|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
27-485 |
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: 830.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 27 SYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTMD 106
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 107 IPRSVQNFRFFASSILHHTSECTQMDHlGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVT 186
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDG-GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 187 AWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDA 266
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 267 NLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRAL 346
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 347 AEGAQIWCGEGVDKLNLPARsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSS 426
Cdd:cd07093 320 AEGATILTGGGRPELPDLEG---GYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 966941000 427 NVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
10-487 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 639.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 10 LENFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEF 87
Cdd:COG1012 6 YPLFIGGEWVAAASgeTFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 88 AQAESKDQGKTLALARtMDIPRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAP 167
Cdd:COG1012 86 AALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 168 AIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC 247
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 248 KKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMG 327
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 328 ALISKAHLEKVRSYVKRALAEGAQIWC-GEGVDKLNlparsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEE 406
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGAELLTgGRRPDGEG-------GYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 407 EVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLI-RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:COG1012 398 EAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
..
gi 966941000 486 KH 487
Cdd:COG1012 478 RL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
20-483 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 610.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 20 PCSSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTL 99
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 100 ALARTmDIPRSVQNFRFFASSILHHTSECTQMDHlGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKP 179
Cdd:pfam00171 84 AEARG-EVDRAIDVLRYYAGLARRLDGETLPSDP-GRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 180 SELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNP 259
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 260 AIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVR 339
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 340 SYVKRALAEGAQIWCGEGVDKLNlparsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGL 419
Cdd:pfam00171 322 KYVEDAKEEGAKLLTGGEAGLDN-------GYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966941000 420 AATVWSSNVGRVHRVAKKLQSGLVWTNCWLI-RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTgDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
10-486 |
0e+00 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 556.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 10 LENFIDGKFLPCSSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPG-WSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:TIGR03216 1 IRNFINGAFVESGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAALKGpWGKMTVAERADLLYAVADEIERRFDDFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESKDQGKTLALARTMDIPRSVQNFRFFASSILHHTSECTQM---DHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKI 165
Cdd:TIGR03216 81 AAEVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTECFEMatpDGKGALNYAVRKPLGVVGVISPWNLPLLLMTWKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 166 APAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGP-RVGEALVSHPEVPLISFTGSQPTAERITQLSA 244
Cdd:TIGR03216 161 GPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRTGSAIMKAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 245 PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLA 324
Cdd:TIGR03216 241 DGVKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDPAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 325 SMGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDklNLPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 404
Cdd:TIGR03216 321 NMGPLISAEHRDKVLSYYALAVEEGATVVTGGGVP--DFGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFDS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 405 EEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:TIGR03216 399 EEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNVC 478
|
..
gi 966941000 485 VK 486
Cdd:TIGR03216 479 IK 480
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
48-485 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 551.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 48 EAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTmDIPRSVQNFRFFASSILHHTSE 127
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 128 CTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIV 207
Cdd:cd07078 80 VIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 208 FGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEIC 287
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 288 LCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDKlnlparS 367
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLE------G 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 368 QAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNC 447
Cdd:cd07078 314 GKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIND 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 966941000 448 WLI-RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07078 394 YSVgAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
13-485 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 522.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSR--SPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07091 7 FINNEFVDSVSgkTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRkmDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESKDQGKTLALARTMDIPRSVQNFRFFA--SSILHHTSECTQMDHLGcmhYTVRAPVGVAGLISPWNLPLYLLTWKIA 166
Cdd:cd07091 87 ALESLDNGKPLEESAKGDVALSIKCLRYYAgwADKIQGKTIPIDGNFLA---YTRREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 167 PAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA-P 245
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAkS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 246 HCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLAS 325
Cdd:cd07091 244 NLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 326 MGALISKAHLEKVRSYVKRALAEGAQIWCGEGvdklnlpARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 405
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGE-------RHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 406 EEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07091 397 DEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
27-485 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 518.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 27 SYDPSTGEVYCRVPNSGKDEIEAAVKAAREAF--PGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALART 104
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 105 MdIPRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTS 184
Cdd:cd07114 81 Q-VRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 185 VTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFE 264
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 265 DANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKR 344
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 345 ALAEGAQIWCGEGVDKLnlpARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVW 424
Cdd:cd07114 320 AREEGARVLTGGERPSG---ADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIW 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966941000 425 SSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07114 397 TRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
10-487 |
0e+00 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 517.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 10 LENFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEF 87
Cdd:TIGR02299 1 IGHFIDGEFVPSESgeTFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKRWAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 88 AQAESKDQGKTLALARTMdIPRSVQNFRFFASSILHHTSECT--QMDHLgcmHYTVRAPVGVAGLISPWNLPLYLLTWKI 165
Cdd:TIGR02299 81 AVLECLDCGQPLRQTRQQ-VIRAAENFRFFADKCEEAMDGRTypVDTHL---NYTVRVPVGPVGLITPWNAPFMLSTWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 166 APAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAP 245
Cdd:TIGR02299 157 APALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNGAD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 246 HCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLAS 325
Cdd:TIGR02299 237 TLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPETE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 326 MGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDKLNLPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 405
Cdd:TIGR02299 317 VGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPTFRGEDLGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFKDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 406 EEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:TIGR02299 397 EEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNVAL 476
|
..
gi 966941000 486 KH 487
Cdd:TIGR02299 477 AL 478
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
28-485 |
9.42e-179 |
|
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: 508.51 E-value: 9.42e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARtMDI 107
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 108 PRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTA 187
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 188 WMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDAN 267
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 268 LDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRALA 347
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 348 EGAQIWCGEGvdklnlpARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSN 427
Cdd:cd07103 321 KGAKVLTGGK-------RLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 966941000 428 VGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07103 394 LARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
13-483 |
7.14e-169 |
|
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: 484.89 E-value: 7.14e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAF--PGWSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07119 1 YIDGEWVEAASgkTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESKDQGKTLALARTmDIPRSVQNFRFFASSILHHTSEctQMDHLGCMH-YTVRAPVGVAGLISPWNLPLYLLTWKIAP 167
Cdd:cd07119 81 RLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGE--VYDVPPHVIsRTVREPVGVCGLITPWNYPLLQAAWKLAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 168 AIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC 247
Cdd:cd07119 158 ALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 248 KKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMG 327
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 328 ALISKAHLEKVRSYVKRALAEGAQIWCGEgvdklNLPARS--QAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 405
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGG-----KRPTGDelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966941000 406 EEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-484 |
3.83e-168 |
|
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: 482.39 E-value: 3.83e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 12 NFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQ 89
Cdd:cd07138 1 FYIDGAWVAPAGteTIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 90 AESKDQGKTLALARTMDIPRSVQNFRFFASSILHHTSECTQMDHLgcmhyTVRAPVGVAGLISPWNLPLYLLTWKIAPAI 169
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEERRGNSL-----VVREPIGVCGLITPWNWPLNQIVLKVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 170 AAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK 249
Cdd:cd07138 156 AAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 250 LSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGAL 329
Cdd:cd07138 236 VALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 330 ISKAHLEKVRSYVKRALAEGAQIWCGeGVDKlnlPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVI 409
Cdd:cd07138 316 ASAAQFDRVQGYIQKGIEEGARLVAG-GPGR---PEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAI 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966941000 410 ERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNcWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07138 392 AIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
28-485 |
5.00e-167 |
|
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: 479.11 E-value: 5.00e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARtMDI 107
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 108 PRSVQNFRFFASSILHHTSECTQMDHlGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTA 187
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPG-GSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 188 WMLCTLLDKAGVPPGVVNIVFGTGpRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDAN 267
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 268 LDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRALA 347
Cdd:cd07090 239 LENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 348 EGAQIWCGEgvDKLNLPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSN 427
Cdd:cd07090 319 EGAKVLCGG--ERVVPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 966941000 428 VGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
26-483 |
1.68e-166 |
|
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: 477.86 E-value: 1.68e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 26 DSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPG--WSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALAR 103
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 104 TMDIPRSVQNFRFFASSI--LHHTSECTQMDHLGcmhYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSE 181
Cdd:cd07112 85 AVDVPSAANTFRWYAEAIdkVYGEVAPTGPDALA---LITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 182 LTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA-PHCKKLSLELGGKNPA 260
Cdd:cd07112 162 QSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNLKRVWLECGGKSPN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 261 IIFEDA-NLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVR 339
Cdd:cd07112 242 IVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 340 SYVKRALAEGAQIWCGEGVDKLNlparsQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGL 419
Cdd:cd07112 322 GYIESGKAEGARLVAGGKRVLTE-----TGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966941000 420 AATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07112 397 AASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
11-485 |
4.53e-165 |
|
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: 474.91 E-value: 4.53e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 11 ENFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07559 2 DNFINGEWVAPSKgeYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESKDQGKTLALARTMDIPRSVQNFRFFASSILHHTSECTQMDHlGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDE-DTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 169 IAAGNTVVAKPSELTSVTAWMLCTLLDKAgVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCK 248
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 249 KLSLELGGKNPAIIFEDAN------LDECIPATVRSSFaNQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDP 322
Cdd:cd07559 240 PVTLELGGKSPNIFFDDAMdadddfDDKAEEGQLGFAF-NQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 323 LASMGALISKAHLEKVRSYVKRALAEGAQIWCGEgvDKLNLPArSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPF 402
Cdd:cd07559 319 ETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGG--ERLTLGG-LDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 403 DSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKT 482
Cdd:cd07559 396 KDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKN 475
|
...
gi 966941000 483 ITV 485
Cdd:cd07559 476 ILV 478
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
29-485 |
4.80e-162 |
|
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: 466.53 E-value: 4.80e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 29 DPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTMDIP 108
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 109 RSVQNFRFFASSILHHTSECTQMDHlGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAW 188
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRG-PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 189 MLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANL 268
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 269 DECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRALAE 348
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 349 GAQIWCGEGVDklnlparSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNV 428
Cdd:cd07115 322 GARLLTGGKRP-------GARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 966941000 429 GRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07115 395 GRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
8-487 |
5.50e-161 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 464.38 E-value: 5.50e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 8 LMLENFIDGKFLPCS-SYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEE 86
Cdd:PRK13473 1 MQTKLLINGELVAGEgEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 87 FAQAESKDQGKTLALARTMDIPRSVQNFRFFASSILH------------HTSectqmdhlgcmhYTVRAPVGVAGLISPW 154
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARClegkaageylegHTS------------MIRRDPVGVVASIAPW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 155 NLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAgVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQP 234
Cdd:PRK13473 149 NYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 235 TAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKW 314
Cdd:PRK13473 228 TGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 315 KVGIPSDPLASMGALISKAHLEKVRSYVKRALAEG-AQIWCGEGvdklnlpARSQAGYFMLPTVITDIKDESCCMTEEIF 393
Cdd:PRK13473 308 KVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGE-------APDGKGYYYEPTLLAGARQDDEIVQREVF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 394 GPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCW--LIRElnLPFGGMKSSGIGREGAK 471
Cdd:PRK13473 381 GPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHfmLVSE--MPHGGQKQSGYGKDMSL 458
|
490
....*....|....*.
gi 966941000 472 DSYDFFTEIKTITVKH 487
Cdd:PRK13473 459 YGLEDYTVVRHVMVKH 474
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
28-485 |
1.12e-159 |
|
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: 460.26 E-value: 1.12e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTMDI 107
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 108 PRSVQNFRFFASSILH------------HTSectqmdhlgcmhYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTV 175
Cdd:cd07092 82 PGAVDNFRFFAGAARTlegpaageylpgHTS------------MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 176 VAKPSELTSVTAWMLCTLLdKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELG 255
Cdd:cd07092 150 VLKPSETTPLTTLLLAELA-AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 256 GKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHL 335
Cdd:cd07092 229 GKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 336 EKVRSYVKRAlAEGAQIWCGEGvdklnlpARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNV 415
Cdd:cd07092 309 ERVAGFVERA-PAHARVLTGGR-------RAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDV 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 416 KYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07092 381 EYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
11-483 |
2.15e-159 |
|
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: 460.18 E-value: 2.15e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 11 ENFIDGKFLPCSSYIDSYDPS-TGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQ 89
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 90 AESKDQGKTLALARTmDIPRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAI 169
Cdd:cd07097 82 LLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 170 AAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK 249
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 250 LSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGAL 329
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 330 ISKAHLEKVRSYVKRALAEGAQIWCGeGvDKLNLPARsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVI 409
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGAKLVYG-G-ERLKRPDE---GYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEAL 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966941000 410 ERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLI-RELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTI 483
Cdd:cd07097 396 AIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
27-485 |
3.89e-154 |
|
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: 446.30 E-value: 3.89e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 27 SYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSR-SPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTm 105
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 106 DIPRSVQNFRFFASSI--LHHTSECTQMDHLGcmhYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELT 183
Cdd:cd07109 80 DVEAAARYFEYYGGAAdkLHGETIPLGPGYFV---YTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 184 SVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIF 263
Cdd:cd07109 157 PLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 264 EDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLaSMGALISKAHLEKVRSYVK 343
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDP-DLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 344 RALAEGAQIWCGEGVdklnLPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATV 423
Cdd:cd07109 316 RARARGARIVAGGRI----AEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966941000 424 WSSNVGRVHRVAKKLQSGLVWTNCWLIRE-LNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNYGAGGgIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
12-485 |
2.10e-153 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 445.48 E-value: 2.10e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 12 NFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQ 89
Cdd:PRK13252 9 LYIDGAYVEATSgeTFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 90 AESKDQGKTLALARTMDIPRSVQNFRFFASsiLHHTSECTQMDHLGC-MHYTVRAPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:PRK13252 89 LETLDTGKPIQETSVVDIVTGADVLEYYAG--LAPALEGEQIPLRGGsFVYTRREPLGVCAGIGAWNYPIQIACWKSAPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 169 IAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGpRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCK 248
Cdd:PRK13252 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 249 KLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGA 328
Cdd:PRK13252 246 EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 329 LISKAHLEKVRSYVKRALAEGAQIWC-GEGVDklnlPARSQAGYFMLPTVITDIKDEsccMT---EEIFGPVTCVVPFDS 404
Cdd:PRK13252 326 LVSFAHRDKVLGYIEKGKAEGARLLCgGERLT----EGGFANGAFVAPTVFTDCTDD---MTivrEEIFGPVMSVLTFDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 405 EEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:PRK13252 399 EDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQ 478
|
.
