cdd:cd07090 317 KQEGAKVLCGGERVVPEDGLEN--GFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 376 SNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
11-435 |
5.23e-121 |
|
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: 360.89 E-value: 5.23e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 11 ENFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07559 2 DNFINGEWVAPSKgeYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESKDQGKTLALARTMDIPRSVQNFRFFASS----------------SLH----------------------------- 123
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGViraqegslseidedtlSYHfheplgvvgqiipwnfpllmaawklapal 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 124 --------HTSECTQMDHLGCMHytvraPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAP 195
Cdd:cd07559 162 aagntvvlKPASQTPLSILVLME-----LIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 196 HCKKLSLELGGKNPAIIFEDAN------LDECIPATVRSSFaNQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIP 269
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAMdadddfDDKAEEGQLGFAF-NQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 270 SDPLVSIGALISKAHLEKVRSYVKRALAEGAQIWCGEgvDKLSLPArNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCV 349
Cdd:cd07559 316 LDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGG--ERLTLGG-LDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 350 VPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTE 429
Cdd:cd07559 393 ITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQ 472
|
....*.
gi 301500698 430 IKTITV 435
Cdd:cd07559 473 TKNILV 478
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-434 |
1.28e-119 |
|
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: 356.81 E-value: 1.28e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 12 NFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQ 89
Cdd:cd07138 1 FYIDGAWVAPAGteTIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 90 AESKDQGKTLALARTMDIPRSVQNFRFFASSS-------------------------------LHHT------------- 125
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALkdfefeerrgnslvvrepigvcglitpwnwpLNQIvlkvapalaagct 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 126 -----SECTQMDHLG---CMHYT-----VrapvgvgvppgvVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQL 192
Cdd:cd07138 161 vvlkpSEVAPLSAIIlaeILDEAglpagV------------FNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 193 SAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDP 272
Cdd:cd07138 229 AADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 273 LVSIGALISKAHLEKVRSYVKRALAEGAQIWCGeGVDKlslPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPF 352
Cdd:cd07138 309 ATTLGPLASAAQFDRVQGYIQKGIEEGARLVAG-GPGR---PEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 353 DSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNcWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKT 432
Cdd:cd07138 385 DDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKS 463
|
..
gi 301500698 433 IT 434
Cdd:cd07138 464 IQ 465
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
26-433 |
2.98e-119 |
|
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: 355.76 E-value: 2.98e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 26 DSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPS--WSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALAR 103
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 104 TMDIPRSVQNFRFFASS--SLHHTSECTQMDHLGCMHY------------------------------------------ 139
Cdd:cd07112 85 AVDVPSAANTFRWYAEAidKVYGEVAPTGPDALALITReplgvvgavvpwnfpllmaawkiapalaagnsvvlkpaeqsp 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 140 --TVRAPVGVGVP---PGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA-PHCKKLSLELGGKNPAIIF 213
Cdd:cd07112 165 ltALRLAELALEAglpAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNLKRVWLECGGKSPNIVF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 214 EDA-NLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYV 292
Cdd:cd07112 245 ADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 293 KRALAEGAQIWCGEGVDKLslparNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAAT 372
Cdd:cd07112 325 ESGKAEGARLVAGGKRVLT-----ETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301500698 373 VWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
28-435 |
3.79e-119 |
|
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: 355.10 E-value: 3.79e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTMDI 107
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 108 PRSVQNFRFFASSSLH------------HTSE--------CTQMD-----------------HLGCmhyTV--------- 141
Cdd:cd07092 82 PGAVDNFRFFAGAARTlegpaageylpgHTSMirrepigvVAQIApwnyplmmaawkiapalAAGN---TVvlkpsettp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 142 ------RAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFED 215
Cdd:cd07092 159 lttlllAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 216 ANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRA 295
Cdd:cd07092 239 ADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 296 lAEGAQIWCGEGvdklSLPARnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWS 375
Cdd:cd07092 319 -PAHARVLTGGR----RAEGP---GYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWT 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 376 SNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07092 391 RDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
13-433 |
1.23e-117 |
|
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: 352.00 E-value: 1.23e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPS--WSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07119 1 YIDGEWVEAASgkTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESKDQGKTLALARTmDIPRSVQNFRFFA------------------SSSLHH-TSECTQMD----------------- 132
Cdd:cd07119 81 RLETLNTGKTLRESEI-DIDDVANCFRYYAglatketgevydvpphviSRTVREpVGVCGLITpwnypllqaawklapal 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 133 HLGC-------------MHYTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK 199
Cdd:cd07119 160 AAGNtvvikpsevtpltTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 200 LSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGAL 279
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 280 ISKAHLEKVRSYVKRALAEGAQIWCGegvDKLSLPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVI 359
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCG---GKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 301500698 360 ERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:cd07119 397 RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
8-437 |
3.16e-117 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 350.75 E-value: 3.16e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 8 LMLENFIDGKFLPCS-SYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEE 86
Cdd:PRK13473 1 MQTKLLINGELVAGEgEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 87 FAQAESKDQGKTLALARTMDIPRSVQNFRFFASSSLH------------HTS---------------------------- 126
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARClegkaageylegHTSmirrdpvgvvasiapwnyplmmaawkla 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 127 --------------ECTQMDHLgcmhyTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQL 192
Cdd:PRK13473 161 palaagntvvlkpsEITPLTAL-----KLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 193 SAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDP 272
Cdd:PRK13473 236 AADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 273 LVSIGALISKAHLEKVRSYVKRALAEG-AQIWCGEGvdklslpARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVP 351
Cdd:PRK13473 316 DTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGE-------APDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 352 FDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCW--LIRElnLPFGGMKSSGIGREGAKDSYDFFTE 429
Cdd:PRK13473 389 FDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHfmLVSE--MPHGGQKQSGYGKDMSLYGLEDYTV 466
|
....*...
gi 301500698 430 IKTITVKH 437
Cdd:PRK13473 467 VRHVMVKH 474
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
12-435 |
1.09e-116 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 349.95 E-value: 1.09e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 12 NFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQ 89
Cdd:PRK13252 9 LYIDGAYVEATSgeTFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 90 AESKDQGKTLALARTMDIPRSVQNFRFFA--------------SSSLHHT------------------------------ 125
Cdd:PRK13252 89 LETLDTGKPIQETSVVDIVTGADVLEYYAglapalegeqiplrGGSFVYTrreplgvcagigawnypiqiacwksapala 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 126 ---------SECTQmdhLGCMH----YT-------VrapvgvgvppgvVNIVFGTGpRVGEALVSHPEVPLISFTGSQPT 185
Cdd:PRK13252 169 agnamifkpSEVTP---LTALKlaeiYTeaglpdgV------------FNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 186 AERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWK 265
Cdd:PRK13252 233 GKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 266 VGIPSDPLVSIGALISKAHLEKVRSYVKRALAEGAQIWC-GEGVDklslPARNQAGYFMLPTVITDIKDEsccMT---EE 341
Cdd:PRK13252 313 IGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCgGERLT----EGGFANGAFVAPTVFTDCTDD---MTivrEE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 342 IFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAK 421
Cdd:PRK13252 386 IFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGI 465
|
490
....*....|....
gi 301500698 422 DSYDFFTEIKTITV 435
Cdd:PRK13252 466 ATLEHYTQIKSVQV 479
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
29-435 |
7.60e-116 |
|
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: 346.73 E-value: 7.60e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 29 DPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTMDIP 108
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 109 RSVQNFRFFASSSLHHTSECTQMDHlGCMHYTVRA--------------------------------------------- 143
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRG-PFLNYTVREpvgvvgaivpwnfplmfaawkvapalaagntvvlkpaeltplsal 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 144 -----PVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANL 218
Cdd:cd07115 162 riaelMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 219 DECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAE 298
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 299 GAQIWC-GEGVDklslparnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSN 377
Cdd:cd07115 322 GARLLTgGKRPG--------ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 301500698 378 VGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07115 394 LGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
27-435 |
1.18e-113 |
|
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: 341.14 E-value: 1.18e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 27 SYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSR-SPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTm 105
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 106 DIPRSVQNFRFFASS--SLHHTSECTQMDHLGcmhYTVR----------------------------------------- 142
Cdd:cd07109 80 DVEAAARYFEYYGGAadKLHGETIPLGPGYFV---YTVRephgvtghiipwnyplqitgrsvapalaagnavvvkpaeda 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 143 ---------APVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIF 213
Cdd:cd07109 157 pltalrlaeLAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 214 EDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLvSIGALISKAHLEKVRSYVK 293
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDP-DLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 294 RALAEGAQIWCGEGVdklsLPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATV 373
Cdd:cd07109 316 RARARGARIVAGGRI----AEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301500698 374 WSSNVGRVHRVAKKLQSGLVWTNCWLIRE-LNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNYGAGGgIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
28-435 |
4.24e-113 |
|
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: 339.12 E-value: 4.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARtMDI 107
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ-FEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 108 PRSVQNFRFFASSSL---------HHTSEcTQMDHLG---------------------------CM-----HYTVRAPVG 146
Cdd:cd07106 81 GGAVAWLRYTASLDLpdeviedddTRRVE-LRRKPLGvvaaivpwnfplllaawkiapallagnTVvlkpsPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 147 VGVPPGVV------NIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDE 220
Cdd:cd07106 160 LGELAQEVlppgvlNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 221 CIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAEGA 300
Cdd:cd07106 239 VAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 301 QIWCGEGVDklslparNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGR 380
Cdd:cd07106 319 KVLAGGEPL-------DGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 301500698 381 VHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
30-435 |
1.87e-110 |
|
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: 332.77 E-value: 1.87e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 30 PSTGEVYCRVPNSGKDEIEAAVKAAREAFPS--WSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTmDI 107
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 108 PRSVQNFRFFASSS--LH---HT-------------------------------------------------SECTQMDH 133
Cdd:cd07118 83 EGAADLWRYAASLArtLHgdsYNnlgddmlglvlrepigvvgiitpwnfpflilsqklpfalaagctvvvkpSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 134 LGCMHYTVRAPVGVGVPpgvvNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIF 213
Cdd:cd07118 163 LMLAELLIEAGLPAGVV----NIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 214 EDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVK 293
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 294 RALAEGAQIWCGEGVdklslpARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATV 373
Cdd:cd07118 319 AGRAEGATLLLGGER------LASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301500698 374 WSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07118 393 WSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
11-433 |
1.71e-109 |
|
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: 331.14 E-value: 1.71e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 11 ENFIDGKFLPCSSYIDSYDPS-TGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQ 89
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 90 AESKDQGKTLALARTmDIPRSVQNFRFFASSSLHHTSECTQMDHLGCMHYTVR--------------------------- 142
Cdd:cd07097 82 LLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTReplgvvglitpwnfpiaipawkiapal 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 143 ----------APVGVGVPPGVV-------------NIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK 199
Cdd:cd07097 161 aygntvvfkpAELTPASAWALVeileeaglpagvfNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 200 LSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGAL 279
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 280 ISKAHLEKVRSYVKRALAEGAQIWCGeGvDKLSLPARnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVI 359
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGAKLVYG-G-ERLKRPDE---GYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEAL 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301500698 360 ERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIR-ELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTI 433
Cdd:cd07097 396 AIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGvDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
29-434 |
2.27e-109 |
|
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: 330.08 E-value: 2.27e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 29 DPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArTMDIP 108
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 109 RSVQNFRFFAS----------SSLHHTSE--------------------------------------CT------QMDHL 134
Cdd:cd07110 82 DVAGCFEYYADlaeqldakaeRAVPLPSEdfkarvrrepvgvvglitpwnfpllmaawkvapalaagCTvvlkpsELTSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 135 GCMHYTvRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFE 214
Cdd:cd07110 162 TELELA-EIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 215 DANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKR 294
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 295 ALAEGAQIWCGEGVdklslPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVW 374
Cdd:cd07110 321 GKEEGARLLCGGRR-----PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 375 SSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 434
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
29-435 |
7.02e-108 |
|
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: 326.24 E-value: 7.02e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 29 DPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLalaRTMDIP 108
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNAL---RTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 109 R---SVQNFRFFASSSLHHTSEcTQMDHLGCMHYTVR------------------------------------------- 142
Cdd:cd07108 80 EaavLADLFRYFGGLAGELKGE-TLPFGPDVLTYTVReplgvvgailpwnaplmlaalkiapalvagntvvlkaaedapl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 143 ------APVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDA 216
Cdd:cd07108 159 avlllaEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 217 NLDECIPATVRSS-FANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVK-- 293
Cdd:cd07108 239 DLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDlg 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 294 RALAEGAQIWCGegvdKLSLPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATV 373
Cdd:cd07108 319 LSTSGATVLRGG----PLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301500698 374 WSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSY-DFFTEIKTITV 435
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMlEHFTQKKTVNI 457
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
13-435 |
1.50e-106 |
|
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: 323.64 E-value: 1.50e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQA 90
Cdd:cd07117 4 FINGEWVKGSSgeTIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 91 ESKDQGKTLALARTMDIPRSVQNFRFFAS--------------------------------------------------- 119
Cdd:cd07117 84 ETLDNGKPIRETRAVDIPLAADHFRYFAGviraeegsanmidedtlsivlrepigvvgqiipwnfpflmaawklapalaa 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 120 --SSLHHTSECTQMDHLGCMHytvraPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC 197
Cdd:cd07117 164 gnTVVIKPSSTTSLSLLELAK-----IIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 198 KKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIG 277
Cdd:cd07117 239 IPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 278 ALISKAHLEKVRSYVKRALAEGAQIWCGegvDKLSLPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEE 357
Cdd:cd07117 319 AQVNKDQLDKILSYVDIAKEEGAKILTG---GHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 301500698 358 VIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07117 396 VIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
13-435 |
2.90e-106 |
|
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: 323.21 E-value: 2.90e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCS--SYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSR-SPQERSRVLNQVADLLEQSLEEFAQ 89
Cdd:cd07144 11 FINNEFVKSSdgETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 90 AESKDQGKTLALARTMDIPRSVQNFRFFASS------------------SLHH--------------------------- 124
Cdd:cd07144 91 IEALDSGKPYHSNALGDLDEIIAVIRYYAGWadkiqgktiptspnklayTLHEpygvcgqiipwnyplamaawklapala 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 125 --------TSECTQMDHLgcmhYTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPH 196
Cdd:cd07144 171 agntvvikPAENTPLSLL----YFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 197 CKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRK-WKVGIPSDPLVS 275
Cdd:cd07144 247 LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 276 IGALISKAHLEKVRSYVKRALAEGAQIWCGEgvdkLSLPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 355
Cdd:cd07144 327 VGPQVSKTQYDRVLSYIEKGKKEGAKLVYGG----EKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 356 EEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
13-433 |
3.56e-105 |
|
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: 320.21 E-value: 3.56e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFP--SWSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07142 7 FINGQFVDAASgkTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESKDQGKTLALARTMDIPRSVQNFRFFA------------------SSSLHH-------------------------- 124
Cdd:cd07142 87 ALETWDNGKPYEQARYAEVPLAARLFRYYAgwadkihgmtlpadgphhVYTLHEpigvvgqiipwnfpllmfawkvgpal 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 125 ---------TSECTQMDHLgcmhYTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA- 194
Cdd:cd07142 167 acgntivlkPAEQTPLSAL----LAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 195 PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLV 274
Cdd:cd07142 243 SNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 275 SIGALISKAHLEKVRSYVKRALAEGAQIWCGEGvdklslpARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 354
Cdd:cd07142 323 EQGPQVDKEQFEKILSYIEHGKEEGATLITGGD-------RIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKT 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 301500698 355 EEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:cd07142 396 VDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
13-433 |
6.42e-105 |
|
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: 319.21 E-value: 6.42e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQA 90
Cdd:cd07088 1 YINGEFVPSSSgeTIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 91 ESKDQGKTLALARtMDIPRSVQNFRFFASSSLHHTSECTQMD----HL-------------------------------- 134
Cdd:cd07088 81 IVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDrpneNIfifkvpigvvagilpwnfpffliarklapalv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 135 -GCmhyTV----------------RAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC 197
Cdd:cd07088 160 tGN---TIvikpseetplnalefaELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 198 KKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIG 277
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 278 ALISKAHLEKVRSYVKRALAEGAQIWCGEGvdklslPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEE 357
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGK------RPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDE 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301500698 358 VIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:cd07088 391 AIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
13-433 |
7.60e-105 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 320.23 E-value: 7.60e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFP--SWSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:PLN02766 24 FINGEFVDAASgkTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESKDQGKTLALARTMDIPRSVQNFRFFASSSLHHTSECTQMDHlGCMHYTVRA------------------------- 143
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSR-QLQGYTLKEpigvvghiipwnfpstmffmkvapa 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 144 -------------------------PVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA-PHC 197
Cdd:PLN02766 183 laagctmvvkpaeqtplsalfyahlAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAtSNL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 198 KKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIG 277
Cdd:PLN02766 263 KQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 278 ALISKAHLEKVRSYVKRALAEGAQIWCGegvdklSLPARNQaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEE 357
Cdd:PLN02766 343 PQVDKQQFEKILSYIEHGKREGATLLTG------GKPCGDK-GYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301500698 358 VIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
13-435 |
4.84e-104 |
|
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: 316.82 E-value: 4.84e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPS--WSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07139 2 FIGGRWVAPSGseTIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESKDQGKTLALARTMDIPRSVQNFRFFASSSLHHTSECTQ----MDHL------------------------------ 134
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRpgsgGGHVlvrrepvgvvaaivpwnaplflaalkiapa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 135 ---GCmhyTV----------------RAPVGVGVPPGVVNIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAP 195
Cdd:cd07139 162 laaGC---TVvlkpspetpldayllaEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 196 HCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVS 275
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 276 IGALISKAHLEKVRSYVKRALAEGAQIWCGEGVdklslPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 355
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGGR-----PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 356 EEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNcWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07139 393 DDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
28-433 |
5.88e-103 |
|
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: 313.80 E-value: 5.88e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWS-SRSPQERSRVLNQVADLLEQSLEEFA---QAESkdqGKTLALAR 103
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRallVAEV---GAPVMTAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 104 TMDIPRSVQNFRFFASSSLHHTSECT---QMDHLGCMHYTV--------------------------------------- 141
Cdd:cd07089 79 AMQVDGPIGHLRYFADLADSFPWEFDlpvPALRGGPGRRVVrrepvgvvaaitpwnfpfflnlaklapalaagntvvlkp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 142 ------------RAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNP 209
Cdd:cd07089 159 apdtplsalllgEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 210 AIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVR 289
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 290 SYVKRALAEGAQIWCGEGVdklslPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGL 369
Cdd:cd07089 319 GYIARGRDEGARLVTGGGR-----PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 301500698 370 AATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:cd07089 394 SGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-437 |
1.35e-102 |
|
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: 313.52 E-value: 1.35e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 12 NFIDGKFLPCSS--YIDSYDPSTG-EVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07131 1 NYIGGEWVDSASgeTFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESKDQGKTLALARTmDIPRSVQNFRFFASSSLH---HT--SECTQMD--------------------------HLG-- 135
Cdd:cd07131 81 RLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRlfgETvpSELPNKDamtrrqpigvvalitpwnfpvaipswKIFpa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 136 -----------------CMHYTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCK 198
Cdd:cd07131 160 lvcgntvvfkpaedtpaCALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 199 KLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGA 278
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 279 LISKAHLEKVRSYVKRALAEGAQIWCG-EGVDKLSLparnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEE 357
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGgERLTGGGY----EKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 358 VIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLI-RELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTITV 435
Cdd:cd07131 396 AIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
..
gi 301500698 436 KH 437
Cdd:cd07131 476 DY 477
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
27-435 |
1.39e-102 |
|
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: 312.74 E-value: 1.39e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 27 SYDPSTGEVYCRVPNSGKDEIEAAVKAAREAF--PSWSsRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARt 104
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 105 MDIPRSVQNFRFFASSSLHHTSECTQM--DHLGCMHY------------------TVRA--------------------- 143
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIEPepGSFSLVLRepmgvagiivpwnspvvlLVRSlapalaagctvvvkpagqtaq 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 144 ---------PVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFE 214
Cdd:cd07120 159 inaaiirilAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 215 DANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKR 294
Cdd:cd07120 239 DADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVER 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 295 ALAEGAQIWC-GEGVDKlslpaRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATV 373
Cdd:cd07120 319 AIAAGAEVVLrGGPVTE-----GLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 301500698 374 WSSNVGRVHRVAKKLQSGLVWTNCW--LIRELNlpFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07120 394 WTRDLARAMRVARAIRAGTVWINDWnkLFAEAE--EGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
13-437 |
3.88e-102 |
|
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: 312.45 E-value: 3.88e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPS-WSSRSPQERSRVLNQVADLLEQSLEEFAQ 89
Cdd:cd07113 3 FIDGRPVAGQSekRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 90 AESKDQGKTLALARTMDIPRSVQNFRFFASSSLHHTSEC----------------TQMDHLGCM---------------- 137
Cdd:cd07113 83 LETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsipsmqgerytafTRREPVGVVagivpwnfsvmiavwk 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 138 ----------------HYT----VRAPVGVGVP---PGVVNIVFGTGpRVGEALVSHPEVPLISFTGSQPTAERITQLSA 194
Cdd:cd07113 163 igaalatgctivikpsEFTpltlLRVAELAKEAgipDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 195 PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLV 274
Cdd:cd07113 242 SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 275 SIGALISKAHLEKVRSYVKRALAEGAQI-WCGEGVDklslparnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFD 353
Cdd:cd07113 322 MFGPLANQPHFDKVCSYLDDARAEGDEIvRGGEALA--------GEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 354 SEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:cd07113 394 DEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
....
gi 301500698 434 TVKH 437
Cdd:cd07113 474 MIRY 477
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-431 |
1.68e-101 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 311.24 E-value: 1.68e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 7 LLMLENFIDGKFLpcSSY----IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQ 82
Cdd:PLN02278 22 LLRTQGLIGGKWT--DAYdgktFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 83 SLEEFAQAESKDQGKTLALART--------MD-------------IPRSVQNFRFFA----------------------- 118
Cdd:PLN02278 100 NKEDLAQLMTLEQGKPLKEAIGevaygasfLEyfaeeakrvygdiIPSPFPDRRLLVlkqpvgvvgaitpwnfplamitr 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 119 ---------SSSLHHTSECTQMDHLGCMHYTVRAPVGVGVPpgvvNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERI 189
Cdd:PLN02278 180 kvgpalaagCTVVVKPSELTPLTALAAAELALQAGIPPGVL----NVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 190 TQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIP 269
Cdd:PLN02278 256 MAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 270 SDPLVSIGALISKAHLEKVRSYVKRALAEGAQIWCGEgvDKLSLparnqAGYFMLPTVITDIKDESCCMTEEIFGPVTCV 349
Cdd:PLN02278 336 FEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGG--KRHSL-----GGTFYEPTVLGDVTEDMLIFREEVFGPVAPL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 350 VPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTE 429
Cdd:PLN02278 409 TRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLE 488
|
..