gi 966941000 485 V 485
Cdd:PRK13252 479 V 479
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
29-484 |
7.58e-153 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 442.95 E-value: 7.58e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 29 DPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArTMDIP 108
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 109 RSVQNFRFFAS---SILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSV 185
Cdd:cd07110 82 DVAGCFEYYADlaeQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 186 TAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFED 265
Cdd:cd07110 162 TELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 266 ANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRA 345
Cdd:cd07110 242 ADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 346 LAEGAQIWCGEGVdklnlPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWS 425
Cdd:cd07110 322 KEEGARLLCGGRR-----PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 966941000 426 SNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
13-485 |
1.42e-152 |
|
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: 443.39 E-value: 1.42e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCS--SYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSR-SPQERSRVLNQVADLLEQSLEEFAQ 89
Cdd:cd07144 11 FINNEFVKSSdgETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 90 AESKDQGKTLALARTMDIPRSVQNFRFFASSILHHTSECTQMDHlGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAI 169
Cdd:cd07144 91 IEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSP-NKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 170 AAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK 249
Cdd:cd07144 170 AAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 250 LSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRK-WKVGIPSDPLASMGA 328
Cdd:cd07144 250 VTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 329 LISKAHLEKVRSYVKRALAEGAQIWCGEGVDKLNLparsQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:cd07144 330 QVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGL----GKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966941000 409 IERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
28-485 |
6.07e-152 |
|
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: 440.43 E-value: 6.07e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARtMDI 107
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ-FEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 108 PRSVQNFRFFAS-----SILHHTSECTQMDHlgcmhytvRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSEL 182
Cdd:cd07106 81 GGAVAWLRYTASldlpdEVIEDDDTRRVELR--------RKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 183 TSVTAWMLCTLLDKAgVPPGVVNIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAII 262
Cdd:cd07106 153 TPLCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 263 FEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYV 342
Cdd:cd07106 231 LPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 343 KRALAEGAQIWCGEGVDKLNlparsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAAT 422
Cdd:cd07106 311 EDAKAKGAKVLAGGEPLDGP-------GYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGAS 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966941000 423 VWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07106 384 VWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
30-485 |
6.27e-151 |
|
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: 437.92 E-value: 6.27e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 30 PSTGEVYCRVPNSGKDEIEAAVKAAREAFP-GWSSRSP-QERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTmDI 107
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDkGPWPRMSgAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 108 PRSVQNFRFFAS--SILHHTSectqMDHLG--CMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELT 183
Cdd:cd07118 83 EGAADLWRYAASlaRTLHGDS----YNNLGddMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 184 SVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIF 263
Cdd:cd07118 159 SGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 264 EDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVK 343
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 344 RALAEGAQIWCGEGVdklnlpARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATV 423
Cdd:cd07118 319 AGRAEGATLLLGGER------LASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966941000 424 WSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07118 393 WSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
52-485 |
1.04e-148 |
|
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: 428.96 E-value: 1.04e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 52 KAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARtMDIPRSVQNFRFFASSILHHTSECTQM 131
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 132 DHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTG 211
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 212 PRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTS 291
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 292 RIFVQKSIYTEFLKRFVeatrkwkvgipsdplasmgaliskahlekvrsyvkralaegaqiwcgegvdklnlparsqagy 371
Cdd:cd06534 240 RLLVHESIYDEFVEKLV--------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 372 fmlpTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLI- 450
Cdd:cd06534 257 ----TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIg 332
|
410 420 430
....*....|....*....|....*....|....*
gi 966941000 451 RELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd06534 333 VGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
28-483 |
1.78e-148 |
|
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: 432.05 E-value: 1.78e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWS-SRSPQERSRVLNQVADLLEQSLEEFA---QAESkdqGKTLALAR 103
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRallVAEV---GAPVMTAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 104 TMDIPRSVQNFRFFASSILHHTSECT---QMDHLGCMHYTV-RAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKP 179
Cdd:cd07089 79 AMQVDGPIGHLRYFADLADSFPWEFDlpvPALRGGPGRRVVrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 180 SELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNP 259
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 260 AIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVR 339
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 340 SYVKRALAEGAQIWCGEGVdklnlPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGL 419
Cdd:cd07089 319 GYIARGRDEGARLVTGGGR-----PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966941000 420 AATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07089 394 SGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
13-485 |
5.56e-148 |
|
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: 431.49 E-value: 5.56e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQA 90
Cdd:cd07117 4 FINGEWVKGSSgeTIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 91 ESKDQGKTLALARTMDIPRSVQNFRFFASSILHHTSECTQMDHlGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:cd07117 84 ETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDE-DTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 171 AGNTVVAKPSELTSVTAWMLCTLLDKAgVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKL 250
Cdd:cd07117 163 AGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 251 SLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALI 330
Cdd:cd07117 242 TLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 331 SKAHLEKVRSYVKRALAEGAQIWCGEGvdKLnLPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIE 410
Cdd:cd07117 322 NKDQLDKILSYVDIAKEEGAKILTGGH--RL-TENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966941000 411 RANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07117 399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
13-483 |
1.32e-147 |
|
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: 430.38 E-value: 1.32e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFP--GWSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07142 7 FINGQFVDAASgkTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESKDQGKTLALARTMDIPRSVQNFRFFA--SSILHHTSECTQMDHLGcmhYTVRAPVGVAGLISPWNLPLYLLTWKIA 166
Cdd:cd07142 87 ALETWDNGKPYEQARYAEVPLAARLFRYYAgwADKIHGMTLPADGPHHV---YTLHEPIGVVGQIIPWNFPLLMFAWKVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 167 PAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA-P 245
Cdd:cd07142 164 PALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAkS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 246 HCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLAS 325
Cdd:cd07142 244 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 326 MGALISKAHLEKVRSYVKRALAEGAQIWCGEGvdklnlpARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 405
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITGGD-------RIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966941000 406 EEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
13-483 |
2.00e-147 |
|
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: 429.76 E-value: 2.00e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQA 90
Cdd:cd07088 1 YINGEFVPSSSgeTIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 91 ESKDQGKTLALARtMDIPRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:cd07088 81 IVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 171 AGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKL 250
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 251 SLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALI 330
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 331 SKAHLEKVRSYVKRALAEGAQIWCGEGVDKLnlparsQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIE 410
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGATLLTGGKRPEG------EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966941000 411 RANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
13-485 |
2.00e-146 |
|
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: 427.38 E-value: 2.00e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPG--WSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07139 2 FIGGRWVAPSGseTIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESKDQGKTLALARTMDIPRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 169 IAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCK 248
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 249 KLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGA 328
Cdd:cd07139 241 RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 329 LISKAHLEKVRSYVKRALAEGAQIWCGEGVdklnlPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:cd07139 321 LASARQRERVEGYIAKGRAEGARLVTGGGR-----PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966941000 409 IERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNcWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-487 |
5.89e-146 |
|
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: 426.38 E-value: 5.89e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 12 NFIDGKFLPCSS--YIDSYDPSTG-EVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07131 1 NYIGGEWVDSASgeTFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESKDQGKTLALARTmDIPRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07131 81 RLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 169 IAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCK 248
Cdd:cd07131 160 LVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 249 KLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGA 328
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 329 LISKAHLEKVRSYVKRALAEGAQIWCG-EGVDKLNLparsQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEE 407
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGgERLTGGGY----EKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 408 VIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLI-RELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTITV 485
Cdd:cd07131 396 AIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
|
..
gi 966941000 486 KH 487
Cdd:cd07131 476 DY 477
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
29-485 |
8.62e-146 |
|
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: 425.24 E-value: 8.62e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 29 DPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLalaRTMDIP 108
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNAL---RTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 109 R---SVQNFRFF---ASSILHHTSECtqmdHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSEL 182
Cdd:cd07108 80 EaavLADLFRYFgglAGELKGETLPF----GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 183 TSVTAWMLCTLLDKAgVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAII 262
Cdd:cd07108 156 APLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 263 FEDANLDECIPATVRSS-FANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSY 341
Cdd:cd07108 235 FPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 342 VK--RALAEGAQIWCGegvdKLNLPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGL 419
Cdd:cd07108 315 IDlgLSTSGATVLRGG----PLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966941000 420 AATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSY-DFFTEIKTITV 485
Cdd:cd07108 391 AAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMlEHFTQKKTVNI 457
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
13-481 |
3.89e-145 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 423.84 E-value: 3.89e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQA 90
Cdd:TIGR01804 1 FIDGEYVEDSAgtTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 91 ESKDQGKTLALARTMDIPRSVQNFRFFASSILHHTSEctQMDHLGC-MHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAI 169
Cdd:TIGR01804 81 ETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGE--IIPLGGPsFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 170 AAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK 249
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 250 LSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGAL 329
Cdd:TIGR01804 239 VTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 330 ISKAHLEKVRSYVKRALAEGAQIWCGEGVdkLNLPArSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVI 409
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGR--PENVG-LQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVI 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966941000 410 ERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIK 481
Cdd:TIGR01804 396 ARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
12-486 |
5.59e-145 |
|
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: 424.07 E-value: 5.59e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 12 NFIDGKFLPcssyidSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAF-PG--WSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07141 17 DSVSGKTFP------TINPATGEKICEVQEGDKADVDKAVKAARAAFkLGspWRTMDASERGRLLNKLADLIERDRAYLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESKDQGKTLALARTMDIPRSVQNFRFFASSILHHTSECTQMDHlGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07141 91 SLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDG-DFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 169 IAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA-PHC 247
Cdd:cd07141 170 LACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGkSNL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 248 KKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMG 327
Cdd:cd07141 250 KRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 328 ALISKAHLEKVRSYVKRALAEGAQIWCGEGvdklnlpARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEE 407
Cdd:cd07141 330 PQIDEEQFKKILELIESGKKEGAKLECGGK-------RHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDE 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966941000 408 VIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITVK 486
Cdd:cd07141 403 VIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-481 |
3.18e-143 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 420.25 E-value: 3.18e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 7 LLMLENFIDGKFLpcSSY----IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQ 82
Cdd:PLN02278 22 LLRTQGLIGGKWT--DAYdgktFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 83 SLEEFAQAESKDQGKTLALARTmDIPRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLT 162
Cdd:PLN02278 100 NKEDLAQLMTLEQGKPLKEAIG-EVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMIT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 163 WKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQL 242
Cdd:PLN02278 179 RKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 243 SAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDP 322
Cdd:PLN02278 259 AAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 323 LASMGALISKAHLEKVRSYVKRALAEGAQIWCGEgvdklnlPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPF 402
Cdd:PLN02278 339 GVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGG-------KRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRF 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966941000 403 DSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIK 481
Cdd:PLN02278 412 KTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
13-483 |
2.57e-142 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 418.07 E-value: 2.57e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPG--WSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:PLN02766 24 FINGEFVDAASgkTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESKDQGKTLALARTMDIPRSVQNFRFFASSILHHTSECTQMDHlGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSR-QLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 169 IAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA-PHC 247
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAtSNL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 248 KKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMG 327
Cdd:PLN02766 263 KQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 328 ALISKAHLEKVRSYVKRALAEGAQIWCGEgvdklnlPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEE 407
Cdd:PLN02766 343 PQVDKQQFEKILSYIEHGKREGATLLTGG-------KPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966941000 408 VIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
25-485 |
1.31e-141 |
|
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: 414.44 E-value: 1.31e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARt 104
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 105 MDIPRSVQNFRFFASSILHHTSECTQMD----HLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPS 180
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 181 ELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPA 260
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 261 IIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRS 340
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 341 YVKRALAEGAQIWCGegvdklnlpARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLA 420
Cdd:cd07145 320 LVNDAVEKGGKILYG---------GKRDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQ 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966941000 421 ATVWSSNVGRVHRVAKKLQSGLVWTN-CWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07145 391 ASVFTNDINRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
13-486 |
2.57e-141 |
|
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: 414.62 E-value: 2.57e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPC--SSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPG-WS-SRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07143 10 FINGEFVDSvhGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGlKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESKDQGKTLALARTMDIPRSVQNFRFF---ASSILHHTSEcTQMDHLGcmhYTVRAPVGVAGLISPWNLPLYLLTWKI 165
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFRYYggwADKIHGQVIE-TDIKKLT---YTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 166 APAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA- 244
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 245 PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLA 324
Cdd:cd07143 246 SNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 325 SMGALISKAHLEKVRSYVKRALAEGAQIWCGeGVDKLNLparsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 404
Cdd:cd07143 326 FQGPQVSQIQYERIMSYIESGKAEGATVETG-GKRHGNE------GYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 405 EEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07143 399 EEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVH 478
|
..