gi 301500698 430 IK 431
Cdd:PLN02278 489 IK 490
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
29-435 |
1.76e-100 |
|
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: 307.38 E-value: 1.76e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 29 DPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTmDIP 108
Cdd:cd07107 3 NPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-DVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 109 RSVQNFRFFASSSLHHTSECTQMDHlGCMHYTVRA--------------------------------------------- 143
Cdd:cd07107 82 VAAALLDYFAGLVTELKGETIPVGG-RNLHYTLREpygvvarivafnhplmfaaakiaaplaagntvvvkppeqaplsal 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 144 ----PVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLD 219
Cdd:cd07107 161 rlaeLAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 220 ECIPATVRS-SFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAE 298
Cdd:cd07107 241 AAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 299 GAQIWCGEGVDKLSLPArnqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNV 378
Cdd:cd07107 321 GARLVTGGGRPEGPALE---GGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 301500698 379 GRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
25-435 |
4.39e-100 |
|
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: 306.20 E-value: 4.39e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARt 104
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 105 MDIPRSVQNFRFFASSSLHHTSECTQMD----HLGCMHYTVRA------------------------------------- 143
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREpigvvgaitpfnfpanlfahkiapaiavgnsvvvkps 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 144 -------------PVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPA 210
Cdd:cd07145 160 sntpltaielakiLEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 211 IIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRS 290
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 291 YVKRALAEGAQIWCGegvdklslpARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLA 370
Cdd:cd07145 320 LVNDAVEKGGKILYG---------GKRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQ 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301500698 371 ATVWSSNVGRVHRVAKKLQSGLVWTN-CWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07145 391 ASVFTNDINRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
52-435 |
5.27e-100 |
|
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: 303.00 E-value: 5.27e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 52 KAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARtMDIPRSVQNFRFFASSS-----LHHTS 126
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLAdklggPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 127 ECTQMDHL--------------------------------GC-------------MHYTVRAPVGVGVPPGVVNIVFGTG 161
Cdd:cd06534 80 PDPGGEAYvrreplgvvgvitpwnfplllaawklapalaaGNtvvlkpseltpltALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 162 PRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTS 241
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 242 RIFVQKSIYSEFLKRFVeatrkwkvgipsdplvsigaliskahlekvrsyvkralaegaqiwcgegvdklslparnqagy 321
Cdd:cd06534 240 RLLVHESIYDEFVEKLV--------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 322 fmlpTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLI- 400
Cdd:cd06534 257 ----TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIg 332
|
410 420 430
....*....|....*....|....*....|....*
gi 301500698 401 RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd06534 333 VGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
26-435 |
4.63e-99 |
|
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: 303.48 E-value: 4.63e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 26 DSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALA--R 103
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAwfE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 104 TMDIPRSVqnfRFFASSSLHHTSECTQMDHLGCMHYTVR----------------------------------------- 142
Cdd:cd07150 82 TTFTPELL---RAAAGECRRVRGETLPSDSPGTVSMSVRrplgvvagitpfnyplilatkkvafalaagntvvlkpseet 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 143 ---------APVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIF 213
Cdd:cd07150 159 pviglkiaeIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 214 EDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVK 293
Cdd:cd07150 239 ADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 294 RALAEGAQIWCGEGVDklslparnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATV 373
Cdd:cd07150 319 DAVAKGAKLLTGGKYD----------GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAI 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301500698 374 WSSNVGRVHRVAKKLQSGLVWTNCWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07150 389 LTNDLQRAFKLAERLESGMVHINDPTILdEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
12-436 |
2.09e-98 |
|
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: 302.73 E-value: 2.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 12 NFIDGKFLPcssyidSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAF---PSWSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07141 17 DSVSGKTFP------TINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRAYLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESKDQGKTLALARTMDIPRSVQNFRFFASSSLHHTSECTQMD--------H--------------------------L 134
Cdd:cd07141 91 SLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDgdfftytrHepvgvcgqiipwnfpllmaawklapaL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 135 GCMH---------------YTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA-PHCK 198
Cdd:cd07141 171 ACGNtvvlkpaeqtpltalYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGkSNLK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 199 KLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGA 278
Cdd:cd07141 251 RVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 279 LISKAHLEKVRSYVKRALAEGAQIWCGEGvdklslpARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEV 358
Cdd:cd07141 331 QIDEEQFKKILELIESGKKEGAKLECGGK-------RHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEV 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 301500698 359 IERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITVK 436
Cdd:cd07141 404 IERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
46-435 |
6.12e-98 |
|
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: 299.83 E-value: 6.12e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 46 EIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArtmdiprsvqNFRF-FASSSLHH 124
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKA----------AFEVgAAIAILRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 125 -TSECTQM-------DHLGCMHYTVR-------------------------------------APVGVGVPPGVV----- 154
Cdd:cd07104 71 aAGLPRRPegeilpsDVPGKESMVRRvplgvvgvispfnfplilamrsvapalalgnavvlkpDSRTPVTGGLLIaeife 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 155 ---------NIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPAT 225
Cdd:cd07104 151 eaglpkgvlNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 226 VRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAEGAQIWCG 305
Cdd:cd07104 231 AFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 306 EGVDklslparnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVA 385
Cdd:cd07104 311 GTYE----------GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFA 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 301500698 386 KKLQSGLVWTNCWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07104 381 ERLETGMVHINDQTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
13-436 |
2.36e-97 |
|
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: 300.21 E-value: 2.36e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPC--SSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFP-SWS-SRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07143 10 FINGEFVDSvhGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWGlKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESKDQGKTLALARTMDIPRSVQNFRFFA------------------SSSLHH-------------------------- 124
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFRYYGgwadkihgqvietdikklTYTRHEpigvcgqiipwnfpllmcawkiapal 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 125 ---------TSECTQMDHLgcmhYTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA- 194
Cdd:cd07143 170 aagntivlkPSELTPLSAL----YMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 195 PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLV 274
Cdd:cd07143 246 SNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 275 SIGALISKAHLEKVRSYVKRALAEGAQIWCGEgvdklslPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 354
Cdd:cd07143 326 FQGPQVSQIQYERIMSYIESGKAEGATVETGG-------KRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 355 EEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 434
Cdd:cd07143 399 EEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVH 478
|
..
gi 301500698 435 VK 436
Cdd:cd07143 479 IN 480
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
25-435 |
4.07e-97 |
|
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: 298.36 E-value: 4.07e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALART 104
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 105 mDIPRSVQNFRFFASSSLHHTSECTQMD----HLGCMHYTVR-------------------------------------- 142
Cdd:cd07149 81 -EVDRAIETLRLSAEEAKRLAGETIPFDaspgGEGRIGFTIRepigvvaaitpfnfplnlvahkvgpaiaagnavvlkpa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 143 ------------APVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAphCKKLSLELGGKNPA 210
Cdd:cd07149 160 sqtplsalklaeLLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 211 IIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRS 290
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 291 YVKRALAEGAQIWCGEGVDklslparnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLA 370
Cdd:cd07149 318 WVEEAVEGGARLLTGGKRD----------GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQ 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301500698 371 ATVWSSNVGRVHRVAKKLQSGLVwtncwLIREL------NLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07149 388 AGVFTNDLQKALKAARELEVGGV-----MINDSstfrvdHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
11-437 |
1.56e-96 |
|
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: 297.83 E-value: 1.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 11 ENFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07116 2 DNFIGGEWVAPVKgeYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESKDQGKTLALARTMDIPRSVQNFRFFAS------SSLHHTSECTQMDH----LGCMHYTV----------------- 141
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGciraqeGSISEIDENTVAYHfhepLGVVGQIIpwnfpllmatwklapal 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 142 ---------------------RAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKL 200
Cdd:cd07116 162 aagncvvlkpaeqtpasilvlMELIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 201 SLELGGKNPAIIFE------DANLDECIPATVRSSFaNQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLV 274
Cdd:cd07116 242 TLELGGKSPNIFFAdvmdadDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 275 SIGALISKAHLEKVRSYVKRALAEGAQIWCGEgvDKLSLPARNQAGYFMLPTVITDIKDEscCMTEEIFGPVTCVVPFDS 354
Cdd:cd07116 321 MIGAQASLEQLEKILSYIDIGKEEGAEVLTGG--ERNELGGLLGGGYYVPTTFKGGNKMR--IFQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 355 EEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 434
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 476
|
...
gi 301500698 435 VKH 437
Cdd:cd07116 477 VSY 479
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
12-437 |
2.14e-96 |
|
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: 297.55 E-value: 2.14e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 12 NFIDGKFLPCSS-YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQA 90
Cdd:cd07086 1 GVIGGEWVGSGGeTFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 91 ESKDQGKTLA------------------LARTMD---IPRSVQN------------------FRF-FASSSLHHT----- 125
Cdd:cd07086 81 VSLEMGKILPeglgevqemidicdyavgLSRMLYgltIPSERPGhrlmeqwnplgvvgvitaFNFpVAVPGWNAAialvc 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 126 --------SECTQMDHLGCMHYTVRAPVGVGVPPGVVNIVFGTGPrVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC 197
Cdd:cd07086 161 gntvvwkpSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 198 KKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIG 277
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 278 ALISKAHLEKVRSYVKRALAEGAQIWCGEGVdklslPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEE 357
Cdd:cd07086 320 PLINQAAVEKYLNAIEIAKSQGGTVLTGGKR-----IDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 358 VIERANNVKYGLAATVWSSNVGRVHRV--AKKLQSGLVWTNCWLI-RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 434
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCT 474
|
...
gi 301500698 435 VKH 437
Cdd:cd07086 475 INY 477
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
13-422 |
2.39e-96 |
|
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: 297.38 E-value: 2.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCS--SYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQA 90
Cdd:cd07111 25 FINGKWVKPEnrKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 91 ESKDQGKTLALARTMDIPRSVQNFRFFASSSLHHTSECTQMDHLG-----------------------CMHYTVRAPVGV 147
Cdd:cd07111 105 ESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTELAGWKPVGvvgqivpwnfpllmlawkicpalAMGNTVVLKPAE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 148 GVPPGV----------------VNIVFGTGpRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAI 211
Cdd:cd07111 185 YTPLTAllfaeicaeaglppgvLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 212 IFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSY 291
Cdd:cd07111 264 VFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIREL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 292 VKRALAEGAQIWCGEGVdklsLPARnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAA 371
Cdd:cd07111 344 VEEGRAEGADVFQPGAD----LPSK---GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAA 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 301500698 372 TVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKD 422
Cdd:cd07111 417 SVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKE 467
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
13-437 |
5.98e-91 |
|
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: 283.62 E-value: 5.98e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPS--WSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07140 9 FINGEFVDAEGgkTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESKDQGKTLALARTMDIPRSVQNFRFFA-------------------------------------------------- 118
Cdd:cd07140 89 TIESLDSGAVYTLALKTHVGMSIQTFRYFAgwcdkiqgktipinqarpnrnltltkrepigvcgivipwnyplmmlawkm 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 119 -------SSSLHHTSECTQMDHLGCMHYTVRAPVGVGVPpgvvNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQ 191
Cdd:cd07140 169 aaclaagNTVVLKPAQVTPLTALKFAELTVKAGFPKGVI----NILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 192 LSA-PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPS 270
Cdd:cd07140 245 SCAvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 271 DPLVSIGALISKAHLEKVRSYVKRALAEGAQIWCGEgvDKLSLParnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVV 350
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGG--KQVDRP-----GFFFEPTVFTDVEDHMFIAKEESFGPIMIIS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 351 PFDSE--EEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFT 428
Cdd:cd07140 398 KFDDGdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYL 477
|
....*....
gi 301500698 429 EIKTITVKH 437
Cdd:cd07140 478 KTKTVTIEY 486
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
28-435 |
2.18e-88 |
|
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: 276.02 E-value: 2.18e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTmDI 107
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL-EV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 108 PRSVQNFRFFA---------------------SSSLHHT------------------------------------SECTq 130
Cdd:cd07099 80 LLALEAIDWAArnaprvlaprkvptgllmpnkKATVEYRpygvvgvispwnyplltpmgdiipalaagnavvlkpSEVT- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 131 mdhLGCMHYTVRAPVGVGVPPGVVNIVFGTGPrVGEALVSHpEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPA 210
Cdd:cd07099 159 ---PLVGELLAEAWAAAGPPQGVLQVVTGDGA-TGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 211 IIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRS 290
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 291 YVKRALAEGAQIWCGeGVDklslpaRNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLA 370
Cdd:cd07099 314 HVDDAVAKGAKALTG-GAR------SNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301500698 371 ATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07099 387 ASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIpaLPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
13-433 |
2.34e-88 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 278.61 E-value: 2.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPS--WSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:PLN02466 61 LINGQFVDAASgkTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESKDQGKTLALARTMDIPRSVQNFRFFA------------SSSLHH-------------------------------- 124
Cdd:PLN02466 141 ALETWDNGKPYEQSAKAELPMFARLFRYYAgwadkihgltvpADGPHHvqtlhepigvagqiipwnfpllmfawkvgpal 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 125 ---------TSECTQMDHLgcmhYTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA- 194
Cdd:PLN02466 221 acgntivlkTAEQTPLSAL----YAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAk 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 195 PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLV 274
Cdd:PLN02466 297 SNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 275 SIGALISKAHLEKVRSYVKRALAEGAQIWCGEgvDKLSlparnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 354
Cdd:PLN02466 377 EQGPQIDSEQFEKILRYIKSGVESGATLECGG--DRFG-----SKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKD 449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 301500698 355 EEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:PLN02466 450 LDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
13-434 |
1.10e-85 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 270.84 E-value: 1.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCS--SYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFP-----SWSSRSPQERSRVLNQVADLLEQSLE 85
Cdd:PLN02467 11 FIGGEWREPVlgKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnkgkDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 86 EFAQAESKDQGKTL----------------------ALARTMDIPRSV--QNFRFF------------------------ 117
Cdd:PLN02467 91 ELAKLETLDCGKPLdeaawdmddvagcfeyyadlaeALDAKQKAPVSLpmETFKGYvlkeplgvvglitpwnypllmatw 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 118 -ASSSLhhTSECT------QMDHLGCMHYTVRAPVGVGVPPgVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERIT 190
Cdd:PLN02467 171 kVAPAL--AAGCTavlkpsELASVTCLELADICREVGLPPG-VLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 191 QLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPS 270
Cdd:PLN02467 248 TAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 271 DPLVSIGALISKAHLEKVRSYVKRALAEGAQIWCGeGVDklslPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVV 350
Cdd:PLN02467 328 EEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCG-GKR----PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 351 PFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEI 430
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSV 482
|
....