gi 966941000 485 VK 486
Cdd:cd07143 479 IN 480
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
46-485 |
2.01e-140 |
|
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: 410.38 E-value: 2.01e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 46 EIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArtmdiprsvqNFRF-FASSILHH 124
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKA----------AFEVgAAIAILRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 125 -TSECTQM-------DHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVT-AWMLCTLLD 195
Cdd:cd07104 71 aAGLPRRPegeilpsDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 196 KAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPAT 275
Cdd:cd07104 151 EAGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 276 VRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRALAEGAQIWCG 355
Cdd:cd07104 231 AFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 356 EGVDklnlparsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVA 435
Cdd:cd07104 311 GTYE----------GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFA 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 966941000 436 KKLQSGLVWTNCWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07104 381 ERLETGMVHINDQTVNdEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
27-485 |
2.75e-140 |
|
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: 410.97 E-value: 2.75e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 27 SYDPSTGEVYCRVPNSGKDEIEAAVKAAREAF--PGWSsRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARt 104
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 105 MDIPRSVQNFRFFASSILHHTSECTQMDHlGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTS 184
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIEPEP-GSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 185 VTAWMLCTLLDKA-GVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIF 263
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 264 EDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVK 343
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 344 RALAEGAQIWC-GEGVDKlnlpaRSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAAT 422
Cdd:cd07120 318 RAIAAGAEVVLrGGPVTE-----GLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966941000 423 VWSSNVGRVHRVAKKLQSGLVWTNCW--LIRELNlpFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07120 393 VWTRDLARAMRVARAIRAGTVWINDWnkLFAEAE--EGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
26-485 |
4.06e-140 |
|
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: 410.57 E-value: 4.06e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 26 DSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALA--R 103
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAwfE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 104 TMDIPRSVQNfrffASSILHH-TSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSEL 182
Cdd:cd07150 82 TTFTPELLRA----AAGECRRvRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 183 TSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAII 262
Cdd:cd07150 158 TPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 263 FEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYV 342
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 343 KRALAEGAQIWCGEGVDklnlparsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAAT 422
Cdd:cd07150 318 EDAVAKGAKLLTGGKYD----------GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966941000 423 VWSSNVGRVHRVAKKLQSGLVWTNCWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07150 388 ILTNDLQRAFKLAERLESGMVHINDPTILdEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
13-487 |
2.40e-139 |
|
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: 409.52 E-value: 2.40e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPG-WSSRSPQERSRVLNQVADLLEQSLEEFAQ 89
Cdd:cd07113 3 FIDGRPVAGQSekRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 90 AESKDQGKTLALARTMDIPRSVQNFRFFASSILHHTSECTQ-----MDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWK 164
Cdd:cd07113 83 LETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLApsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 165 IAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGpRVGEALVSHPEVPLISFTGSQPTAERITQLSA 244
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 245 PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLA 324
Cdd:cd07113 242 SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 325 SMGALISKAHLEKVRSYVKRALAEGAQIWCGEGvdklnlpARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 404
Cdd:cd07113 322 MFGPLANQPHFDKVCSYLDDARAEGDEIVRGGE-------ALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYED 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 405 EEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:cd07113 395 EEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
...
gi 966941000 485 VKH 487
Cdd:cd07113 475 IRY 477
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
13-472 |
1.23e-137 |
|
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: 405.24 E-value: 1.23e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCS--SYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQA 90
Cdd:cd07111 25 FINGKWVKPEnrKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 91 ESKDQGKTLALARTMDIPRSVQNFrffassiLHHTSECTQMDHLGCMHytvrAPVGVAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:cd07111 105 ESLDNGKPIRESRDCDIPLVARHF-------YHHAGWAQLLDTELAGW----KPVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 171 AGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGpRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKL 250
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 251 SLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALI 330
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 331 SKAHLEKVRSYVKRALAEGAQIWCGEGvdklNLPARsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIE 410
Cdd:cd07111 333 DPAQLKRIRELVEEGRAEGADVFQPGA----DLPSK---GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVA 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966941000 411 RANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKD 472
Cdd:cd07111 406 LANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKE 467
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
25-485 |
3.97e-137 |
|
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: 402.74 E-value: 3.97e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALART 104
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 105 mDIPRSVQNFRFFASSILHHTSECTQMD----HLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPS 180
Cdd:cd07149 81 -EVDRAIETLRLSAEEAKRLAGETIPFDaspgGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 181 ELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAphCKKLSLELGGKNPA 260
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 261 IIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRS 340
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 341 YVKRALAEGAQIWCGEGVDklnlparsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLA 420
Cdd:cd07149 318 WVEEAVEGGARLLTGGKRD----------GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQ 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966941000 421 ATVWSSNVGRVHRVAKKLQSGLVwtncwLIREL------NLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07149 388 AGVFTNDLQKALKAARELEVGGV-----MINDSstfrvdHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
11-487 |
4.60e-136 |
|
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: 401.06 E-value: 4.60e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 11 ENFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07116 2 DNFIGGEWVAPVKgeYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESKDQGKTLALARTMDIPRSVQNFRFFASSILHHTSECTQMDHlGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDE-NTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 169 IAAGNTVVAKPSELTSVTAWMLCTLLDKAgVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCK 248
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 249 KLSLELGGKNPAIIFE------DANLDECIPATVRSSFaNQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDP 322
Cdd:cd07116 240 PVTLELGGKSPNIFFAdvmdadDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 323 LASMGALISKAHLEKVRSYVKRALAEGAQIWCGEgvDKLNLPARSQAGYFMLPTVITDIKDEscCMTEEIFGPVTCVVPF 402
Cdd:cd07116 319 ETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGG--ERNELGGLLGGGYYVPTTFKGGNKMR--IFQEEIFGPVLAVTTF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 403 DSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKT 482
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKN 474
|
....*
gi 966941000 483 ITVKH 487
Cdd:cd07116 475 LLVSY 479
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
29-485 |
8.78e-133 |
|
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: 391.74 E-value: 8.78e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 29 DPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTmDIP 108
Cdd:cd07107 3 NPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-DVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 109 RSVQNFRFFASSILHHTSECTQMDHlGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAW 188
Cdd:cd07107 82 VAAALLDYFAGLVTELKGETIPVGG-RNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 189 MLCTLLDKAgVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANL 268
Cdd:cd07107 161 RLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 269 DECIPATVRS-SFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRALA 347
Cdd:cd07107 240 EAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 348 EGAQIWCGEGVDKLNLPArsqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSN 427
Cdd:cd07107 320 EGARLVTGGGRPEGPALE---GGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 966941000 428 VGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07107 397 ISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
13-487 |
3.53e-131 |
|
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: 388.78 E-value: 3.53e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPG--WSSRSPQERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07140 9 FINGEFVDAEGgkTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESKDQGKTLALARTMDIPRSVQNFRFFA---SSILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKI 165
Cdd:cd07140 89 TIESLDSGAVYTLALKTHVGMSIQTFRYFAgwcDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYPLMMLAWKM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 166 APAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA- 244
Cdd:cd07140 169 AACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAv 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 245 PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLA 324
Cdd:cd07140 249 SNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRST 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 325 SMGALISKAHLEKVRSYVKRALAEGAQIWCGEgvDKLNLParsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 404
Cdd:cd07140 329 DHGPQNHKAHLDKLVEYCERGVKEGATLVYGG--KQVDRP-----GFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 405 E--EEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKT 482
Cdd:cd07140 402 GdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKT 481
|
....*
gi 966941000 483 ITVKH 487
Cdd:cd07140 482 VTIEY 486
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
13-484 |
1.63e-128 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 382.54 E-value: 1.63e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCS--SYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPG-----WSSRSPQERSRVLNQVADLLEQSLE 85
Cdd:PLN02467 11 FIGGEWREPVlgKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 86 EFAQAESKDQGKTLALArTMDIPRSVQNFRFFASsiLHHTSECTQ-------MDHLGCmhYTVRAPVGVAGLISPWNLPL 158
Cdd:PLN02467 91 ELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYAD--LAEALDAKQkapvslpMETFKG--YVLKEPLGVVGLITPWNYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 159 YLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAER 238
Cdd:PLN02467 166 LMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 239 ITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGI 318
Cdd:PLN02467 246 IMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 319 PSDPLASMGALISKAHLEKVRSYVKRALAEGAQIWCGeGVDklnlPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTC 398
Cdd:PLN02467 326 PLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCG-GKR----PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 399 VVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFT 478
Cdd:PLN02467 401 VKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYL 480
|
....*.
gi 966941000 479 EIKTIT 484
Cdd:PLN02467 481 SVKQVT 486
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
12-487 |
9.71e-128 |
|
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: 379.60 E-value: 9.71e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 12 NFIDGKFLPCSS-YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQA 90
Cdd:cd07086 1 GVIGGEWVGSGGeTFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 91 ESKDQGKTLALARTmdiprSVQNF---RFFA---SSILH-HTSECTQMDHlgcMHYTVRAPVGVAGLISPWNLPLYLLTW 163
Cdd:cd07086 81 VSLEMGKILPEGLG-----EVQEMidiCDYAvglSRMLYgLTIPSERPGH---RLMEQWNPLGVVGVITAFNFPVAVPGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 164 KIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKA----GVPPGVVNIVFGTGPrVGEALVSHPEVPLISFTGSQPTAERI 239
Cdd:cd07086 153 NAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 240 TQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIP 319
Cdd:cd07086 232 GETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 320 SDPLASMGALISKAHLEKVRSYVKRALAEGAQIWCGEGVdklnlPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCV 399
Cdd:cd07086 312 LDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKR-----IDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 400 VPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRV--AKKLQSGLVWTNCWLI-RELNLPFGGMKSSGIGREGAKDSYDF 476
Cdd:cd07086 387 IKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSgAEIGGAFGGEKETGGGRESGSDAWKQ 466
|
490
....*....|.
gi 966941000 477 FTEIKTITVKH 487
Cdd:cd07086 467 YMRRSTCTINY 477
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
13-486 |
5.10e-126 |
|
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: 376.56 E-value: 5.10e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSSYIDSYDPS-TGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAE 91
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 92 SKDQGK--TLALArtmDIPRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRaPVGVAGLISPWNLPLYLLTWKIAPAI 169
Cdd:cd07124 116 VLEVGKnwAEADA---DVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTTAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 170 AAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA----- 244
Cdd:cd07124 192 VTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkvqpg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 245 -PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPL 323
Cdd:cd07124 272 qKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 324 ASMGALISKAHLEKVRSYVKRALAEGaQIWCGEGVdklnlPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFD 403
Cdd:cd07124 352 VYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEV-----LELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 404 SEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTN-----CWLIRElnlPFGGMKSSGIG-REGAKDSYDFF 477
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkitgALVGRQ---PFGGFKMSGTGsKAGGPDYLLQF 502
|
....*....
gi 966941000 478 TEIKTITVK 486
Cdd:cd07124 503 MQPKTVTEN 511
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
13-483 |
4.17e-125 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 375.30 E-value: 4.17e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAF---PgWSSRSPQERSRVLNQVADLLEQSLEEF 87
Cdd:PLN02466 61 LINGQFVDAASgkTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFdegP-WPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 88 AQAESKDQGKTLALARTMDIPRSVQNFRFF---ASSILHHTSECTQMDHLGCMHytvrAPVGVAGLISPWNLPLYLLTWK 164
Cdd:PLN02466 140 AALETWDNGKPYEQSAKAELPMFARLFRYYagwADKIHGLTVPADGPHHVQTLH----EPIGVAGQIIPWNFPLLMFAWK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 165 IAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA 244
Cdd:PLN02466 216 VGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 245 -PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPL 323
Cdd:PLN02466 296 kSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 324 ASMGALISKAHLEKVRSYVKRALAEGAQIWCGEgvDKLnlparSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFD 403
Cdd:PLN02466 376 VEQGPQIDSEQFEKILRYIKSGVESGATLECGG--DRF-----GSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 404 SEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PLN02466 449 DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
46-485 |
3.91e-124 |
|
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: 368.83 E-value: 3.91e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 46 EIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARtMDIPRSVQNFRFFASSILHHT 125
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAG-FNVDLAAGMLREAASLITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 126 SECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVN 205
Cdd:cd07105 80 GGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 206 IVF---GTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFAN 282
Cdd:cd07105 160 VVThspEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 283 QGEICLCTSRIFVQKSIYTEFLKRFVEATRKwkvgIPSDPlASMGALISKAHLEKVRSYVKRALAEGAQIWCGegvdklN 362
Cdd:cd07105 240 SGQICMSTERIIVHESIADEFVEKLKAAAEK----LFAGP-VVLGSLVSAAAADRVKELVDDALSKGAKLVVG------G 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 363 LPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGL 442
Cdd:cd07105 309 LADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 966941000 443 VWTNCWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07105 389 VHINGMTVHdEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
10-486 |
6.49e-124 |
|
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: 369.92 E-value: 6.49e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 10 LENFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEF 87
Cdd:cd07085 1 LKLFINGEWVESKTteWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 88 AQAESKDQGKTLALARTmDIPRSVQNFRFfASSILHH----TSE--CTQMDHlgcmhYTVRAPVGVAGLISPWNLPLYLL 161
Cdd:cd07085 81 ARLITLEHGKTLADARG-DVLRGLEVVEF-ACSIPHLlkgeYLEnvARGIDT-----YSYRQPLGVVAGITPFNFPAMIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 162 TWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQ 241
Cdd:cd07085 154 LWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 242 LSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSD 321
Cdd:cd07085 233 RAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 322 PLASMGALISKAHLEKVRSYVKRALAEGAQIWC-GEGVDKLNLParsqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVV 400
Cdd:cd07085 313 PGADMGPVISPAAKERIEGLIESGVEEGAKLVLdGRGVKVPGYE----NGNFVGPTILDNVTPDMKIYKEEIFGPVLSIV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 401 PFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVwtncwlirELNLP---------FGGMKSSGIGREGA- 470
Cdd:cd07085 389 RVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMV--------GINVPipvplaffsFGGWKGSFFGDLHFy 460
|
490
....*....|....*..