gi 301500698 431 KTIT 434
Cdd:PLN02467 483 KQVT 486
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
46-435 |
2.06e-85 |
|
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: 267.52 E-value: 2.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 46 EIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARtMDIPRSVQNFRFFASSSLHHT 125
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAG-FNVDLAAGMLREAASLITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 126 SECTQMD--------------------------HLG------------------------CMHYTVRAPVGVGVPPGVVN 155
Cdd:cd07105 80 GGSIPSDkpgtlamvvkepvgvvlgiapwnapvILGtraiayplaagntvvlkaselsprTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 156 IVF---GTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFAN 232
Cdd:cd07105 160 VVThspEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 233 QGEICLCTSRIFVQKSIYSEFLKRFVEATRKwkvgIPSDPlVSIGALISKAHLEKVRSYVKRALAEGAQIWCGegvdklS 312
Cdd:cd07105 240 SGQICMSTERIIVHESIADEFVEKLKAAAEK----LFAGP-VVLGSLVSAAAADRVKELVDDALSKGAKLVVG------G 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 313 LPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGL 392
Cdd:cd07105 309 LADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 301500698 393 VWTNCWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07105 389 VHINGMTVHdEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
25-437 |
2.49e-85 |
|
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: 268.40 E-value: 2.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKT-----L 99
Cdd:cd07151 12 IDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTrikanI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 100 ALARTMDIPRSVQNFRFfASSSLHHTSECTQMDH------LGC----------MHYTVRAPVGVGVP------------- 150
Cdd:cd07151 92 EWGAAMAITREAATFPL-RMEGRILPSDVPGKENrvyrepLGVvgvispwnfpLHLSMRSVAPALALgnavvlkpasdtp 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 151 -----------------PGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIF 213
Cdd:cd07151 171 itgglllakifeeaglpKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 214 EDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVK 293
Cdd:cd07151 251 EDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 294 RALAEGAQIWCGEGVDklslparnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATV 373
Cdd:cd07151 331 QAVEEGATLLVGGEAE----------GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301500698 374 WSSNVGRVHRVAKKLQSGLVWTNCWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITVKH 437
Cdd:cd07151 401 FTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQH 465
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
25-435 |
4.57e-84 |
|
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: 265.07 E-value: 4.57e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARt 104
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 105 MDIPRSVQNFRFFASSSLHHTSECTQMD----------------------------------H-------LGC--MHYT- 140
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRGEEIPLDatqgsdnrlawtirepvgvvlaitpfnfplnlvaHklapaiaTGCpvVLKPa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 141 ----------VRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAphCKKLSLELGGKNPA 210
Cdd:cd07094 160 sktplsalelAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 211 IIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRS 290
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 291 YVKRALAEGAQIWCGEGVDklslparnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLA 370
Cdd:cd07094 318 WVEEAVEAGARLLCGGERD----------GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301500698 371 ATVWSSNVGRVHRVAKKLQSGLVWTN-CWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07094 388 AGIFTRDLNVAFKAAEKLEVGGVMVNdSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
13-436 |
4.86e-84 |
|
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: 266.78 E-value: 4.86e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSSYIDSYDPS-TGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAE 91
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 92 SKDQGK--TLALArtmDIPRSVQNFRFFASSSLHHTSECTQMDHLGCMHYT----------------------------- 140
Cdd:cd07124 116 VLEVGKnwAEADA---DVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVyrplgvgavispwnfplailagmttaalv 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 141 --------------------VRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA------ 194
Cdd:cd07124 193 tgntvvlkpaedtpviaaklVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkvqpgq 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 195 PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLV 274
Cdd:cd07124 273 KWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 275 SIGALISKAHLEKVRSYVKRALAEGaQIWCGEGVdklslPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 354
Cdd:cd07124 353 YMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEV-----LELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 355 EEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTN-----CWLIRElnlPFGGMKSSGIG-REGAKDSYDFFT 428
Cdd:cd07124 427 FDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkitgALVGRQ---PFGGFKMSGTGsKAGGPDYLLQFM 503
|
....*...
gi 301500698 429 EIKTITVK 436
Cdd:cd07124 504 QPKTVTEN 511
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
10-436 |
2.42e-83 |
|
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: 263.61 E-value: 2.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 10 LENFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEF 87
Cdd:cd07085 1 LKLFINGEWVESKTteWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 88 AQAESKDQGKTLALARTmDIPRSVQNFRFfASSSLHH----TSE--CTQMDH------LG-------------------- 135
Cdd:cd07085 81 ARLITLEHGKTLADARG-DVLRGLEVVEF-ACSIPHLlkgeYLEnvARGIDTysyrqpLGvvagitpfnfpamiplwmfp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 136 -------------------CMHYTVRAPVGVGVPPGVVNIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPH 196
Cdd:cd07085 159 maiacgntfvlkpservpgAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 197 CKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSI 276
Cdd:cd07085 238 GKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 277 GALISKAHLEKVRSYVKRALAEGAQIWC-GEGVDklslPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 355
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVLdGRGVK----VPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 356 EEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVwtncwlirELNLP---------FGGMKSSGIGREGA--KDSY 424
Cdd:cd07085 394 DEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMV--------GINVPipvplaffsFGGWKGSFFGDLHFygKDGV 465
|
490
....*....|..
gi 301500698 425 DFFTEIKTITVK 436
Cdd:cd07085 466 RFYTQTKTVTSR 477
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
47-435 |
3.99e-80 |
|
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: 253.92 E-value: 3.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 47 IEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALART--------------------MD 106
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAevekcawicryyaenaeaflAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 107 IPRSV--------------------------QNFRFFASS-------SLHHTSECTQMDHL------------GCmhYTV 141
Cdd:cd07100 81 EPIETdagkayvryeplgvvlgimpwnfpfwQVFRFAAPNlmagntvLLKHASNVPGCALAieelfreagfpeGV--FQN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 142 rapvgvgvppgvvniVFGTGPRVgEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDEC 221
Cdd:cd07100 159 ---------------LLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 222 IPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAEGAQ 301
Cdd:cd07100 223 VKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGAT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 302 IWCGEGVDKlslparnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRV 381
Cdd:cd07100 303 LLLGGKRPD-------GPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERA 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 301500698 382 HRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07100 376 ERVARRLEAGMVFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
29-435 |
8.29e-80 |
|
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: 253.77 E-value: 8.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 29 DPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFA---QAESkdqGKTLALA--R 103
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLdliQLET---GKARRHAfeE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 104 TMDIprsVQNFRFFASSS---------------LHHTSECTQ-------------------MDHLG-------------- 135
Cdd:cd07101 79 VLDV---AIVARYYARRAerllkprrrrgaipvLTRTTVNRRpkgvvgvispwnypltlavSDAIPallagnavvlkpds 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 136 ----CMHYTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEvpLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAI 211
Cdd:cd07101 156 qtalTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD--YVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 212 IFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSY 291
Cdd:cd07101 234 VLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 292 VKRALAEGAQIWCGeGVdklslpARNQAG-YFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLA 370
Cdd:cd07101 314 VDDAVAKGATVLAG-GR------ARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLN 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 371 ATVWSSNVGRVHRVAKKLQSGLVWTN-----CWliRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07101 387 ASVWTRDGARGRRIAARLRAGTVNVNegyaaAW--ASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
25-437 |
1.86e-77 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 249.80 E-value: 1.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEE---FAQAESkdqGKTLAL 101
Cdd:PRK09407 34 REVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREElldLVQLET---GKARRH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 102 A--RTMDIPrsvQNFRFFASSS---------------LHHTSECTQ-------------------MDHL-----G----- 135
Cdd:PRK09407 111 AfeEVLDVA---LTARYYARRApkllaprrragalpvLTKTTELRQpkgvvgvispwnypltlavSDAIpallaGnavvl 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 136 --------CMHYTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHpeVPLISFTGSQPTAERITQLSAPHCKKLSLELGGK 207
Cdd:PRK09407 188 kpdsqtplTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 208 NPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEK 287
Cdd:PRK09407 266 NPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLET 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 288 VRSYVKRALAEGAQIWCGeGVdklslpARNQAG-YFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVK 366
Cdd:PRK09407 346 VSAHVDDAVAKGATVLAG-GK------ARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTP 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301500698 367 YGLAATVWSSNVGRVHRVAKKLQSGLVWTN-----CWliRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITVKH 437
Cdd:PRK09407 419 YGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAW--GSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIATQR 492
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
33-435 |
6.55e-77 |
|
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: 246.05 E-value: 6.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 33 GEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARtMDIPRSVQ 112
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAG-FEVGAAIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 113 NFRFFASSSLHH-----TSECTQMDH-----LGC----------MHYTVRAPVGVgvppgvvnIVFGT------------ 160
Cdd:cd07152 80 ELHEAAGLPTQPqgeilPSAPGRLSLarrvpLGVvgvispfnfpLILAMRSVAPA--------LALGNavvlkpdprtpv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 161 -------------------------GPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFED 215
Cdd:cd07152 152 sggvviarlfeeaglpagvlhvlpgGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 216 ANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRA 295
Cdd:cd07152 232 ADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 296 LAEGAQIWCGEGVDklslparnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWS 375
Cdd:cd07152 312 VAAGARLEAGGTYD----------GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIIS 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301500698 376 SNVGRVHRVAKKLQSGLVWTN-CWLIRELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTITV 435
Cdd:cd07152 382 RDVGRAMALADRLRTGMLHINdQTVNDEPHNPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
8-433 |
1.20e-76 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 247.12 E-value: 1.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 8 LMLEN--FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPS--WSSRSPQERSRVLNQVADLLE 81
Cdd:PRK09847 16 LAIENrlFINGEYTAAAEneTFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 82 QSLEEFAQAESKDQGKTLALARTMDIPRSVQNFRFFASSSLHHTSECTQMDH-------------------------LGC 136
Cdd:PRK09847 96 AHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSShelamivrepvgviaaivpwnfpllLTC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 137 MH------------------------YTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQL 192
Cdd:PRK09847 176 WKlgpalaagnsvilkpseksplsaiRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 193 SA-PHCKKLSLELGGKNPAIIFEDA-NLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPS 270
Cdd:PRK09847 256 AGdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 271 DPLVSIGALISKAHLEKVRSYVKRALAEGaqiwcgegvdKLSLPARNQAGYFML-PTVITDIKDESCCMTEEIFGPVTCV 349
Cdd:PRK09847 336 DPATTMGTLIDCAHADSVHSFIREGESKG----------QLLLDGRNAGLAAAIgPTIFVDVDPNASLSREEIFGPVLVV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 350 VPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTE 429
Cdd:PRK09847 406 TRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTE 485
|
....