gi 966941000 471 -KDSYDFFTEIKTITVK 486
Cdd:cd07085 461 gKDGVRFYTQTKTVTSR 477
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
25-487 |
4.60e-123 |
|
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: 367.40 E-value: 4.60e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArT 104
Cdd:cd07151 12 IDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKA-N 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 105 MDIPRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTS 184
Cdd:cd07151 91 IEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 185 VTAWML-CTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIF 263
Cdd:cd07151 171 ITGGLLlAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 264 EDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVK 343
Cdd:cd07151 251 EDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 344 RALAEGAQIWCGEGVDklnlparsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATV 423
Cdd:cd07151 331 QAVEEGATLLVGGEAE----------GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966941000 424 WSSNVGRVHRVAKKLQSGLVWTNCWLIR-ELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITVKH 487
Cdd:cd07151 401 FTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQH 465
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
25-485 |
3.23e-121 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 362.14 E-value: 3.23e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARt 104
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 105 MDIPRSVQNFRFFASSILHHTSECTQMD----HLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPS 180
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRGEEIPLDatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 181 ELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAphCKKLSLELGGKNPA 260
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 261 IIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRS 340
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 341 YVKRALAEGAQIWCGEgvdklnlparSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLA 420
Cdd:cd07094 318 WVEEAVEAGARLLCGG----------ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966941000 421 ATVWSSNVGRVHRVAKKLQSGLVWTN-CWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07094 388 AGIFTRDLNVAFKAAEKLEVGGVMVNdSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
28-485 |
2.93e-120 |
|
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: 359.61 E-value: 2.93e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTmDI 107
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL-EV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 108 PRSVQNFRFFASS---ILH----HTSECTqMDHLGCMHYTvraPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPS 180
Cdd:cd07099 80 LLALEAIDWAARNaprVLAprkvPTGLLM-PNKKATVEYR---PYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 181 ELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPrVGEALVSHpEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPA 260
Cdd:cd07099 156 EVTPLVGELLAEAWAAAGPPQGVLQVVTGDGA-TGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 261 IIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRS 340
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 341 YVKRALAEGAQIWCGegvdklNLPARSQaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLA 420
Cdd:cd07099 314 HVDDAVAKGAKALTG------GARSNGG-GPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966941000 421 ATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07099 387 ASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIpaLPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
5-483 |
1.01e-115 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 349.58 E-value: 1.01e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 5 KAL-LMLEN--FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPG--WSSRSPQERSRVLNQVA 77
Cdd:PRK09847 12 KALsLAIENrlFINGEYTAAAEneTFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 78 DLLEQSLEEFAQAESKDQGKTLALARTMDIPRSVQNFRFFASSILHHTSECTQMDHlGCMHYTVRAPVGVAGLISPWNLP 157
Cdd:PRK09847 92 DLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSS-HELAMIVREPVGVIAAIVPWNFP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 158 LYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAE 237
Cdd:PRK09847 171 LLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 238 RITQLSA-PHCKKLSLELGGKNPAIIFEDA-NLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWK 315
Cdd:PRK09847 251 QLLKDAGdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 316 VGIPSDPLASMGALISKAHLEKVRSYVKRALAEGaqiwcgegvdKLNLPARSQAGYFML-PTVITDIKDESCCMTEEIFG 394
Cdd:PRK09847 331 PGHPLDPATTMGTLIDCAHADSVHSFIREGESKG----------QLLLDGRNAGLAAAIgPTIFVDVDPNASLSREEIFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 395 PVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSY 474
Cdd:PRK09847 401 PVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHAL 480
|
....*....
gi 966941000 475 DFFTEIKTI 483
Cdd:PRK09847 481 EKFTELKTI 489
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
25-487 |
1.45e-113 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 344.94 E-value: 1.45e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEE---FAQAESkdqGKTLAL 101
Cdd:PRK09407 34 REVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREElldLVQLET---GKARRH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 102 A--RTMDIPrsvQNFRFFASS---------------ILHHTSEctqmdhlgcmhytVRAPVGVAGLISPWNLPLYLLTWK 164
Cdd:PRK09407 111 AfeEVLDVA---LTARYYARRapkllaprrragalpVLTKTTE-------------LRQPKGVVGVISPWNYPLTLAVSD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 165 IAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHpeVPLISFTGSQPTAERITQLSA 244
Cdd:PRK09407 175 AIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 245 PHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLA 324
Cdd:PRK09407 253 RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 325 SMGALISKAHLEKVRSYVKRALAEGAQIWCGeGVdklnlpARSQAG-YFMLPTVITDIKDESCCMTEEIFGPVTCVVPFD 403
Cdd:PRK09407 333 DMGSLISEAQLETVSAHVDDAVAKGATVLAG-GK------ARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 404 SEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTN-----CWliRELNLPFGGMKSSGIGREGAKDSYDFFT 478
Cdd:PRK09407 406 DVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAW--GSVDAPMGGMKDSGLGRRHGAEGLLKYT 483
|
....*....
gi 966941000 479 EIKTITVKH 487
Cdd:PRK09407 484 ESQTIATQR 492
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
29-485 |
8.14e-113 |
|
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: 340.83 E-value: 8.14e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 29 DPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFA---QAESkdqGKTLALA--R 103
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLdliQLET---GKARRHAfeE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 104 TMDIprsVQNFRFFASS---------------ILHHTSECtqmdhlgcmhytvRAPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07101 79 VLDV---AIVARYYARRaerllkprrrrgaipVLTRTTVN-------------RRPKGVVGVISPWNYPLTLAVSDAIPA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 169 IAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEvpLISFTGSQPTAERITQLSAPHCK 248
Cdd:cd07101 143 LLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD--YVMFTGSTATGRVVAERAGRRLI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 249 KLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGA 328
Cdd:cd07101 221 GCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 329 LISKAHLEKVRSYVKRALAEGAQIWCGeGVdklnlpARSQAG-YFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEE 407
Cdd:cd07101 301 LISQAQLDRVTAHVDDAVAKGATVLAG-GR------ARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 408 VIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTN-----CWliRELNLPFGGMKSSGIGREGAKDSYDFFTEIKT 482
Cdd:cd07101 374 AIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNegyaaAW--ASIDAPMGGMKDSGLGRRHGAEGLLKYTETQT 451
|
...
gi 966941000 483 ITV 485
Cdd:cd07101 452 VAV 454
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
33-485 |
2.79e-110 |
|
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: 333.88 E-value: 2.79e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 33 GEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArtmDIPRSVq 112
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKA---GFEVGA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 113 nfrffASSILHHTSEC-TQ-MDHL-----GCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSV 185
Cdd:cd07152 77 -----AIGELHEAAGLpTQpQGEIlpsapGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 186 TA-WMLCTLLDKAGVPPGVVNIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFE 264
Cdd:cd07152 152 SGgVVIARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 265 DANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKR 344
Cdd:cd07152 231 DADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 345 ALAEGAQIWCGEGVDklnlparsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVW 424
Cdd:cd07152 311 SVAAGARLEAGGTYD----------GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGII 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966941000 425 SSNVGRVHRVAKKLQSGLVWTN-CWLIRELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTITV 485
Cdd:cd07152 381 SRDVGRAMALADRLRTGMLHINdQTVNDEPHNPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
25-481 |
3.50e-110 |
|
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: 333.83 E-value: 3.50e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALART 104
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 105 mDIPRSVQNFRFFASSILHHTSECTQMD----HLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPS 180
Cdd:cd07147 81 -EVARAIDTFRIAAEEATRIYGEVLPLDisarGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 181 ELTSVTAWMLCTLLDKAGVPPGVVNIVfgtgP---RVGEALVSHPEVPLISFTGSQPTAERITQLsAPHcKKLSLELGGK 257
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVL----PcsrDDADLLVTDERIKLLSFTGSPAVGWDLKAR-AGK-KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 258 NPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEK 337
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 338 VRSYVKRALAEGAQIWCGEGVDklnlparsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKY 417
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGKRD----------GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKF 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966941000 418 GLAATVWSSNVGRVHRVAKKLQSGLVWTN---CWliRELNLPFGGMKSSGIGREGAKDSYDFFTEIK 481
Cdd:cd07147 384 GLQAGVFTRDLEKALRAWDELEVGGVVINdvpTF--RVDHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
29-485 |
1.73e-108 |
|
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: 329.70 E-value: 1.73e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 29 DPSTGEVYCRVPnsgKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARtMDIP 108
Cdd:cd07146 5 NPYTGEVVGTVP---AGTEEALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR-YEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 109 RSVQNFRFFASSILHHTSECTQMD-------HLGcmhYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSE 181
Cdd:cd07146 81 RAADVLRFAAAEALRDDGESFSCDltangkaRKI---FTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 182 LTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAphCKKLSLELGGKNPAI 261
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 262 IFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSY 341
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 342 VKRALAEGAQIWCGEGVDklnlparsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAA 421
Cdd:cd07146 316 VEEAIAQGARVLLGNQRQ----------GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSS 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966941000 422 TVWSSNVGRVHRVAKKLQSGLVwtNCWLI---RELNLPFGGMKSSGIG-REGAKDSYDFFTEIKTITV 485
Cdd:cd07146 386 GVCTNDLDTIKRLVERLDVGTV--NVNEVpgfRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
11-486 |
1.88e-107 |
|
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: 327.61 E-value: 1.88e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 11 ENFIDGKFLPCS-SYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSP-QERSRVLNQVADLLEQSLEEFA 88
Cdd:cd07082 3 KYLINGEWKESSgKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESKDQGKTLALArTMDIPRSVQNFRFFASSILHHTSECTQMD----HLGCMHYTVRAPVGVAGLISPWNLPLYLLTWK 164
Cdd:cd07082 83 NLLMWEIGKTLKDA-LKEVDRTIDYIRDTIEELKRLDGDSLPGDwfpgTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 165 IAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSa 244
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQH- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 245 pHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLA 324
Cdd:cd07082 241 -PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 325 SMGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDKLNLparsqagyfMLPTVITDIKDESCCMTEEIFGPVTCVVPFDS 404
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGNL---------IYPTLLDPVTPDMRLAWEEPFGPVLPIIRVND 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 405 EEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIREL-NLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07082 391 IEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPdHFPFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
...
gi 966941000 484 TVK 486
Cdd:cd07082 471 VIN 473
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
47-485 |
4.68e-105 |
|
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: 319.79 E-value: 4.68e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 47 IEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTmDIPRSVQNFRFFA---SSILh 123
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYYAenaEAFL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 124 htsECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGV 203
Cdd:cd07100 79 ---ADEPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 204 VNIVFGTGPRVgEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQ 283
Cdd:cd07100 156 FQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 284 GEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDKlnl 363
Cdd:cd07100 235 GQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPD--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 364 parsQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLV 443
Cdd:cd07100 312 ----GPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 966941000 444 WTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07100 388 FINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
73-466 |
1.40e-100 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 307.82 E-value: 1.40e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 73 LNQVADLLEQSLEEFAQAESKDQGKTLALARTmDIPRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRAPVGVAGLIS 152
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEV-EVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 153 PWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGS 232
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 233 QPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATR 312
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 313 KWKVGIPSDPLA-SMGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDklnlparSQAGYFMLPTVITDIKDESCCMTEE 391
Cdd:PRK10090 240 AVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAV-------EGKGYYYPPTLLLDVRQEMSIMHEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 392 IFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNcwliRElNLP-----FGGMKSSGIG 466
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN----RE-NFEamqgfHAGWRKSGIG 387
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
7-481 |
1.46e-100 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 310.30 E-value: 1.46e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 7 LLMLENFIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSL 84
Cdd:PRK11241 8 LFRQQALINGEWLDANNgeVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 85 EEFAQAESKDQGKTLALARTmDIPRSVQNFRFFASS---ILHHTSECTQMDHlgcMHYTVRAPVGVAGLISPWNLPLYLL 161
Cdd:PRK11241 88 DDLARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEgkrIYGDTIPGHQADK---RLIVIKQPIGVTAAITPWNFPAAMI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 162 TWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQ 241
Cdd:PRK11241 164 TRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLME 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 242 LSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSD 321
Cdd:PRK11241 244 QCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 322 PLASMGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDKLnlparsqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVP 401
Cdd:PRK11241 324 KGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHEL-------GGNFFQPTILVDVPANAKVAKEETFGPLAPLFR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 402 FDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIK 481
Cdd:PRK11241 397 FKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
14-484 |
2.49e-99 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 308.02 E-value: 2.49e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 14 IDGKFLPCSSYIDSYDPS-TGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAES 92
Cdd:PRK03137 41 IGGERITTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 93 KDQGKTLALArTMDIPRSVQNFRFFASSILH--HTSECTQM-DHLGCMHYTvraPVGVAGLISPWNLPLYLLTWKIAPAI 169
Cdd:PRK03137 121 KEAGKPWAEA-DADTAEAIDFLEYYARQMLKlaDGKPVESRpGEHNRYFYI---PLGVGVVISPWNFPFAIMAGMTLAAI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 170 AAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA---P- 245
Cdd:PRK03137 197 VAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAkvqPg 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 246 --HCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPl 323
Cdd:PRK03137 277 qiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 324 ASMGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDKlnlparsqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFD 403
Cdd:PRK03137 356 AYMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDS--------KGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAK 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 404 SEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGlvwtNCWLIRELN------LPFGGMKSSGI-GREGAKDSYDF 476
Cdd:PRK03137 428 DFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVG----NLYFNRGCTgaivgyHPFGGFNMSGTdSKAGGPDYLLL 503
|
....*...
gi 966941000 477 FTEIKTIT 484
Cdd:PRK03137 504 FLQAKTVS 511
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-485 |
9.59e-99 |
|
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: 304.99 E-value: 9.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTMDI 107
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 108 PRSVQNFRFfassILHHTSECTQ---------MDHLGCM-HYTvraPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVA 177
Cdd:cd07098 81 LVTCEKIRW----TLKHGEKALRpesrpggllMFYKRARvEYE---PLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 178 KPSELTS-VTAW---MLCTLLDKAGVPPGVVNIVFGTgPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLE 253
Cdd:cd07098 154 KVSEQVAwSSGFflsIIRECLAACGHDPDLVQLVTCL-PETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 254 LGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKA 333
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 334 HLEKVRSYVKRALAEGAQIWCGeGVdKLNLPARSQAGYFmLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERAN 413
Cdd:cd07098 313 RFDRLEELVADAVEKGARLLAG-GK-RYPHPEYPQGHYF-PPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIAN 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966941000 414 NVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTITV 485
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVqqLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
13-484 |
2.35e-97 |
|
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: 302.94 E-value: 2.35e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSSYIDSYDPS-TGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAE 91
Cdd:TIGR01237 36 VINGERVETENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 92 SKDQGKTLALArTMDIPRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAA 171
Cdd:TIGR01237 116 VKEVGKPWNEA-DAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 172 GNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA------P 245
Cdd:TIGR01237 195 GNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvqpgqK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 246 HCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLAS 325
Cdd:TIGR01237 275 HLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 326 MGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDKlnlparsqAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSE 405
Cdd:TIGR01237 355 VGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDS--------KGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 406 EEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGlvwtNCWLIRELN------LPFGGMKSSGIG-REGAKDSYDFFT 478
Cdd:TIGR01237 427 DEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVG----NLYFNRNITgaivgyQPFGGFKMSGTDsKAGGPDYLALFM 502
|
....*.
gi 966941000 479 EIKTIT 484
Cdd:TIGR01237 503 QAKTVT 508
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
28-483 |
8.20e-96 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 296.85 E-value: 8.20e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 28 YDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTmDI 107
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG-EI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 108 PRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTA 187
Cdd:cd07102 80 RGMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 188 WMLCTLLDKAGVPPGVVNIVFGTGPrVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDAN 267
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 268 LDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRALA 347
Cdd:cd07102 239 LDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 348 EGAQIWCGEGVdklnLPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSN 427
Cdd:cd07102 319 KGARALIDGAL----FPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 966941000 428 VGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07102 395 IARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
13-466 |
2.35e-85 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 271.76 E-value: 2.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSSYIDSYDPSTGE-VYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEF---A 88
Cdd:cd07125 36 IINGEETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELialA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 89 QAESkdqGKTLALArtmdIP--RSVQNF-RFFASSILHHTSECTQMDHLGcMHYTVRA-PVGVAGLISPWNLPLYLLTWK 164
Cdd:cd07125 116 AAEA---GKTLADA----DAevREAIDFcRYYAAQARELFSDPELPGPTG-ELNGLELhGRGVFVCISPWNFPLAIFTGQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 165 IAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA 244
Cdd:cd07125 188 IAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 245 PHCK---KLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSD 321
Cdd:cd07125 268 ERDGpilPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWD 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 322 PLASMGALISKAHLEKVRSYVKRALAEGAQIWcgegvdklNLPARSQAGYFMLPTVITDikDESCCMTEEIFGPVTCVVP 401
Cdd:cd07125 348 LSTDVGPLIDKPAGKLLRAHTELMRGEAWLIA--------PAPLDDGNGYFVAPGIIEI--VGIFDLTTEVFGPILHVIR 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966941000 402 FDSE--EEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGlvwtNCWLIRE------LNLPFGGMKSSGIG 466
Cdd:cd07125 418 FKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG----NLYINRNitgaivGRQPFGGWGLSGTG 486
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
32-487 |
1.83e-78 |
|
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: 253.66 E-value: 1.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 32 TGEVYCRVPNSGKDEIEAAVKAAREAFPGWSsRSPQE-RSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArTMDIPRS 110
Cdd:cd07083 42 PSEVVGTTAKADKAEAEAALEAAWAAFKTWK-DWPQEdRARLLLKAADLLRRRRRELIATLTYEVGKNWVEA-IDDVAEA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 111 VQNFRFFASSILHHTSECTQMDHL-GCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWM 189
Cdd:cd07083 120 IDFIRYYARAALRLRYPAVEVVPYpGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 190 LCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHC------KKLSLELGGKNPAIIF 263
Cdd:cd07083 200 VFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLApgqtwfKRLYVETGGKNAIIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 264 EDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVK 343
Cdd:cd07083 280 ETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 344 RALAEG---AQIWCGEGVdklnlparsqaGYFMLPTVITDIKDESCCMTEEIFGPVTCV--VPFDSEEEVIERANNVKYG 418
Cdd:cd07083 360 HGKNEGqlvLGGKRLEGE-----------GYFVAPTVVEEVPPKARIAQEEIFGPVLSVirYKDDDFAEALEVANSTPYG 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966941000 419 LAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIREL--NLPFGGMKSSGIG-REGAKDSYDFFTEIKTITVKH 487
Cdd:cd07083 429 LTGGVYSRKREHLEEARREFHVGNLYINRKITGALvgVQPFGGFKLSGTNaKTGGPHYLRRFLEMKAVAERF 500
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
46-470 |
2.62e-78 |
|
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: 251.04 E-value: 2.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 46 EIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALART--------MDIprSVQNFRFF 117
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDI--SIKAYHER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 118 AssilhhTSECTQM-DHLGCMHYTvraPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDK 196
Cdd:cd07095 79 T------GERATPMaQGRAVLRHR---PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 197 AGVPPGVVNIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK-LSLELGGKNPAIIFEDANLDECIPAT 275
Cdd:cd07095 150 AGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKiLALEMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 276 VRSSFANQGEICLCTSRIFV-QKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRALAEGAQIWc 354
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVpDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 355 gegvdkLNLPARSQAGYFMLPTVI--TDIKDESccmTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVH 432
Cdd:cd07095 308 ------LAMERLVAGTAFLSPGIIdvTDAADVP---DEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFE 378
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 966941000 433 RVAKKLQSGLVWTNcwliRELN-----LPFGGMKSSGIGREGA 470
Cdd:cd07095 379 RFLARIRAGIVNWN----RPTTgasstAPFGGVGLSGNHRPSA 417
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
25-483 |
3.47e-78 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 251.58 E-value: 3.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALART 104
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 105 mDIPRSVQNFRFFA---SSILhhTSECTQMDHLGCMHYTVR-APVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPS 180
Cdd:PRK09406 83 -EALKCAKGFRYYAehaEALL--ADEPADAAAVGASRAYVRyQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 181 ELTSVTAWMLCTLLDKAGVPPGVvnivFGT---GPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGK 257
Cdd:PRK09406 160 SNVPQTALYLADLFRRAGFPDGC----FQTllvGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 258 NPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEK 337
Cdd:PRK09406 236 DPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 338 VRSYVKRALAEGAQIWCGEgvdklNLPARSqaGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKY 417
Cdd:PRK09406 316 VEKQVDDAVAAGATILCGG-----KRPDGP--GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTF 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966941000 418 GLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PRK09406 389 GLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
13-470 |
8.73e-76 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 246.02 E-value: 8.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSSY-IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAE 91
Cdd:PRK09457 4 WINGDWIAGQGEaFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 92 SKDQGKTLALART--------MDIprSVQNfrffassilHHTSECTQMDHLGCMHYTVR-APVGVAGLISPWNLPLYLLT 162
Cdd:PRK09457 84 ARETGKPLWEAATevtaminkIAI--SIQA---------YHERTGEKRSEMADGAAVLRhRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 163 WKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQL 242
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 243 SAPHCKK-LSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTE-FLKRFVEATRKWKVGIP- 319
Cdd:PRK09457 232 FAGQPEKiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWd 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 320 SDPLASMGALISKAHLEKVRSYVKRALAEGAQIwcgegvdkLNLPARSQAGY-FMLPTVI--TDIKDESccmTEEIFGPV 396
Cdd:PRK09457 312 AEPQPFMGAVISEQAAQGLVAAQAQLLALGGKS--------LLEMTQLQAGTgLLTPGIIdvTGVAELP---DEEYFGPL 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966941000 397 TCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNcwliRELN-----LPFGGMKSSGIGREGA 470
Cdd:PRK09457 381 LQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWN----KPLTgassaAPFGGVGASGNHRPSA 455
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
15-487 |
7.01e-75 |
|
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: 243.27 E-value: 7.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 15 DGKFLPCSSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKD 94
Cdd:cd07130 4 DGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 95 QGKTLALARTmdiprSVQNF-----------RFFASSILHhtSEctQMDHlgcMHYTVRAPVGVAGLISPWNLPLYLLTW 163
Cdd:cd07130 84 MGKILPEGLG-----EVQEMidicdfavglsRQLYGLTIP--SE--RPGH---RMMEQWNPLGVVGVITAFNFPVAVWGW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 164 KIAPAIAAGNTVVAKPSELTSVTAwMLCT-----LLDKAGVPPGVVNIVFGtGPRVGEALVSHPEVPLISFTGSQPTAER 238
Cdd:cd07130 152 NAAIALVCGNVVVWKPSPTTPLTA-IAVTkivarVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 239 ITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGI 318
Cdd:cd07130 230 VGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 319 PSDPLASMGALISKAHLEKVRSYVKRALAEGAQIWCGegvdklnlPARSQ-AGYFMLPTVITDIKDEScCMTEEIFGPVT 397
Cdd:cd07130 310 PLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFG--------GKVIDgPGNYVEPTIVEGLSDAP-IVKEETFAPIL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 398 CVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQS--GLVwtNCwlirelNLP---------FGGMKSSGIG 466
Cdd:cd07130 381 YVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIV--NV------NIGtsgaeiggaFGGEKETGGG 452
|
490 500
....*....|....*....|.
gi 966941000 467 REGAKDSYDFFTEIKTITVKH 487
Cdd:cd07130 453 RESGSDAWKQYMRRSTCTINY 473
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
50-483 |
1.09e-72 |
|
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: 236.27 E-value: 1.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 50 AVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTMDI-------------------PRS 110
Cdd:cd07087 3 LVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIavvlgeidhalkhlkkwmkPRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 111 VQNFR--FFASSilhhtsectqmdhlgcmhYTVRAPVGVAGLISPWNLPLYLLtwkIAP---AIAAGNTVVAKPSELTSV 185
Cdd:cd07087 83 VSVPLllQPAKA------------------YVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 186 TAWMLCTLLDKAgVPPGVVNIVFGtGPRVGEALVSHPeVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFED 265
Cdd:cd07087 142 TSALLAKLIPKY-FDPEAVAVVEG-GVEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 266 ANLDEcipaTVRS----SFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWkvgIPSDPLAS--MGALISKAHLEKVR 339
Cdd:cd07087 219 ANLEV----AARRiawgKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEF---YGEDPKESpdYGRIINERHFDRLA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 340 SyvkraLAEGAQIWCGEGVDKLNLparsqagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGL 419
Cdd:cd07087 292 S-----LLDDGKVVIGGQVDKEER--------YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPL 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966941000 420 AATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07087 359 ALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIpnLPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
25-469 |
2.30e-70 |
|
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: 231.15 E-value: 2.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 25 IDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSP-QERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALAR 103
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWLPaHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 104 tMDIPRSVQNFRFFASSILHHTSECTQMDHL----GCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKP 179
Cdd:cd07148 81 -VEVTRAIDGVELAADELGQLGGREIPMGLTpasaGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 180 SELTSVTAWMLCTLLDKAGVPPGVVNIVFgTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHcKKLSLELGGKNP 259
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 260 AIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVR 339
Cdd:cd07148 238 VIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 340 SYVKRALAEGAQIWCGEgvdklnlpARSQAGYFMlPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGL 419
Cdd:cd07148 318 EWVNEAVAAGARLLCGG--------KRLSDTTYA-PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAF 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 966941000 420 AATVWSSNVGRVHRVAKKLQSGLVWTN-------CWlirelnLPFGGMKSSGIGREG 469
Cdd:cd07148 389 QAAVFTKDLDVALKAVRRLDATAVMVNdhtafrvDW------MPFAGRRQSGYGTGG 439
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
12-484 |
1.05e-64 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 220.00 E-value: 1.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 12 NFIDGKFLPC--SSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQ 89
Cdd:PLN02419 116 NLIGGSFVESqsSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 90 AESKDQGKTLALARTmDIPRSVQNFRFFASSILHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAI 169
Cdd:PLN02419 196 NITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 170 AAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVgEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK 249
Cdd:PLN02419 275 TCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 250 LSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSR-IFVQKSIYTEflKRFVEATRKWKVGIPSDPLASMGA 328
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDAKSWE--DKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 329 LISKAHLEKVRSYVKRALAEGAQIWCgEGVDkLNLPArSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLL-DGRD-IVVPG-YEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 409 IERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLirELNLP---FGGMKSSGIGREG--AKDSYDFFTEIKTI 483
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI--PVPLPffsFTGNKASFAGDLNfyGKAGVDFFTQIKLV 586
|
.