gi 301500698 430 IKTI 433
Cdd:PRK09847 486 LKTI 489
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
25-431 |
1.83e-75 |
|
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: 242.54 E-value: 1.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALART 104
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 105 mDIPRSVQNFRFFASSSLHHTSECTQMD-------HLGCmhytVR----------------------------------- 142
Cdd:cd07147 81 -EVARAIDTFRIAAEEATRIYGEVLPLDisargegRQGL----VRrfpigpvsaitpfnfplnlvahkvapaiaagcpfv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 143 ---APVGVGVPPGVVNIVFGTG---------P---RVGEALVSHPEVPLISFTGSQPTAERITQLsAPHcKKLSLELGGK 207
Cdd:cd07147 156 lkpASRTPLSALILGEVLAETGlpkgafsvlPcsrDDADLLVTDERIKLLSFTGSPAVGWDLKAR-AGK-KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 208 NPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEK 287
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 288 VRSYVKRALAEGAQIWCGEGVDklslparnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKY 367
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGKRD----------GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKF 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301500698 368 GLAATVWSSNVGRVHRVAKKLQSGLVWTN---CWliRELNLPFGGMKSSGIGREGAKDSYDFFTEIK 431
Cdd:cd07147 384 GLQAGVFTRDLEKALRAWDELEVGGVVINdvpTF--RVDHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-435 |
6.37e-73 |
|
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: 236.43 E-value: 6.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTMDI 107
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 108 ---------------------PRSVQNFRFFASSSLHHtsectqmDHLG------------------------------- 135
Cdd:cd07098 81 lvtcekirwtlkhgekalrpeSRPGGLLMFYKRARVEY-------EPLGvvgaivswnypfhnllgpiiaalfagnaivv 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 136 -CMHYTV-----------RAPVGVGVPPGVVNIVFGTgPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLE 203
Cdd:cd07098 154 kVSEQVAwssgfflsiirECLAACGHDPDLVQLVTCL-PETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 204 LGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKA 283
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 284 HLEKVRSYVKRALAEGAQIWCGeGVdklslpaRNQA-----GYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEV 358
Cdd:cd07098 313 RFDRLEELVADAVEKGARLLAG-GK-------RYPHpeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEA 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 301500698 359 IERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTITV 435
Cdd:cd07098 385 VEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVqqLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
11-436 |
2.02e-72 |
|
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: 235.16 E-value: 2.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 11 ENFIDGKFLPCS-SYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSP-QERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07082 3 KYLINGEWKESSgKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESKDQGKTLALArTMDIPRSVQNFRFFASSSLHHTSECTQMDH---------------LG---CM------------- 137
Cdd:cd07082 83 NLLMWEIGKTLKDA-LKEVDRTIDYIRDTIEELKRLDGDSLPGDWfpgtkgkiaqvrrepLGvvlAIgpfnyplnltvsk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 138 -----------------------HYTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSa 194
Cdd:cd07082 162 lipalimgntvvfkpatqgvllgIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQH- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 195 pHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLV 274
Cdd:cd07082 241 -PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 275 SIGALISKAHLEKVRSYVKRALAEGAQIWCGEGvdklslparNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 354
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGG---------REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVND 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 355 EEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIREL-NLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:cd07082 391 IEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPdHFPFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
...
gi 301500698 434 TVK 436
Cdd:cd07082 471 VIN 473
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
29-435 |
3.94e-72 |
|
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: 233.79 E-value: 3.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 29 DPSTGEVYCRVPNSGKDEIEAAVKAAReAFPSWSSRspQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARtMDIP 108
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALAA-SYRSTLTR--YQRSAILNKAAALLEARREEFARLITLESGLCLKDTR-YEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 109 RSVQNFRFFASSSLHHTSECTQMD-------HLGcmhYTVRAPVGVGVPPGVVN-------------------IVFGTGP 162
Cdd:cd07146 81 RAADVLRFAAAEALRDDGESFSCDltangkaRKI---FTLREPLGVVLAITPFNhplnqvahkiapaiaannrIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 163 R-------------------------------VGEALVSHPEVPLISFTGSQPTAERITQLSAphCKKLSLELGGKNPAI 211
Cdd:cd07146 158 KtplsaiyladllyeaglppdmlsvvtgepgeIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 212 IFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSY 291
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 292 VKRALAEGAQIWCGegvdklslPARNqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAA 371
Cdd:cd07146 316 VEEAIAQGARVLLG--------NQRQ--GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSS 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 301500698 372 TVWSSNVGRVHRVAKKLQSGLVwtNCWLI---RELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTITV 435
Cdd:cd07146 386 GVCTNDLDTIKRLVERLDVGTV--NVNEVpgfRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
7-431 |
3.81e-70 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 229.79 E-value: 3.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 7 LLMLENFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSL 84
Cdd:PRK11241 8 LFRQQALINGEWLDANNgeVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 85 EEFAQAESKDQGKTLALARTmDIPRSVQNFRFFASSSL---------HHTSE---------------------------- 127
Cdd:PRK11241 88 DDLARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKriygdtipgHQADKrlivikqpigvtaaitpwnfpaamitrk 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 128 --------CTQM---------DHLGCMHYTVRAPVGVGVPpgvvNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERIT 190
Cdd:PRK11241 167 agpalaagCTMVlkpasqtpfSALALAELAIRAGIPAGVF----NVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 191 QLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPS 270
Cdd:PRK11241 243 EQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 271 DPLVSIGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDKLslparnqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVV 350
Cdd:PRK11241 323 EKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHEL-------GGNFFQPTILVDVPANAKVAKEETFGPLAPLF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 351 PFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEI 430
Cdd:PRK11241 396 RFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEI 475
|
.
gi 301500698 431 K 431
Cdd:PRK11241 476 K 476
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
155-416 |
7.22e-70 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 226.93 E-value: 7.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 155 NIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQG 234
Cdd:PRK10090 132 NLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSG 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 235 EICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPL-VSIGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDklsl 313
Cdd:PRK10090 212 QVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEGARVALGGKAV---- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 314 parNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLV 393
Cdd:PRK10090 288 ---EGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGET 364
|
250 260
....*....|....*....|....*...
gi 301500698 394 WTNcwliRElNLP-----FGGMKSSGIG 416
Cdd:PRK10090 365 YIN----RE-NFEamqgfHAGWRKSGIG 387
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
13-434 |
2.66e-65 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 217.81 E-value: 2.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSSYIDSYDPS-TGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAE 91
Cdd:TIGR01237 36 VINGERVETENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 92 SKDQGKTLALA-----------------------------------RTMDIPRSVQ------NFRF--FASSSLHH--TS 126
Cdd:TIGR01237 116 VKEVGKPWNEAdaevaeaidfmeyyarqmielakgkpvnsregetnQYVYTPTGVTvvispwNFPFaiMVGMTVAPivTG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 127 ECTQM----DHLGCMHYTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA------PH 196
Cdd:TIGR01237 196 NCVVLkpaeAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvqpgqKH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 197 CKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSI 276
Cdd:TIGR01237 276 LKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 277 GALISKAHLEKVRSYVKRALAEGAQIWCGEGVDKlslparnqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEE 356
Cdd:TIGR01237 356 GPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDS--------KGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFD 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 357 EVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGlvwtNCWLIRELN------LPFGGMKSSGIG-REGAKDSYDFFTE 429
Cdd:TIGR01237 428 EALEIANNTEYGLTGGVISNNRDHINRAKAEFEVG----NLYFNRNITgaivgyQPFGGFKMSGTDsKAGGPDYLALFMQ 503
|
....*
gi 301500698 430 IKTIT 434
Cdd:TIGR01237 504 AKTVT 508
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
28-433 |
3.73e-64 |
|
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: 213.26 E-value: 3.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALA----R 103
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAggeiR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 104 TM--------DI-PRSVQNFRFFASSSLHHTSECtqmDHLG--------------------------------------- 135
Cdd:cd07102 81 GMlerarymiSIaEEALADIRVPEKDGFERYIRR---EPLGvvliiapwnypyltavnavipallagnavilkhspqtpl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 136 CMHYTVRAPVGVGVPPGVVNIVFGTGPrVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFED 215
Cdd:cd07102 158 CGERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 216 ANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRA 295
Cdd:cd07102 237 ADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 296 LAEGAQIWCGEGvdklSLPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWS 375
Cdd:cd07102 317 IAKGARALIDGA----LFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWT 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 301500698 376 SNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:cd07102 393 KDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
14-434 |
1.12e-60 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 205.55 E-value: 1.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 14 IDGKFLPCSSYIDSYDPS-TGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAES 92
Cdd:PRK03137 41 IGGERITTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 93 KDQGKTLALArTMDIPRSVQNFRFFASS--SLHHTSECTQM-DHLGCMHYT----------------------------- 140
Cdd:PRK03137 121 KEAGKPWAEA-DADTAEAIDFLEYYARQmlKLADGKPVESRpGEHNRYFYIplgvgvvispwnfpfaimagmtlaaivag 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 141 ------------------VRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA---P---H 196
Cdd:PRK03137 200 ntvllkpasdtpviaakfVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAkvqPgqiW 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 197 CKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVsI 276
Cdd:PRK03137 280 LKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAY-M 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 277 GALISKAHLEKVRSYVKRALAEGAQIWCGEGVDKlslparnqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEE 356
Cdd:PRK03137 359 GPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDS--------KGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 357 EVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGlvwtNCWLIRELN------LPFGGMKSSGI-GREGAKDSYDFFTE 429
Cdd:PRK03137 431 HALEIANNTEYGLTGAVISNNREHLEKARREFHVG----NLYFNRGCTgaivgyHPFGGFNMSGTdSKAGGPDYLLLFLQ 506
|
....*
gi 301500698 430 IKTIT 434
Cdd:PRK03137 507 AKTVS 511
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
25-433 |
1.89e-58 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 198.42 E-value: 1.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALART 104
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 105 mDIPRSVQNFRFFASSS---------------------------------------------------------LHHTSE 127
Cdd:PRK09406 83 -EALKCAKGFRYYAEHAealladepadaaavgasrayvryqplgvvlavmpwnfplwqvvrfaapalmagnvglLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 128 CTQmdhlgCMHYTV----RAPVGVGvppgvvniVFGT---GPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKL 200
Cdd:PRK09406 162 VPQ-----TALYLAdlfrRAGFPDG--------CFQTllvGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 201 SLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALI 280
Cdd:PRK09406 229 VLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 281 SKAHLEKVRSYVKRALAEGAQIWCGEgvdklSLPARNqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIE 360
Cdd:PRK09406 309 TEQGRDEVEKQVDDAVAAGATILCGG-----KRPDGP--GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIE 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301500698 361 RANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:PRK09406 382 IANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
15-437 |
9.05e-55 |
|
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: 188.95 E-value: 9.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 15 DGKFLPCSSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKD 94
Cdd:cd07130 4 DGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 95 QGKTLA------------------LARTMD---IP--RS----------------VQNFRFFAS--------------SS 121
Cdd:cd07130 84 MGKILPeglgevqemidicdfavgLSRQLYgltIPseRPghrmmeqwnplgvvgvITAFNFPVAvwgwnaaialvcgnVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 122 LHHTSECTQMDHLGCMHYTVRAPVGVGVPPGVVNIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLS 201
Cdd:cd07130 164 VWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 202 LELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALIS 281
Cdd:cd07130 243 LELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 282 KAHLEKVRSYVKRALAEGAQIWCGEgvdklslPARNQAGYFMLPTVITDIKDEScCMTEEIFGPVTCVVPFDSEEEVIER 361
Cdd:cd07130 323 KAAVDNYLAAIEEAKSQGGTVLFGG-------KVIDGPGNYVEPTIVEGLSDAP-IVKEETFAPILYVLKFDTLEEAIAW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 362 ANNVKYGLAATVWSSNVGRVHRVAKKLQS--GLVwtNCwlirelNLP---------FGGMKSSGIGREGAKDSYDFFTEI 430
Cdd:cd07130 395 NNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIV--NV------NIGtsgaeiggaFGGEKETGGGRESGSDAWKQYMRR 466
|
....*..