gi 966941000 484 T 484
Cdd:PLN02419 587 T 587
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
45-483 |
5.92e-63 |
|
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: 210.92 E-value: 5.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 45 DEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTMDIpRSVQNfrffasSILHH 124
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEV-SGVKN------DILHM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 125 TS--------ECTQMDHLGCMHYTVR---APVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTL 193
Cdd:cd07135 78 LKnlkkwakdEKVKDGPLAFMFGKPRirkEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 194 LDKAgVPPGVVNIVFGTGPRVGEALVSHPEvpLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIP 273
Cdd:cd07135 158 VPKY-LDPDAFQVVQGGVPETTALLEQKFD--KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 274 ATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWkvgIPSDPLAS--MGALISKAHLEKVRSYVKRAlaeGAQ 351
Cdd:cd07135 235 RILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEF---YPGGANASpdYTRIVNPRHFNRLKSLLDTT---KGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 352 IWCGEGVDKLNLparsqagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRV 431
Cdd:cd07135 309 VVIGGEMDEATR--------FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEI 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 966941000 432 HRVAKKLQSG-LVWTNCWL---IRelNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07135 381 DHILTRTRSGgVVINDTLIhvgVD--NAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
27-483 |
1.68e-62 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 210.49 E-value: 1.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 27 SYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTmD 106
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-E 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 107 IPRSVQNFRFFAS---SILhhTSECTQMDH-LGCMHYTvraPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSEL 182
Cdd:PRK13968 90 VAKSANLCDWYAEhgpAML--KAEPTLVENqQAVIEYR---PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 183 TSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEAlVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAII 262
Cdd:PRK13968 165 VMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQM-INDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 263 FEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYV 342
Cdd:PRK13968 244 LNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 343 KRALAEGAQIWCGEgvDKLnlparSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAAT 422
Cdd:PRK13968 324 EATLAEGARLLLGG--EKI-----AGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSAT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966941000 423 VWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
45-487 |
2.39e-61 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 208.34 E-value: 2.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 45 DEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTMDIPRSVQNFRFFASSILHH 124
Cdd:PTZ00381 7 EIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 125 TSE--CTQMDHLG---CmhYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAgV 199
Cdd:PTZ00381 87 LKPekVDTVGVFGpgkS--YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-L 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 200 PPGVVNIVFGtGPRVGEALVSHPeVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSS 279
Cdd:PTZ00381 164 DPSYVRVIEG-GVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 280 FANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWkvgIPSDPLAS--MGALISKAHLEKVRSYVKRalaEGAQIWCGEG 357
Cdd:PTZ00381 242 FLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEF---FGEDPKKSedYSRIVNEFHTKRLAELIKD---HGGKVVYGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 358 VDKLNLparsqagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKK 437
Cdd:PTZ00381 316 VDIENK--------YVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLEN 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 966941000 438 LQSGLVWTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTITVKH 487
Cdd:PTZ00381 388 TSSGAVVINDCVFHLLNpnLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKS 439
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
28-466 |
1.48e-60 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 214.80 E-value: 1.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 28 YDPST--GEVYcrvpNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEF---AQAESkdqGKTL--A 100
Cdd:COG4230 578 ADHSDvvGTVV----EATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELmalLVREA---GKTLpdA 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 101 LArtmDIPRSVqNF-RFFASSILHHtsectqmdhlgCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKP 179
Cdd:COG4230 651 IA---EVREAV-DFcRYYAAQARRL-----------FAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKP 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 180 SELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERIT-QLSAPHCKKLSL--ELGG 256
Cdd:COG4230 716 AEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINrTLAARDGPIVPLiaETGG 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 257 KNpAIIFEDANLDE-CIPATVRSSFANQGEIClctS--RI-FVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISK 332
Cdd:COG4230 796 QN-AMIVDSSALPEqVVDDVLASAFDSAGQRC---SalRVlCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDA 871
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 333 AHLEKVRSYVKRALAEGAQIWcgegvdKLNLPARSQAGYFMLPTV--ITDIKDesccMTEEIFGPVTCVVPFDSEE--EV 408
Cdd:COG4230 872 EARANLEAHIERMRAEGRLVH------QLPLPEECANGTFVAPTLieIDSISD----LEREVFGPVLHVVRYKADEldKV 941
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966941000 409 IERANNVKYGLAATVWSSNVGRVHRVAKKLQSGlvwtNCWLIRelNL--------PFGGMKSSGIG 466
Cdd:COG4230 942 IDAINATGYGLTLGVHSRIDETIDRVAARARVG----NVYVNR--NIigavvgvqPFGGEGLSGTG 1001
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
144-467 |
2.70e-59 |
|
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: 201.30 E-value: 2.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 144 PVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAgVPPGVVNIVFGtGPRVGEALVSHPe 223
Cdd:cd07134 100 PKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-DAEVAQALLELP- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 224 VPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEF 303
Cdd:cd07134 177 FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAF 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 304 LKRFVEATRKW----KVGIPSDPLASMgalISKAHLEKVRSYVKRALAEGAQIWCGEGVDKlnlparsqAGYFMLPTVIT 379
Cdd:cd07134 257 VEHLKAEIEKFygkdAARKASPDLARI---VNDRHFDRLKGLLDDAVAKGAKVEFGGQFDA--------AQRYIAPTVLT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 380 DIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIREL--NLPF 457
Cdd:cd07134 326 NVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLnpNLPF 405
|
330
....*....|
gi 966941000 458 GGMKSSGIGR 467
Cdd:cd07134 406 GGVNNSGIGS 415
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
38-466 |
5.02e-59 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 210.06 E-value: 5.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 38 RVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTL--ALArtmDIPRSVQNFR 115
Cdd:PRK11904 578 EVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLqdAIA---EVREAVDFCR 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 116 FFASSILHHTSECTQM-DHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLL 194
Cdd:PRK11904 655 YYAAQARRLFGAPEKLpGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLL 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 195 DKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQ-LSAPHCKKLSL--ELGGKNPAIIFEDANLDEC 271
Cdd:PRK11904 735 HEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRtLAARDGPIVPLiaETGGQNAMIVDSTALPEQV 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 272 IPATVRSSFANQGEIClctS--RI-FVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRALAE 348
Cdd:PRK11904 815 VDDVVTSAFRSAGQRC---SalRVlFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE 891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 349 GAQIWcgegvdKLNLPARSQAGYFMLPTV--ITDIKDesccMTEEIFGPVTCVVPFDSEE--EVIERANNVKYGLAATVW 424
Cdd:PRK11904 892 ARLLA------QLPLPAGTENGHFVAPTAfeIDSISQ----LEREVFGPILHVIRYKASDldKVIDAINATGYGLTLGIH 961
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 966941000 425 SSNVGRVHRVAKKLQSGlvwtNCWLIRelNL--------PFGGMKSSGIG 466
Cdd:PRK11904 962 SRIEETADRIADRVRVG----NVYVNR--NQigavvgvqPFGGQGLSGTG 1005
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
45-466 |
7.03e-58 |
|
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: 199.37 E-value: 7.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 45 DEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArTMDIPRSVQNFRFFASSILHH 124
Cdd:TIGR01238 74 AHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNA-IAEVREAVDFCRYYAKQVRDV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 125 TSEctqmdhlgcmhYTVRaPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVV 204
Cdd:TIGR01238 153 LGE-----------FSVE-SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 205 NIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQ-----LSAPhcKKLSLELGGKNPAIIFEDANLDECIPATVRSS 279
Cdd:TIGR01238 221 QLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQtlaqrEDAP--VPLIAETGGQNAMIVDSTALPEQVVRDVLRSA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 280 FANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRALAEGAQIWCGegvd 359
Cdd:TIGR01238 299 FDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQL---- 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 360 KLNLPARSQAGYFMLPTVIT-DIKDEsccMTEEIFGPVTCVVPFDSEE--EVIERANNVKYGLAATVWSSNVGRVHRVAK 436
Cdd:TIGR01238 375 TLDDSRACQHGTFVAPTLFElDDIAE---LSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIETTYRWIEK 451
|
410 420 430
....*....|....*....|....*....|....*.
gi 966941000 437 KLQSGlvwtNCWLIREL------NLPFGGMKSSGIG 466
Cdd:TIGR01238 452 HARVG----NCYVNRNQvgavvgVQPFGGQGLSGTG 483
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
32-466 |
9.83e-58 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 206.64 E-value: 9.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 32 TGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArtMDIPRSV 111
Cdd:PRK11905 577 HDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANA--IAEVREA 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 112 QNF-RFFASSILHHTSEctqmdhlgcmhyTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWML 190
Cdd:PRK11905 655 VDFlRYYAAQARRLLNG------------PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARA 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 191 CTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK---LSLELGGKNpAIIFEDAN 267
Cdd:PRK11905 723 VRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpvpLIAETGGQN-AMIVDSSA 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 268 LDECIPATV-RSSFANQGEIClctS--RI-FVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVK 343
Cdd:PRK11905 802 LPEQVVADViASAFDSAGQRC---SalRVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIE 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 344 RALAEGAQIWcgegvdKLNLPARSQAGYFMLPTVI--TDIKDesccMTEEIFGPVTCVVPFDSEE--EVIERANNVKYGL 419
Cdd:PRK11905 879 AMRAAGRLVH------QLPLPAETEKGTFVAPTLIeiDSISD----LEREVFGPVLHVVRFKADEldRVIDDINATGYGL 948
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 966941000 420 AATVWSSNVGRVHRVAKKLQSGLVWTNcwliRelNL--------PFGGMKSSGIG 466
Cdd:PRK11905 949 TFGLHSRIDETIAHVTSRIRAGNIYVN----R--NIigavvgvqPFGGEGLSGTG 997
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
129-483 |
7.36e-57 |
|
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: 195.03 E-value: 7.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 129 TQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLtwkIAP---AIAAGNTVVAKPSELTSVTAWMLCTLLDKAgVPPGVVN 205
Cdd:cd07136 85 TPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 206 IVFGtGPRVGEALVSHPeVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGE 285
Cdd:cd07136 161 VVEG-GVEENQELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 286 ICLCTSRIFVQKSIYTEFLKRFVEATRKWkvgIPSDPLAS--MGALISKAHLEKVRSYVkralaEGAQIWCGEGVDKLNL 363
Cdd:cd07136 239 TCVAPDYVLVHESVKEKFIKELKEEIKKF---YGEDPLESpdYGRIINEKHFDRLAGLL-----DNGKIVFGGNTDRETL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 364 parsqagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLV 443
Cdd:cd07136 311 --------YIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGG 382
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 966941000 444 WTNCWLIRELN--LPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07136 383 CINDTIMHLANpyLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
13-482 |
1.43e-56 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 195.75 E-value: 1.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSS--YIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQA 90
Cdd:PLN00412 19 YADGEWRTSSSgkSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 91 ESKDQGKTLALARTmDIPRSVQNFRFFASS---------ILHHTS----ECTQMdhlgCMhyTVRAPVGVAGLISPWNLP 157
Cdd:PLN00412 99 LVKEIAKPAKDAVT-EVVRSGDLISYTAEEgvrilgegkFLVSDSfpgnERNKY----CL--TSKIPLGVVLAIPPFNYP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 158 LYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQpTAE 237
Cdd:PLN00412 172 VNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TGI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 238 RItqlsaphCKK-----LSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATR 312
Cdd:PLN00412 251 AI-------SKKagmvpLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 313 KWKVGIPSDPlASMGALISKAHLEKVRSYVKRALAEGA---QIWCGEGvdklNLparsqagyfMLPTVITDIKDESCCMT 389
Cdd:PLN00412 324 KLTVGPPEDD-CDITPVVSESSANFIEGLVMDAKEKGAtfcQEWKREG----NL---------IWPLLLDNVRPDMRIAW 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 390 EEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELN-LPFGGMKSSGIGRE 468
Cdd:PLN00412 390 EEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQ 469
|
490
....*....|....
gi 966941000 469 GAKDSYDFFTEIKT 482
Cdd:PLN00412 470 GITNSINMMTKVKS 483
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
33-425 |
1.57e-56 |
|
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: 196.27 E-value: 1.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 33 GEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSL-EEFAQAESKDQGKTLALARTMDIPRSV 111
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLGQGKNVWQAEIDAACELI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 112 QNFRF---FASSILHHTSECTQMDHLGCMHYtvRAPVGVAGLISPWN-------LPLylltwkiAPAIAaGNTVVAKPSE 181
Cdd:cd07123 137 DFLRFnvkYAEELYAQQPLSSPAGVWNRLEY--RPLEGFVYAVSPFNftaiggnLAG-------APALM-GNVVLWKPSD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 182 LTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA---------PhckKLSL 252
Cdd:cd07123 207 TAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGenldryrtyP---RIVG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 253 ELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISK 332
Cdd:cd07123 284 ETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 333 AHLEKVRSYVKRALAE-GAQIWCGEGVDKlnlparsQAGYFMLPTVI--TDIKDESccMTEEIFGPVTCV-VPFDSE-EE 407
Cdd:cd07123 364 KAFDRIKGYIDHAKSDpEAEIIAGGKCDD-------SVGYFVEPTVIetTDPKHKL--MTEEIFGPVLTVyVYPDSDfEE 434
|
410
....*....|....*....
gi 966941000 408 VIERANNV-KYGLAATVWS 425
Cdd:cd07123 435 TLELVDTTsPYALTGAIFA 453
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
52-483 |
4.59e-55 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 190.00 E-value: 4.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 52 KAA--REAFPGWssrspQERSRVLNQVADLLEQSLEEFAQAESKDQGKtlalartmdipRSVQNFRF--FASSI--LHHT 125
Cdd:cd07133 8 KAAflANPPPSL-----EERRDRLDRLKALLLDNQDALAEAISADFGH-----------RSRHETLLaeILPSIagIKHA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 126 sectqMDHL-----------GCMHYTVRA-----PVGVAGLISPWNLPLYLLtwkIAP---AIAAGNTVVAKPSELTSVT 186
Cdd:cd07133 72 -----RKHLkkwmkpsrrhvGLLFLPAKAeveyqPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 187 AWMLCTLLDKAGvPPGVVNIVFGtGPRVGEALVSHPEVPLIsFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDA 266
Cdd:cd07133 144 SALLAELLAEYF-DEDEVAVVTG-GADVAAAFSSLPFDHLL-FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 267 NLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPlaSMGALISKAHLEKVRSYVKRAL 346
Cdd:cd07133 221 DLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNP--DYTSIINERHYARLQGLLEDAR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 347 AEGAQIW-CGEGvdklnlPARSQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWS 425
Cdd:cd07133 299 AKGARVIeLNPA------GEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFG 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 426 SNVGRVHRVAKKLQSGLVWTNCWLIREL--NLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07133 373 EDKAEQDRVLRRTHSGGVTINDTLLHVAqdDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
41-464 |
1.64e-52 |
|
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: 185.76 E-value: 1.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 41 NSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSL-EEFAQAESKDQGKTLALARTMDIPRSVQNFRF--- 116
Cdd:TIGR01236 65 NATEEDAMKAVEAALDAKKDWSNLPFYDRAAIFLKAADLLSGPYrYEILAATMLGQSKTVYQAEIDAVAELIDFFRFnvk 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 117 FASSILHHTSECTQmdhlGCMHYTVRAPV-GVAGLISPWNLPLYLLTWKIAPAIAaGNTVVAKPSELTSVTAWMLCTLLD 195
Cdd:TIGR01236 145 YARELYAQQPISAP----GEWNRTEYRPLeGFVYAISPFNFTAIAGNLAGAPALM-GNTVVWKPSQTAALSNYLLMRILE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 196 KAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKK------LSLELGGKNPAIIFEDANLD 269
Cdd:TIGR01236 220 EAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRyhnfprIVGETGGKDFHLVHPSADIS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 270 ECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRA--LA 347
Cdd:TIGR01236 300 HAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAkkDP 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 348 EGAQIWCGEGVDKlnlparSQaGYFMLPTVI--TDIKDESccMTEEIFGPVTCVVPFDSE--EEVIERANNV-KYGLAAT 422
Cdd:TIGR01236 380 EALTILYGGKYDD------SQ-GYFVEPTVVesKDPDHPL--MSEEIFGPVLTVYVYPDDkyKEILDLVDSTsQYGLTGA 450
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 966941000 423 VWSSNVGRVHRVAKKLQ--SGLVWTN--CWLIRELNLPFGGMKSSG 464
Cdd:TIGR01236 451 VFAKDRKAILEADKKLRfaAGNFYINdkCTGAVVGQQPFGGARMSG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
48-486 |
7.46e-48 |
|
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: 170.87 E-value: 7.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 48 EAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKT--------LALARTmDIPRSVQNFRFFAS 119
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPkfeavlseILLVKN-EIKYAISNLPEWMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 120 SILHHTSECTQMDHLgcmhYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTL----LD 195
Cdd:cd07132 80 PEPVKKNLATLLDDV----YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELipkyLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 196 KAGVPpgvvniVFGTGPRVGEALVSHpEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDecipAT 275
Cdd:cd07132 156 KECYP------VVLGGVEETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDID----VA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 276 VR----SSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWkvgIPSDPLAS--MGALISKAHLEKVrsyvkRALAEG 349
Cdd:cd07132 225 ARriawGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEF---YGEDPKESpdYGRIINDRHFQRL-----KKLLSG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 350 AQIWCGEGVDKLNLparsqagyFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVG 429
Cdd:cd07132 297 GKVAIGGQTDEKER--------YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKK 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 966941000 430 RVHRVAKKLQSGLVWTNCWLIREL--NLPFGGMKSSGIGREGAKDSYDFFTEIKTITVK 486
Cdd:cd07132 369 VINKILSNTSSGGVCVNDTIMHYTldSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
45-466 |
4.34e-45 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 169.38 E-value: 4.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 45 DEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArTMDIPRSVQNFRFFASSILHH 124
Cdd:PRK11809 682 AEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNA-IAEVREAVDFLRYYAGQVRDD 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 125 TSECTQMdhlgcmhytvraPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVV 204
Cdd:PRK11809 761 FDNDTHR------------PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVV 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 205 NIVFGTGPRVGEALVSHPEVPLISFTGSQPTAeRITQLS-------APHCKKLSLELGGKNpAIIFEDANLDECIPATV- 276
Cdd:PRK11809 829 QLLPGRGETVGAALVADARVRGVMFTGSTEVA-RLLQRNlagrldpQGRPIPLIAETGGQN-AMIVDSSALTEQVVADVl 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 277 RSSFANQGEIC-----LCtsrifVQKSIYTEFLKRFVEATRKWKVGIPsDPLAS-MGALISK-------AHLEKVRSY-- 341
Cdd:PRK11809 907 ASAFDSAGQRCsalrvLC-----LQDDVADRTLKMLRGAMAECRMGNP-DRLSTdIGPVIDAeakanieRHIQAMRAKgr 980
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 342 -VKRALAEGAQIWcgegvdklnlparsQAGYFMLPTVIT-DIKDEsccMTEEIFGPVTCVVPFDSEE--EVIERANNVKY 417
Cdd:PRK11809 981 pVFQAARENSEDW--------------QSGTFVPPTLIElDSFDE---LKREVFGPVLHVVRYNRNQldELIEQINASGY 1043
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 966941000 418 GLAATVWSSNVGRVHRVAKKLQSGlvwtNCWLIRelNL--------PFGGMKSSGIG 466
Cdd:PRK11809 1044 GLTLGVHTRIDETIAQVTGSAHVG----NLYVNR--NMvgavvgvqPFGGEGLSGTG 1094
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
13-487 |
1.12e-41 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 155.38 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 13 FIDGKFLPCSSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAES 92
Cdd:PLN02315 24 YVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 93 KDQGKTLA-----LARTMDI-PRSVQNFRFFASSILhhTSEctQMDHlgcMHYTVRAPVGVAGLISPWNLPLYLLTWKIA 166
Cdd:PLN02315 104 LEMGKILAegigeVQEIIDMcDFAVGLSRQLNGSII--PSE--RPNH---MMMEVWNPLGIVGVITAFNFPCAVLGWNAC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 167 PAIAAGNTVVAKPSELTSV----TAWMLCTLLDKAGVPPGVVNIVFGtGPRVGEALVSHPEVPLISFTGSQPTAERITQL 242
Cdd:PLN02315 177 IALVCGNCVVWKGAPTTPLitiaMTKLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 243 SAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDP 322
Cdd:PLN02315 256 VNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 323 LASMGALISKAHLEKVRSYVKRALAEGAQIWCGEGvdklnlpARSQAGYFMLPTVItDIKDESCCMTEEIFGPVTCVVPF 402
Cdd:PLN02315 336 GTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGS-------AIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKF 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 403 DSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSglvwtNCWLIrELNLP---------FGGMKSSGIGREGAKDS 473
Cdd:PLN02315 408 KTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGS-----DCGIV-NVNIPtngaeiggaFGGEKATGGGREAGSDS 481
|
490
....*....|....
gi 966941000 474 YDFFTEIKTITVKH 487
Cdd:PLN02315 482 WKQYMRRSTCTINY 495
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
144-483 |
7.20e-38 |
|
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: 143.71 E-value: 7.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 144 PVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAgVPPGVVNIVFGtGPRVGEALVSHpE 223
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQ-K 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 224 VPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSF-ANQGEICLCTSRIFVQKSIYTE 302
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAPT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 303 FLKRFVEATRKWkvgIPSDPLAS--MGALISKAHLEKVRSYVKRALAEgAQIWCGEGVDKLNLparsqagyFMLPTVITD 380
Cdd:cd07137 258 LIDALKNTLEKF---FGENPKESkdLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGGERDEKNL--------YIEPTILLD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 381 IKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELN--LPFG 458
Cdd:cd07137 326 PPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIdtLPFG 405
|
330 340
....*....|....*....|....*
gi 966941000 459 GMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:cd07137 406 GVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
48-448 |
7.22e-35 |
|
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: 135.44 E-value: 7.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 48 EAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALArtMDIPRSVQNFRFFASSILHHTSE 127
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA--ENICGDQVQLRARAFVIYSYRIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 128 CTQMDHLGC-----MHYtVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAG-VPP 201
Cdd:cd07084 80 HEPGNHLGQglkqqSHG-YRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 202 GVVNIVFGTGpRVGEALVSHPEVPLISFTGSQPTAERItqLSAPHCKKLSLELGGKNPAIIFEDAN-----LDECipatV 276
Cdd:cd07084 159 EDVTLINGDG-KTMQALLLHPNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQavdyvAWQC----V 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 277 RSSFANQGEICLCTSRIFVQKSIYTEflkRFVEATrKWKVGIPSDPLASMGALIS---KAHLEKVRSYVKRALAEGAQIW 353
Cdd:cd07084 232 QDMTACSGQKCTAQSMLFVPENWSKT---PLVEKL-KALLARRKLEDLLLGPVQTfttLAMIAHMENLLGSVLLFSGKEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 354 cgEGVDKLNLPARSQAGYFMLPTVITDIKDESccMTEEIFGPVTCVVPF--DSEEEVIERANNVKYGLAATVWSSNVGRV 431
Cdd:cd07084 308 --KNHSIPSIYGACVASALFVPIDEILKTYEL--VTEEIFGPFAIVVEYkkDQLALVLELLERMHGSLTAAIYSNDPIFL 383
|
410
....*....|....*...
gi 966941000 432 HRVAKKLQS-GLVWTNCW 448
Cdd:cd07084 384 QELIGNLWVaGRTYAILR 401
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
47-426 |
6.18e-34 |
|
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: 133.05 E-value: 6.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 47 IEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLE---QSLEEFAQAESkdqgkTLALAR-TMDIPRSVQNFRFFASSIL 122
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEalgDELVARAHAET-----GLPEARlQGELGRTTGQLRLFADLVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 123 HHTSECTQMDH-------LGCMHYT-VRAPVGVAGLISPWNLPLYLLTW--KIAPAIAAGNTVVAKP-------SELTSV 185
Cdd:cd07129 76 EGSWLDARIDPadpdrqpLPRPDLRrMLVPLGPVAVFGASNFPLAFSVAggDTASALAAGCPVVVKAhpahpgtSELVAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 186 TAwmlCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSA--PHCKKLSLELGGKNPAIIF 263
Cdd:cd07129 156 AI---RAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAarPEPIPFYAELGSVNPVFIL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 264 EDAnLDECiPATVRSSFA-----NQGEICLCTSRIFVQKSiytEFLKRFVEATRKWKVGIPSDPLASMGalISKAHLEKV 338
Cdd:cd07129 233 PGA-LAER-GEAIAQGFVgsltlGAGQFCTNPGLVLVPAG---PAGDAFIAALAEALAAAPAQTMLTPG--IAEAYRQGV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 339 rsyvkRALAEGAqiwcgeGVDKLNLPARSQAGYFMLPTVI-TD----IKDESccMTEEIFGPVTCVVPFDSEEEVIERAN 413
Cdd:cd07129 306 -----EALAAAP------GVRVLAGGAAAEGGNQAAPTLFkVDaaafLADPA--LQEEVFGPASLVVRYDDAAELLAVAE 372
|
410
....*....|...
gi 966941000 414 NVKYGLAATVWSS 426
Cdd:cd07129 373 ALEGQLTATIHGE 385
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
144-484 |
7.74e-34 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 133.31 E-value: 7.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 144 PVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAgVPPGVVNIVFGtGPRVGEALVSHPe 223
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLLQHK- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 224 VPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVR------SSFAnqGEICLCTSRIFVQK 297
Cdd:PLN02203 185 WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSLSSSRDTKVAVNRivggkwGSCA--GQACIAIDYVLVEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 298 SiYTEFLKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRALAEgAQIWCGEGVDKLNLparsqagyFMLPTV 377
Cdd:PLN02203 263 R-FAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSIDEKKL--------FIEPTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 378 ITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIREL--NL 455
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdSL 412
|
330 340
....*....|....*....|....*....