gi 301500698 431 KTITVKH 437
Cdd:cd07130 467 STCTINY 473
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
32-437 |
1.79e-48 |
|
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: 172.76 E-value: 1.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 32 TGEVYCRVPNSGKDEIEAAVKAAREAFPSWSsRSPQE-RSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArTMDIPRS 110
Cdd:cd07083 42 PSEVVGTTAKADKAEAEAALEAAWAAFKTWK-DWPQEdRARLLLKAADLLRRRRRELIATLTYEVGKNWVEA-IDDVAEA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 111 VQNFRFFASSSLH----------HTSECTQMDHLG-------------------------CMHYTVRAPVGVGVPPGVV- 154
Cdd:cd07083 120 IDFIRYYARAALRlrypavevvpYPGEDNESFYVGlgagvvispwnfpvaiftgmivapvAVGNTVIAKPAEDAVVVGYk 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 155 ---------------NIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC------KKLSLELGGKNPAIIF 213
Cdd:cd07083 200 vfeifheagfppgvvQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLApgqtwfKRLYVETGGKNAIIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 214 EDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVK 293
Cdd:cd07083 280 ETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 294 RALAEGAQIWCGegvdklSLPARNqaGYFMLPTVITDIKDESCCMTEEIFGPVTCV--VPFDSEEEVIERANNVKYGLAA 371
Cdd:cd07083 360 HGKNEGQLVLGG------KRLEGE--GYFVAPTVVEEVPPKARIAQEEIFGPVLSVirYKDDDFAEALEVANSTPYGLTG 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 301500698 372 TVWSSNVGRVHRVAKKLQSGLVWTNCWLIREL--NLPFGGMKSSGIG-REGAKDSYDFFTEIKTITVKH 437
Cdd:cd07083 432 GVYSRKREHLEEARREFHVGNLYINRKITGALvgVQPFGGFKLSGTNaKTGGPHYLRRFLEMKAVAERF 500
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
13-416 |
8.06e-48 |
|
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: 171.22 E-value: 8.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSSYIDSYDPSTGE-VYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEF---A 88
Cdd:cd07125 36 IINGEETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELialA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 89 QAESkdqGKTLALArtmdIP--RSVQNF-RFFASSSLHHTSECTQMDHLG------------------------------ 135
Cdd:cd07125 116 AAEA---GKTLADA----DAevREAIDFcRYYAAQARELFSDPELPGPTGelnglelhgrgvfvcispwnfplaiftgqi 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 136 --------------------CMHYTVRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAP 195
Cdd:cd07125 189 aaalaagntviakpaeqtplIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 196 HCK---KLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDP 272
Cdd:cd07125 269 RDGpilPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 273 LVSIGALISKAHLEKVRSYVKRALAEGAQIWcgegvdKLSLPARNqaGYFMLPTVITDikDESCCMTEEIFGPVTCVVPF 352
Cdd:cd07125 349 STDVGPLIDKPAGKLLRAHTELMRGEAWLIA------PAPLDDGN--GYFVAPGIIEI--VGIFDLTTEVFGPILHVIRF 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301500698 353 DSE--EEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGlvwtNCWLIRE------LNLPFGGMKSSGIG 416
Cdd:cd07125 419 KAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG----NLYINRNitgaivGRQPFGGWGLSGTG 486
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
46-420 |
6.85e-47 |
|
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: 166.68 E-value: 6.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 46 EIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALART--------MDIprSVQNFR-- 115
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDI--SIKAYHer 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 116 --------FFASSSLHHT------------------------------------SECTQMdhlgCMHYTVRAPVGVGVPP 151
Cdd:cd07095 79 tgeratpmAQGRAVLRHRphgvmavfgpfnfpghlpnghivpallagntvvfkpSELTPA----VAELMVELWEEAGLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 152 GVVNIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK-LSLELGGKNPAIIFEDANLDECIPATVRSSF 230
Cdd:cd07095 155 GVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKiLALEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 231 ANQGEICLCTSRIFV-QKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAEGAQIwcgegvd 309
Cdd:cd07095 234 LTAGQRCTCARRLIVpDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEP------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 310 klSLPAR--NQAGYFMLPTVI--TDIKDESccmTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVA 385
Cdd:cd07095 307 --LLAMErlVAGTAFLSPGIIdvTDAADVP---DEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFL 381
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 301500698 386 KKLQSGLVWTNcwliRELN-----LPFGGMKSSGIGREGA 420
Cdd:cd07095 382 ARIRAGIVNWN----RPTTgasstAPFGGVGLSGNHRPSA 417
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
157-433 |
5.76e-46 |
|
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: 164.24 E-value: 5.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 157 VFGTGPRVGEALVSHPeVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDEcipaTVRS----SFAN 232
Cdd:cd07087 161 VVEGGVEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEV----AARRiawgKFLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 233 QGEICLCTSRIFVQKSIYSEFLKRFVEATRKWkvgIPSDPLVS--IGALISKAHLEKVRSyvkraLAEGAQIWCGEGVDK 310
Cdd:cd07087 236 AGQTCIAPDYVLVHESIKDELIEELKKAIKEF---YGEDPKESpdYGRIINERHFDRLAS-----LLDDGKVVIGGQVDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 311 LSLparnqagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQS 390
Cdd:cd07087 308 EER--------YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSS 379
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 301500698 391 GLVWTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:cd07087 380 GGVCVNDVLLHAAIpnLPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
27-433 |
3.72e-45 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 163.11 E-value: 3.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 27 SYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTmD 106
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-E 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 107 IPRS---------------------VQN------FR-------------------------FFASSS--LHHTSECTqmd 132
Cdd:PRK13968 90 VAKSanlcdwyaehgpamlkaeptlVENqqavieYRplgtilaimpwnfplwqvmrgavpiLLAGNGylLKHAPNVM--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 133 hlGCMHYTVRAPVGVGVPPGVVNIVFGTGPRVGEAlVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAII 212
Cdd:PRK13968 167 --GCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQM-INDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 213 FEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYV 292
Cdd:PRK13968 244 LNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 293 KRALAEGAQIWCGEgvDKLSlparnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAAT 372
Cdd:PRK13968 324 EATLAEGARLLLGG--EKIA-----GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSAT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301500698 373 VWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
25-419 |
4.59e-45 |
|
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: 162.59 E-value: 4.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSP-QERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALAR 103
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWLPaHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 104 tMDIPRSVQNFRFFASSSLHHTSECTQMDHL----GCMHYTVRAPVGVGVPPGVVN-----IVFGTGP------------ 162
Cdd:cd07148 81 -VEVTRAIDGVELAADELGQLGGREIPMGLTpasaGRIAFTTREPIGVVVAISAFNhplnlIVHQVAPaiaagcpvivkp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 163 --------------------------------RVGEALVSHPEVPLISFTGSQPTAERITQLSAPHcKKLSLELGGKNPA 210
Cdd:cd07148 160 alatplsclafvdllheaglpegwcqavpcenAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 211 IIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRS 290
Cdd:cd07148 239 IVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 291 YVKRALAEGAQIWCGegvdklslpARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLA 370
Cdd:cd07148 319 WVNEAVAAGARLLCG---------GKRLSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQ 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 301500698 371 ATVWSSNVGRVHRVAKKLQSGLVWTN-------CWlirelnLPFGGMKSSGIGREG 419
Cdd:cd07148 390 AAVFTKDLDVALKAVRRLDATAVMVNdhtafrvDW------MPFAGRRQSGYGTGG 439
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
13-420 |
2.29e-44 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 161.28 E-value: 2.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 13 FIDGKFLPCSSY-IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAE 91
Cdd:PRK09457 4 WINGDWIAGQGEaFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 92 SKDQGKTLALART--------MDIprSVQNFR----------FFASSSLHHT---------------------------- 125
Cdd:PRK09457 84 ARETGKPLWEAATevtaminkIAI--SIQAYHertgekrsemADGAAVLRHRphgvvavfgpynfpghlpnghivpalla 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 126 --------SECTQmdhlGCMHYTVRAPVGVGVPPGVVNIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC 197
Cdd:PRK09457 162 gntvvfkpSELTP----WVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 198 KK-LSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSE-FLKRFVEATRKWKVGIP-SDPLV 274
Cdd:PRK09457 237 EKiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWdAEPQP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 275 SIGALISKAHLEKVRSYVKRALAEGAQIWcgegvdkLSLPARNQAGYFMLPTVI--TDIKDESccmTEEIFGPVTCVVPF 352
Cdd:PRK09457 317 FMGAVISEQAAQGLVAAQAQLLALGGKSL-------LEMTQLQAGTGLLTPGIIdvTGVAELP---DEEYFGPLLQVVRY 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301500698 353 DSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNcwliRELN-----LPFGGMKSSGIGREGA 420
Cdd:PRK09457 387 DDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWN----KPLTgassaAPFGGVGASGNHRPSA 455
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
157-417 |
2.43e-40 |
|
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: 149.30 E-value: 2.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 157 VFGTGPRVGEALVSHPeVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEI 236
Cdd:cd07134 161 VFEGDAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQT 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 237 CLCTSRIFVQKSIYSEFLKRFVEATRKW----KVGIPSDPLVSIgalISKAHLEKVRSYVKRALAEGAQIWCGEGVDkls 312
Cdd:cd07134 240 CIAPDYVFVHESVKDAFVEHLKAEIEKFygkdAARKASPDLARI---VNDRHFDRLKGLLDDAVAKGAKVEFGGQFD--- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 313 lPARNqagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGL 392
Cdd:cd07134 314 -AAQR----YIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGG 388
|
250 260
....*....|....*....|....*..
gi 301500698 393 VWTNCWLIREL--NLPFGGMKSSGIGR 417
Cdd:cd07134 389 VVVNDVVLHFLnpNLPFGGVNNSGIGS 415
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
12-434 |
4.15e-39 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 148.74 E-value: 4.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 12 NFIDGKFLPC--SSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQ 89
Cdd:PLN02419 116 NLIGGSFVESqsSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 90 AESKDQGKTLALARTmDIPRSVQNFRFFASSSLHHTSECTQMDHLGCMHYTVRA-------------------------- 143
Cdd:PLN02419 196 NITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREplgvcagicpfnfpamiplwmfpvav 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 144 ------------------------PVGVGVPPGVVNIVFGTGPRVgEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK 199
Cdd:PLN02419 275 tcgntfilkpsekdpgasvilaelAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 200 LSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRI-FVQKSIYSEflKRFVEATRKWKVGIPSDPLVSIGA 278
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVvFVGDAKSWE--DKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 279 LISKAHLEKVRSYVKRALAEGAQIWCgEGVDkLSLPARnQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEV 358
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLL-DGRD-IVVPGY-EKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 359 IERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLirELNLP---FGGMKSSGIGREG--AKDSYDFFTEIKTI 433
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI--PVPLPffsFTGNKASFAGDLNfyGKAGVDFFTQIKLV 586
|
.
gi 301500698 434 T 434
Cdd:PLN02419 587 T 587
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
177-433 |
1.52e-36 |
|
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: 138.89 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 177 ISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKR 256
Cdd:cd07135 188 IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 257 FVEATRK-WKVGIPSDPlvSIGALISKAHLEKVRSYVKRAlaeGAQIWCGEGVDKLSLparnqagyFMLPTVITDIKDES 335
Cdd:cd07135 268 LKKVLDEfYPGGANASP--DYTRIVNPRHFNRLKSLLDTT---KGKVVIGGEMDEATR--------FIPPTIVSDVSWDD 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 336 CCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSG-LVWTNCWL---IRelNLPFGGMK 411
Cdd:cd07135 335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGgVVINDTLIhvgVD--NAPFGGVG 412
|
250 260
....*....|....*....|..
gi 301500698 412 SSGIGREGAKDSYDFFTEIKTI 433
Cdd:cd07135 413 DSGYGAYHGKYGFDTFTHERTV 434
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
176-437 |
2.08e-36 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 139.39 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 176 LISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLK 255
Cdd:PTZ00381 188 HIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 256 RFVEATRKWkvgIPSDPLVS--IGALISKAHLEKVRSYVKRalaEGAQIWCGEGVDKlslparnqAGYFMLPTVITDIKD 333
Cdd:PTZ00381 268 ALKEAIKEF---FGEDPKKSedYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVDI--------ENKYVAPTIIVNPDL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 334 ESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELN--LPFGGMK 411
Cdd:PTZ00381 334 DSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNpnLPFGGVG 413
|
250 260
....*....|....*....|....*.
gi 301500698 412 SSGIGREGAKDSYDFFTEIKTITVKH 437
Cdd:PTZ00381 414 NSGMGAYHGKYGFDTFSHPKPVLNKS 439
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
177-433 |
2.80e-36 |
|
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: 138.41 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 177 ISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKR 256
Cdd:cd07136 180 IFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 257 FVEATRKWkvgIPSDPLVSI--GALISKAHLEKVRSYVkralaEGAQIWCGEGVDKLSLparnqagyFMLPTVITDIKDE 334
Cdd:cd07136 260 LKEEIKKF---YGEDPLESPdyGRIINEKHFDRLAGLL-----DNGKIVFGGNTDRETL--------YIEPTILDNVTWD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 335 SCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELN--LPFGGMKS 412
Cdd:cd07136 324 DPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANpyLPFGGVGN 403
|
250 260
....*....|....*....|.
gi 301500698 413 SGIGREGAKDSYDFFTEIKTI 433
Cdd:cd07136 404 SGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
157-433 |
1.36e-33 |
|
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: 130.68 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 157 VFGTGPRVGEALVSHPEVPLIsFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEI 236
Cdd:cd07133 162 VVTGGADVAAAFSSLPFDHLL-FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 237 CLCTSRIFVQKSIYSEFLKRFVEATRK-WKVGIPSDPLVSIgalISKAHLEKVRSYVKRALAEGAQIW-CGEGvdklslP 314
Cdd:cd07133 241 CVAPDYVLVPEDKLEEFVAAAKAAVAKmYPTLADNPDYTSI---INERHYARLQGLLEDARAKGARVIeLNPA------G 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 315 ARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVW 394
Cdd:cd07133 312 EDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVT 391
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 301500698 395 TNCWLIREL--NLPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:cd07133 392 INDTLLHVAqdDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
33-375 |
2.16e-32 |
|
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: 128.47 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 33 GEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSL-EEFAQAESKDQGKTLALARTMDIPRSV 111
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLGQGKNVWQAEIDAACELI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 112 QNFRF---FASS-----SLHHTSECT-QMDH---------------------LGC----MHYTV---------------- 141
Cdd:cd07123 137 DFLRFnvkYAEElyaqqPLSSPAGVWnRLEYrplegfvyavspfnftaiggnLAGapalMGNVVlwkpsdtavlsnylvy 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 142 RAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA---------PhckKLSLELGGKNPAII 212
Cdd:cd07123 217 KILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGenldryrtyP---RIVGETGGKNFHLV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 213 FEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYV 292
Cdd:cd07123 294 HPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYI 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 293 KRALAE-GAQIWCGEGVDKlslparnQAGYFMLPTVI--TDIKDESccMTEEIFGPVTCV-VPFDSE-EEVIERANNV-K 366
Cdd:cd07123 374 DHAKSDpEAEIIAGGKCDD-------SVGYFVEPTVIetTDPKHKL--MTEEIFGPVLTVyVYPDSDfEETLELVDTTsP 444
|
....*....
gi 301500698 367 YGLAATVWS 375
Cdd:cd07123 445 YALTGAIFA 453
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
155-432 |
8.35e-32 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 126.79 E-value: 8.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 155 NIVFGTGPRVGEALVSHPEVPLISFTGSQpTAERItqlsaphCKK-----LSLELGGKNPAIIFEDANLDECIPATVRSS 229
Cdd:PLN00412 219 SCVTGKGSEIGDFLTMHPGVNCISFTGGD-TGIAI-------SKKagmvpLQMELGGKDACIVLEDADLDLAAANIIKGG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 230 FANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPlVSIGALISKAHLEKVRSYVKRALAEGA---QIWCGE 306
Cdd:PLN00412 291 FSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDD-CDITPVVSESSANFIEGLVMDAKEKGAtfcQEWKRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 307 gvdklslparnqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAK 386
Cdd:PLN00412 370 -------------GNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISD 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 301500698 387 KLQSGLVWTNCWLIRELN-LPFGGMKSSGIGREGAKDSYDFFTEIKT 432
Cdd:PLN00412 437 AMETGTVQINSAPARGPDhFPFQGLKDSGIGSQGITNSINMMTKVKS 483
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
28-416 |
1.05e-29 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 122.35 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 28 YDPST--GEVYcrvpNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEF---AQAESkdqGKTL--A 100
Cdd:COG4230 578 ADHSDvvGTVV----EATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELmalLVREA---GKTLpdA 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 101 LArtmDIPRSVqNF-RFFASSSLHHTSECTQMDHLGCM---------------------------------------HYT 140
Cdd:COG4230 651 IA---EVREAV-DFcRYYAAQARRLFAAPTVLRGRGVFvcispwnfplaiftgqvaaalaagntvlakpaeqtpliaARA 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 141 VRapvgvgvppgvvnI-------------VFGTGPRVGEALVSHPEVPLISFTGSQPTAERIT-QLSAPHCKKLSL--EL 204
Cdd:COG4230 727 VR-------------LlheagvpadvlqlLPGDGETVGAALVADPRIAGVAFTGSTETARLINrTLAARDGPIVPLiaET 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 205 GGKNpAIIFEDANLDE-CIPATVRSSFANQGEIClctS--RI-FVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALI 280
Cdd:COG4230 794 GGQN-AMIVDSSALPEqVVDDVLASAFDSAGQRC---SalRVlCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVI 869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 281 SKAHLEKVRSYVKRALAEGAQIWcgegvdKLSLPARNQAGYFMLPTV--ITDIKDesccMTEEIFGPVTCVVPFDSEE-- 356
Cdd:COG4230 870 DAEARANLEAHIERMRAEGRLVH------QLPLPEECANGTFVAPTLieIDSISD----LEREVFGPVLHVVRYKADEld 939
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 301500698 357 EVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGlvwtNCWLIRelNL--------PFGGMKSSGIG 416
Cdd:COG4230 940 KVIDAINATGYGLTLGVHSRIDETIDRVAARARVG----NVYVNR--NIigavvgvqPFGGEGLSGTG 1001
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
155-414 |
1.48e-29 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 120.66 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 155 NIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK------LSLELGGKNPAIIFEDANLDECIPATVRS 228
Cdd:TIGR01236 229 NFVPGDGVQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRyhnfprIVGETGGKDFHLVHPSADISHAVLGTIRG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 229 SFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRA--LAEGAQIWCGE 306
Cdd:TIGR01236 309 AFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAkkDPEALTILYGG 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 307 GVDKlslparnQAGYFMLPTVI--TDIKDESccMTEEIFGPVTCVVPFDSE--EEVIERANNV-KYGLAATVWSSNVGRV 381
Cdd:TIGR01236 389 KYDD-------SQGYFVEPTVVesKDPDHPL--MSEEIFGPVLTVYVYPDDkyKEILDLVDSTsQYGLTGAVFAKDRKAI 459
|
250 260 270
....*....|....*....|....*....|....*..
gi 301500698 382 HRVAKKLQ--SGLVWTN--CWLIRELNLPFGGMKSSG 414
Cdd:TIGR01236 460 LEADKKLRfaAGNFYINdkCTGAVVGQQPFGGARMSG 496
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
38-416 |
8.46e-29 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 119.53 E-value: 8.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 38 RVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTL--ALArtmDIPRSVQNFR 115
Cdd:PRK11904 578 EVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLqdAIA---EVREAVDFCR 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 116 FFASSSLHHTSECTQM-------DHLG--------CM------------------------------------HYTVRAP 144
Cdd:PRK11904 655 YYAAQARRLFGAPEKLpgptgesNELRlhgrgvfvCIspwnfplaiflgqvaaalaagntviakpaeqtpliaAEAVKLL 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 145 VGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQ-LSAPHCKKLSL--ELGGKNPAIIFEDANLDEC 221
Cdd:PRK11904 735 HEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRtLAARDGPIVPLiaETGGQNAMIVDSTALPEQV 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 222 IPATVRSSFANQGEIClctS--RI-FVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAE 298
Cdd:PRK11904 815 VDDVVTSAFRSAGQRC---SalRVlFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE 891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 299 GAQIWcgegvdKLSLPARNQAGYFMLPTV--ITDIKDesccMTEEIFGPVTCVVPFDSEE--EVIERANNVKYGLAATVW 374
Cdd:PRK11904 892 ARLLA------QLPLPAGTENGHFVAPTAfeIDSISQ----LEREVFGPILHVIRYKASDldKVIDAINATGYGLTLGIH 961
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 301500698 375 SSNVGRVHRVAKKLQSGlvwtNCWLIRelNL--------PFGGMKSSGIG 416
Cdd:PRK11904 962 SRIEETADRIADRVRVG----NVYVNR--NQigavvgvqPFGGQGLSGTG 1005
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
32-416 |
9.55e-29 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 119.58 E-value: 9.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 32 TGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArtMDIPRSV 111
Cdd:PRK11905 577 HDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANA--IAEVREA 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 112 QNF-RFFASSSlHHTSECTQMDHLGCM---------------------------------------HYTVRAPVGVGVPP 151
Cdd:PRK11905 655 VDFlRYYAAQA-RRLLNGPGHKPLGPVvcispwnfplaiftgqiaaalvagntvlakpaeqtpliaARAVRLLHEAGVPK 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 152 GVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK---LSLELGGKNpAIIFEDANLDECIPATV-R 227
Cdd:PRK11905 734 DALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpvpLIAETGGQN-AMIVDSSALPEQVVADViA 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 228 SSFANQGEIClctS--RI-FVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAEGAQIWc 304
Cdd:PRK11905 813 SAFDSAGQRC---SalRVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVH- 888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 305 gegvdKLSLPARNQAGYFMLPTVI--TDIKDesccMTEEIFGPVTCVVPFDSEE--EVIERANNVKYGLAATVWSSNVGR 380
Cdd:PRK11905 889 -----QLPLPAETEKGTFVAPTLIeiDSISD----LEREVFGPVLHVVRFKADEldRVIDDINATGYGLTFGLHSRIDET 959
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 301500698 381 VHRVAKKLQSGLVWTNcwliRelNL--------PFGGMKSSGIG 416
Cdd:PRK11905 960 IAHVTSRIRAGNIYVN----R--NIigavvgvqPFGGEGLSGTG 997
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
177-436 |
2.52e-27 |
|
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: 113.09 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 177 ISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDecipATVR----SSFANQGEICLCTSRIFVQKSIYSE 252
Cdd:cd07132 180 IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDID----VAARriawGKFINAGQTCIAPDYVLCTPEVQEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 253 FLKRFVEATRKWkVGipSDPLVS--IGALISKAHLEKVRsyvkrALAEGAQIWCGEGVDKLSLparnqagyFMLPTVITD 330
Cdd:cd07132 256 FVEALKKTLKEF-YG--EDPKESpdYGRIINDRHFQRLK-----KLLSGGKVAIGGQTDEKER--------YIAPTVLTD 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 331 IKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIREL--NLPFG 408
Cdd:cd07132 320 VKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTldSLPFG 399
|
250 260
....*....|....*....|....*...
gi 301500698 409 GMKSSGIGREGAKDSYDFFTEIKTITVK 436
Cdd:cd07132 400 GVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
45-416 |
4.85e-27 |
|
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: 113.08 E-value: 4.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 45 DEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArTMDIPRSVQNFRFFASSSLHH 124
Cdd:TIGR01238 74 AHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNA-IAEVREAVDFCRYYAKQVRDV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 125 TSECTqMDHLG---CM------------------------------------HYTVRAPVGVGVPPGVVNIVFGTGPRVG 165
Cdd:TIGR01238 153 LGEFS-VESRGvfvCIspwnfplaiftgqisaalaagntviakpaeqtsliaYRAVELMQEAGFPAGTIQLLPGRGADVG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 166 EALVSHPEVPLISFTGSQPTAERITQ-----LSAPhcKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCT 240
Cdd:TIGR01238 232 AALTSDPRIAGVAFTGSTEVAQLINQtlaqrEDAP--VPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSAL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 241 SRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAEGAQIWCGegvdKLSLPARNQAG 320
Cdd:TIGR01238 310 RVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQL----TLDDSRACQHG 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 321 YFMLPTVIT-DIKDEsccMTEEIFGPVTCVVPFDSEE--EVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGlvwtNC 397
Cdd:TIGR01238 386 TFVAPTLFElDDIAE---LSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVG----NC 458
|
410 420
....*....|....*....|....*
gi 301500698 398 WLIREL------NLPFGGMKSSGIG 416
Cdd:TIGR01238 459 YVNRNQvgavvgVQPFGGQGLSGTG 483
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
158-437 |
6.67e-27 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 112.62 E-value: 6.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 158 FGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEIC 237
Cdd:PLN02315 221 FCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRC 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 238 LCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAEGAQIWCGEGvdklslpARN 317
Cdd:PLN02315 301 TTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGS-------AIE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 318 QAGYFMLPTVItDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSglvwtNC 397
Cdd:PLN02315 374 SEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGS-----DC 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 301500698 398 WLIrELNLP---------FGGMKSSGIGREGAKDSYDFFTEIKTITVKH 437
Cdd:PLN02315 448 GIV-NVNIPtngaeiggaFGGEKATGGGREAGSDSWKQYMRRSTCTINY 495
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
161-433 |
3.52e-21 |
|
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: 95.17 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 161 GPRVGEALVSHpEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSF-ANQGEICLC 239
Cdd:cd07137 166 GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 240 TSRIFVQKSIYSEFLKRFVEATRKW--KVGIPSDPLVSIgalISKAHLEKVRSYVKRALAEgAQIWCGEGVDKLSLparn 317
Cdd:cd07137 245 PDYVLVEESFAPTLIDALKNTLEKFfgENPKESKDLSRI---VNSHHFQRLSRLLDDPSVA-DKIVHGGERDEKNL---- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 318 qagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNC 397
Cdd:cd07137 317 ----YIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFND 392
|
250 260 270
....*....|....*....|....*....|....*...
gi 301500698 398 WLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:cd07137 393 TVVQYAIdtLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
161-434 |
2.30e-19 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 90.17 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 161 GPRVGEALVSHPEvPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVR------SSFAnqG 234
Cdd:PLN02203 173 GPAVGEQLLQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSLSSSRDTKVAVNRivggkwGSCA--G 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 235 EICLCTSRIFVQKSiYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAEgAQIWCGEGVDKLSLp 314
Cdd:PLN02203 250 QACIAIDYVLVEER-FAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSIDEKKL- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 315 arnqagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVW 394
Cdd:PLN02203 327 -------FIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVT 399
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 301500698 395 TNCWLIREL--NLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 434
Cdd:PLN02203 400 FNDAIIQYAcdSLPFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
47-376 |
1.55e-17 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 84.52 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 47 IEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLE---QSLEEFAQAESKdqgktLALAR-TMDIPRSVQNFRFFASSSL 122
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEalgDELVARAHAETG-----LPEARlQGELGRTTGQLRLFADLVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 123 HHTSECTQMDH-----------------------------------------------LGC--------MH-YT------ 140
Cdd:cd07129 76 EGSWLDARIDPadpdrqplprpdlrrmlvplgpvavfgasnfplafsvaggdtasalaAGCpvvvkahpAHpGTselvar 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 141 --VRAPVGVGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA--PHCKKLSLELGGKNPAIIFEDA 216
Cdd:cd07129 156 aiRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAarPEPIPFYAELGSVNPVFILPGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 217 nLDECiPATVRSSFA-----NQGEICLCTSRIFVQKsiySEFLKRFVEATRKWKVGIPSDPLVSIGalISKAHLEKVrsy 291
Cdd:cd07129 236 -LAER-GEAIAQGFVgsltlGAGQFCTNPGLVLVPA---GPAGDAFIAALAEALAAAPAQTMLTPG--IAEAYRQGV--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 292 vkRALAEGAqiwcgeGVDKLSLPARNQAGYFMLPTVI-TD----IKDESccMTEEIFGPVTCVVPFDSEEEVIERANNVK 366
Cdd:cd07129 306 --EALAAAP------GVRVLAGGAAAEGGNQAAPTLFkVDaaafLADPA--LQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
410
....*....|
gi 301500698 367 YGLAATVWSS 376
Cdd:cd07129 376 GQLTATIHGE 385
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
177-382 |
2.15e-17 |
|
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: 84.24 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 177 ISFTGSQPTAER------ITQLSAPhckkLSLELGGKNPAIIFEDAN-----LDECIPATVRSSFANQGEICLCTSRIFV 245
Cdd:cd07128 225 VAFTGSAATAAKlrahpnIVARSIR----FNAEADSLNAAILGPDATpgtpeFDLFVKEVAREMTVKAGQKCTAIRRAFV 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 246 QKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRaLAEGAQIWCGEGVDKLSLPARNQAGYFMLP 325
Cdd:cd07128 301 PEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDRFEVVGADAEKGAFFPP 379
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301500698 326 TVIT--DIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSN--------------VGRVH 382
Cdd:cd07128 380 TLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDpafarelvlgaapyHGRLL 452
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
45-416 |
3.49e-16 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 81.17 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 45 DEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArTMDIPRSVQNFRFFASSSLHH 124
Cdd:PRK11809 682 AEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNA-IAEVREAVDFLRYYAGQVRDD 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 125 TSECTQMDhLGCM---------------------------------------HYTVRAPVGVGVPPGVVNIVFGTGPRVG 165
Cdd:PRK11809 761 FDNDTHRP-LGPVvcispwnfplaiftgqvaaalaagnsvlakpaeqtpliaAQAVRILLEAGVPAGVVQLLPGRGETVG 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 166 EALVSHPEVPLISFTGSQPTAeRITQLS-------APHCKKLSLELGGKNpAIIFEDANLDECIPATV-RSSFANQGEIC 237
Cdd:PRK11809 840 AALVADARVRGVMFTGSTEVA-RLLQRNlagrldpQGRPIPLIAETGGQN-AMIVDSSALTEQVVADVlASAFDSAGQRC 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 238 -----LCtsrifVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISK-------AHLEKVRSY---VKRALAEGAQI 302
Cdd:PRK11809 918 salrvLC-----LQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAeakanieRHIQAMRAKgrpVFQAARENSED 992
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 303 WcgegvdklslparnQAGYFMLPTVIT-DIKDEsccMTEEIFGPVTCVVPFDSEE--EVIERANNVKYGLAATVWSSNVG 379
Cdd:PRK11809 993 W--------------QSGTFVPPTLIElDSFDE---LKREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRIDE 1055
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 301500698 380 RVHRVAKKLQSGlvwtNCWLIRelNL--------PFGGMKSSGIG 416
Cdd:PRK11809 1056 TIAQVTGSAHVG----NLYVNR--NMvgavvgvqPFGGEGLSGTG 1094
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
163-398 |
6.39e-15 |
|
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: 76.51 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 163 RVGEALVSHPEVPLISFTGSQPTAERItqLSAPHCKKLSLELGGKNPAIIFEDAN-----LDECipatVRSSFANQGEIC 237
Cdd:cd07084 169 KTMQALLLHPNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQavdyvAWQC----VQDMTACSGQKC 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 238 LCTSRIFVQKsiySEFLKRFVEATR-KWKVGIPSDPLvsIGALIS---KAHLEKVRSYVKRALAEGAQIWcgEGVDKLSL 313
Cdd:cd07084 243 TAQSMLFVPE---NWSKTPLVEKLKaLLARRKLEDLL--LGPVQTfttLAMIAHMENLLGSVLLFSGKEL--KNHSIPSI 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 314 PARNQAGYFMLPTVITDIKDESccMTEEIFGPVTCVVPF--DSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQS- 390
Cdd:cd07084 316 YGACVASALFVPIDEILKTYEL--VTEEIFGPFAIVVEYkkDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWVa 393
|
....*...
gi 301500698 391 GLVWTNCW 398
Cdd:cd07084 394 GRTYAILR 401
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
177-433 |
1.30e-14 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 75.47 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 177 ISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDecipATVRSSFA-----NQGEICLCTSRIFVQKsiys 251
Cdd:PLN02174 192 IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLK----VTVRRIIAgkwgcNNGQACISPDYILTTK---- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 252 EFLKRFVEATRK-WKVGIPSDPLVS--IGALISKAHLEKVRSYVKRALAEGAQIWCGEgvdklslpaRNQAGYFMLPTVI 328
Cdd:PLN02174 264 EYAPKVIDAMKKeLETFYGKNPMESkdMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGE---------KDRENLKIAPTIL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 329 TDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIREL--NLP 406
Cdd:PLN02174 335 LDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLP 414
|
250 260
....*....|....*....|....*..
gi 301500698 407 FGGMKSSGIGREGAKDSYDFFTEIKTI 433
Cdd:PLN02174 415 FGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
177-389 |
1.49e-14 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 75.51 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 177 ISFTGSQPTAERITQLSA--PHCKKLSLELGGKNPAIIFEDAN-----LDECIPATVRSSFANQGEICLCTSRIFVQKSI 249
Cdd:PRK11903 229 VSFTGSAETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEAL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 250 YSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRaLAEGAQIWCGEGVDKLsLPARNQAGYFMLPT--V 327
Cdd:PRK11903 309 YDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGFAL-VDADPAVAACVGPTllG 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301500698 328 ITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNV--------------GRVHRVAKKLQ 389
Cdd:PRK11903 387 ASDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAaflaaaaleladshGRVHVISPDVA 462
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
12-384 |
8.14e-05 |
|
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: 44.79 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 12 NFIDGKFLPCSSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAReAFPSWSSRSP---QER----SRVLNQVADLLEQ-S 83
Cdd:cd07126 1 NLVAGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLR-QCPKSGLHNPlknPERyllyGDVSHRVAHELRKpE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 84 LEEF-------AQAESKDQgktlALARTMDIPRSVQNF-----RFFASS---SLHHTSE--------------------- 127
Cdd:cd07126 80 VEDFfarliqrVAPKSDAQ----ALGEVVVTRKFLENFagdqvRFLARSfnvPGDHQGQqssgyrwpygpvaiitpfnfp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 128 ----CTQMdhLGC------------------MHYTVRAPVGVGVPPGVVNIVFGTGPRVGEaLVSHPEVPLISFTGSQPT 185
Cdd:cd07126 156 leipALQL--MGAlfmgnkpllkvdskvsvvMEQFLRLLHLCGMPATDVDLIHSDGPTMNK-ILLEANPRMTLFTGSSKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 186 AERitqlsaphckkLSLELGGKnpaIIFEDANLDECI--PATV----------RSSFANQGEICLCTSRIFVQKS-IYSE 252
Cdd:cd07126 233 AER-----------LALELHGK---VKLEDAGFDWKIlgPDVSdvdyvawqcdQDAYACSGQKCSAQSILFAHENwVQAG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 253 FLKRFVEATRKWKVgipSDplVSIGALISKAHlEKVRSYVKRALA-EGAQI-WCGEGVDKLSLPARNQAgyfMLPTVI-- 328
Cdd:cd07126 299 ILDKLKALAEQRKL---ED--LTIGPVLTWTT-ERILDHVDKLLAiPGAKVlFGGKPLTNHSIPSIYGA---YEPTAVfv 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301500698 329 ----TDIKDESCCMTEEIFGPVTCVVPFDSEEE--VIERANNVKYGLAATVWSSNVGRVHRV 384
Cdd:cd07126 370 pleeIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEV 431
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
166-342 |
4.22e-04 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 42.21 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 166 EALVSHPEVPLISFTGSqPTAERITQLSAPHckKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFV 245
Cdd:cd07077 174 EELLSHPKIDLIVATGG-RDAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQNACASEQNLYV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 246 QKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGaLISKAHLEKVRSYVKRALAegaqiwCGEGVDKLSLPARNQAGYFMLP 325
Cdd:cd07077 251 VDDVLDPLYEEFKLKLVVEGLKVPQETKPLSK-ETTPSFDDEALESMTPLEC------QFRVLDVISAVENAWMIIESGG 323
|
170
....*....|....*..
gi 301500698 326 TVITDikdesCCMTEEI 342
Cdd:cd07077 324 GPHTR-----CVYTHKI 335
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
45-91 |
7.58e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 38.34 E-value: 7.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 301500698 45 DEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAE 91
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELA 82
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
166-396 |
8.35e-03 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 38.40 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 166 EALVSHPEVPLISFTGsqptAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFV 245
Cdd:cd07081 171 QRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIV 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 246 QKSIYSEFLKRFVEATrkwkvgipsdplvsiGALISKAHLEKVRSYVKRALAEGAQiWCGEGVDK------LSLPARNQa 319
Cdd:cd07081 247 VDSVYDEVMRLFEGQG---------------AYKLTAEELQQVQPVILKNGDVNRD-IVGQDAYKiaaaagLKVPQETR- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500698 320 gyfmLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKY----GLAATVWSSNVG---RVHRVAKKLQSGL 392
Cdd:cd07081 310 ----ILIGEVTSLAEHEPFAHEKLSPVLAMYRAANFADADAKALALKLeggcGHTSAMYSDNIKaieNMNQFANAMKTSR 385
|
....
gi 301500698 393 VWTN 396
Cdd:cd07081 386 FVKN 389
|
|
| |