gi 966941000 456 PFGGMKSSGIGREGAKDSYDFFTEIKTIT 484
Cdd:PLN02203 413 PFGGVGESGFGRYHGKYSFDTFSHEKAVL 441
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
10-432 |
5.67e-28 |
|
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: 116.60 E-value: 5.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 10 LENFIDGKFL-PCSSYIDSYDPSTGEVYCRVPNSGKDeIEAAVKAARE-AFPGWSSRSPQERSRVLNQVADLLEQSLEEF 87
Cdd:cd07128 1 LQSYVAGQWHaGTGDGRTLHDAVTGEVVARVSSEGLD-FAAAVAYAREkGGPALRALTFHERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 88 aQAESKDQGKTLALARtMDIPRSVQNFRFFAS--------SILHHTSECTQMDHLGCM---H-YTVRApvGVAGLISPWN 155
Cdd:cd07128 80 -YALSAATGATRRDSW-IDIDGGIGTLFAYASlgrrelpnAHFLVEGDVEPLSKDGTFvgqHiLTPRR--GVAVHINAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 156 LPLYLLTWKIAPAIAAGNTVVAKPSELTS-VTAWMLCTLLDKAGVPPGVVNIVFGTgprVGEALVSHPEVPLISFTGSQP 234
Cdd:cd07128 156 FPVWGMLEKFAPALLAGVPVIVKPATATAyLTEAVVKDIVESGLLPEGALQLICGS---VGDLLDHLGEQDVVAFTGSAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 235 TAER------ITQLSAPhckkLSLELGGKNPAIIFEDAN-----LDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEF 303
Cdd:cd07128 233 TAAKlrahpnIVARSIR----FNAEADSLNAAILGPDATpgtpeFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 304 LKRFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRaLAEGAQIWCGEGVDKLNLPARSQAGYFMLPTVIT--DI 381
Cdd:cd07128 309 IEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDRFEVVGADAEKGAFFPPTLLLcdDP 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966941000 382 KDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSN--------------VGRVH 432
Cdd:cd07128 388 DAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDpafarelvlgaapyHGRLL 452
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
141-483 |
6.29e-28 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 116.30 E-value: 6.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 141 VRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAgVPPGVVNIVFGTGPRVGEALvs 220
Cdd:PLN02174 109 VSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALL-- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 221 HPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDecipATVRSSFA-----NQGEICLCTSRIFV 295
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLK----VTVRRIIAgkwgcNNGQACISPDYILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 296 QKsiytEFLKRFVEATRK-WKVGIPSDPLAS--MGALISKAHLEKVRSYVKRALAEGAQIWCGEGvDKLNLParsqagyf 372
Cdd:PLN02174 262 TK----EYAPKVIDAMKKeLETFYGKNPMESkdMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEK-DRENLK-------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 373 MLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRE 452
Cdd:PLN02174 329 IAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHL 408
|
330 340 350
....*....|....*....|....*....|...
gi 966941000 453 L--NLPFGGMKSSGIGREGAKDSYDFFTEIKTI 483
Cdd:PLN02174 409 AlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
10-439 |
2.35e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 114.80 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 10 LENFIDGKFLPCS-SYIDSYDPSTGEVYCRVPNSGKDeIEAAVKAARE-AFPGWSSRSPQERSRVLNQVADLLEQSLEEF 87
Cdd:PRK11903 5 LANYVAGRWQAGSgAGTPLFDPVTGEELVRVSATGLD-LAAAFAFAREqGGAALRALTYAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 88 AQAESKDQGKTLALArTMDIPRSVQNFRFFAS-----SILHHTSECTqMDHLG------CMHYTVRAPvGVAGLISPWNL 156
Cdd:PRK11903 84 YDIATANSGTTRNDS-AVDIDGGIFTLGYYAKlgaalGDARLLRDGE-AVQLGkdpafqGQHVLVPTR-GVALFINAFNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 157 PLYLLTWKIAPAIAAGNTVVAKPSeltSVTAW----MLCTLLDKAGVPPGVVNIVFGTGPRVGEALvshPEVPLISFTGS 232
Cdd:PRK11903 161 PAWGLWEKAAPALLAGVPVIVKPA---TATAWltqrMVKDVVAAGILPAGALSVVCGSSAGLLDHL---QPFDVVSFTGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 233 QPTAERITQLSA--PHCKKLSLELGGKNPAIIFEDAN-----LDECIPATVRSSFANQGEICLCTSRIFVQKSIYTEFLK 305
Cdd:PRK11903 235 AETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 306 RFVEATRKWKVGIPSDPLASMGALISKAHLEKVRSYVKRaLAEGAQIWCGEGVDKLnLPARSQAGYFMLPT--VITDIKD 383
Cdd:PRK11903 315 ALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGFAL-VDADPAVAACVGPTllGASDPDA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 384 ESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNV--------------GRVHRVAKKLQ 439
Cdd:PRK11903 393 ATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAaflaaaaleladshGRVHVISPDVA 462
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
12-434 |
7.13e-21 |
|
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: 95.25 E-value: 7.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 12 NFIDGKFLPCSSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAReAFPGWSSRSP---QER----SRVLNQVADLLEQ-S 83
Cdd:cd07126 1 NLVAGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLR-QCPKSGLHNPlknPERyllyGDVSHRVAHELRKpE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 84 LEEF-------AQAESKDQgktlALARTMDIPRSVQNF-----RFFASSIlhhtseCTQMDHLGCMHYTVRAPVGVAGLI 151
Cdd:cd07126 80 VEDFfarliqrVAPKSDAQ----ALGEVVVTRKFLENFagdqvRFLARSF------NVPGDHQGQQSSGYRWPYGPVAII 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 152 SPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKAGVPPGVVNIVFGTGPRVGEaLVSHPEVPLISFTG 231
Cdd:cd07126 150 TPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNK-ILLEANPRMTLFTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 232 SQPTAERitqlsaphckkLSLELGGKnpaIIFEDANLDECI--PATV----------RSSFANQGEICLCTSRIFVQKS- 298
Cdd:cd07126 229 SSKVAER-----------LALELHGK---VKLEDAGFDWKIlgPDVSdvdyvawqcdQDAYACSGQKCSAQSILFAHENw 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 299 IYTEFLKRFVEATRKWKVgipSDplASMGALISKAHlEKVRSYVKRALA-EGAQI-WCGEGVDKLNLPARSQAgyfMLPT 376
Cdd:cd07126 295 VQAGILDKLKALAEQRKL---ED--LTIGPVLTWTT-ERILDHVDKLLAiPGAKVlFGGKPLTNHSIPSIYGA---YEPT 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966941000 377 VI------TDIKDESCCMTEEIFGPVTCVVPFDSEEE--VIERANNVKYGLAATVWSSNVGRVHRV 434
Cdd:cd07126 366 AVfvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEV 431
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
53-323 |
2.99e-15 |
|
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: 77.26 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 53 AAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLA-----LARTMDIPRSVQNFRFFAS----SILH 123
Cdd:cd07077 2 SAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRslianWIAMMGCSESKLYKNIDTErgitASVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 124 HTSECTQMDHLGCmhYTVRAPVGVAGLISPWNLPLYLLTwKIAPAIAAGNTVVAKPSELTSVTAWMLcTLLDKAGVPPGV 203
Cdd:cd07077 82 HIQDVLLPDNGET--YVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRAL-ALLFQAADAAHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 204 VNIVFGTGP----RVGEALVSHPEVPLISFTGSqPTAERITQLSAPHckKLSLELGGKNPAIIFEDANLDECIPATVRSS 279
Cdd:cd07077 158 PKILVLYVPhpsdELAEELLSHPKIDLIVATGG-RDAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 966941000 280 FANQGEICLCTSRIFVQKSIYTEFLKRFVEATRKWKVGIPSDPL 323
Cdd:cd07077 235 KFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETK 278
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
46-412 |
1.64e-13 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 72.51 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 46 EIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQA--ESKDQGKTLAL----ARTMDIPRSVQNFRFFAS 119
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAvmHTTGQAFMMAFqaggPHAQDRGLEAVAYAWREM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 120 SILHHTSECTQ---------MDHlgcmHYTVrAPVGVAGLISPWNLPlyllTWKIAPA----IAAGNTVVAKPSELT--- 183
Cdd:cd07127 165 SRIPPTAEWEKpqgkhdplaMEK----TFTV-VPRGVALVIGCSTFP----TWNGYPGlfasLATGNPVIVKPHPAAilp 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 184 -SVTAWMLCTLLDKAGVPPGVVNIV-FGTGPRVGEALVSHPEVPLISFTGSQPTAERITQlsapHCKKLSL--ELGGKNP 259
Cdd:cd07127 236 lAITVQVAREVLAEAGFDPNLVTLAaDTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEA----NARQAQVytEKAGVNT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 260 AIIFEDANLDECIPATVRSSFANQGEICLCTSRIFV----------QKSiYTEFLKRFVEATRKWkVGIPSDPLASMGAL 329
Cdd:cd07127 312 VVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtddgRKS-FDEVAADLAAAIDGL-LADPARAAALLGAI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 330 ISKAHLEKvrsyVKRALAEGAQIWCGEGVDKLNLP-ARSQAgyfmlPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEV 408
Cdd:cd07127 390 QSPDTLAR----IAEARQLGEVLLASEAVAHPEFPdARVRT-----PLLLKLDASDEAAYAEERFGPIAFVVATDSTDHS 460
|
....
gi 966941000 409 IERA 412
Cdd:cd07127 461 IELA 464
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
45-439 |
7.47e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 57.60 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 45 DEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQG----------KTLALARTMDIprsvqnf 114
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedkiakNVAAAEKTPGV------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 115 rffassilhhtsECTQMDHL---GCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVV------AKpseltSV 185
Cdd:PRK15398 109 ------------EDLTTEALtgdNGLTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVfsphpgAK-----KV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 186 TAW---MLCTLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAEriTQLSAPhcKKLSLELGGKNPAII 262
Cdd:PRK15398 172 SLRaieLLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVK--AAMKSG--KKAIGAGAGNPPVVV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 263 FEDANLDECIPATVRS-SFANQgEICLCTSRIFVQKSIYTEFLKRFVEAtrkwkvgipsdplasmGA-LISKAHLEKV-- 338
Cdd:PRK15398 248 DETADIEKAARDIVKGaSFDNN-LPCIAEKEVIVVDSVADELMRLMEKN----------------GAvLLTAEQAEKLqk 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 339 ----------RSYVKR---ALAEGAQIWCGEGVDklnlparsqagyfmLPTVITDiKDESCCMTEEIFgPVTCVVPFDSE 405
Cdd:PRK15398 311 vvlknggtvnKKWVGKdaaKILEAAGINVPKDTR--------------LLIVETD-ANHPFVVTELMM-PVLPVVRVKDV 374
|
410 420 430
....*....|....*....|....*....|....*.
gi 966941000 406 EEVIERANNVKYGL--AATVWSSNVGRVHRVAKKLQ 439
Cdd:PRK15398 375 DEAIALAVKLEHGNrhTAIMHSRNVDNLNKMARAIQ 410
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
47-309 |
1.05e-07 |
|
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: 54.19 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 47 IEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGktlaLARTMDipRSVQNFrfFASSILHHtS 126
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETG----MGRVED--KVIKNH--FAAEYIYN-V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 127 ECtqmDHLGC---------MHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKP----SELTSVTAWMLCTL 193
Cdd:cd07081 72 YK---DEKTCgvltgdengGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 194 LDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGsqptAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIP 273
Cdd:cd07081 149 AVAAGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQ 224
|
250 260 270
....*....|....*....|....*....|....*.
gi 966941000 274 ATVRSSFANQGEICLCTSRIFVQKSIYTEFLKRFVE 309
Cdd:cd07081 225 SIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEG 260
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
45-439 |
8.85e-07 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 51.08 E-value: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 45 DEIEAAVKAAREAFPGWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQG------KTLALARTMDIPRSVQNFRFFA 118
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGmgrvedKIAKNHLAAEKTPGTEDLTTTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 119 SSilhhtsectqMDHlGcMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAIAAGNTVVAKPSELTSVTAWMLCTLLDKA- 197
Cdd:cd07121 84 WS----------GDN-G-LTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAi 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 198 ---GVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQlsapHCKKLSLELGGKNPAIIFEDANLDECIPA 274
Cdd:cd07121 152 aeaGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALS----SGKKAIGAGAGNPPVVVDETADIEKAARD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 275 TVRS-SFANQgEICLCTSRIFVQKSIYTEFLKRFV----------EATRKWKVGIPSDPlasmGALISKAHLEKVRSYvk 343
Cdd:cd07121 228 IVQGaSFDNN-LPCIAEKEVIAVDSVADYLIAAMQrngayvlndeQAEQLLEVVLLTNK----GATPNKKWVGKDASK-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 344 raLAEGAQIWCGEGVdklnlparsqagyfmlPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGL--AA 421
Cdd:cd07121 301 --ILKAAGIEVPADI----------------RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTA 362
|
410
....*....|....*...
gi 966941000 422 TVWSSNVGRVHRVAKKLQ 439
Cdd:cd07121 363 IIHSKNVENLTKMARAMQ 380
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
144-309 |
1.19e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, 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: 143440 [Multi-domain] Cd Length: 436 Bit Score: 47.49 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 144 PVGV-AGLI---SPWNLPLYlltwKIAPAIAAGNTVVAKPSELTSVTAWMLCTLL----DKAGVPPGVVNIVFGTGPRVG 215
Cdd:cd07122 95 PVGViAALIpstNPTSTAIF----KALIALKTRNAIIFSPHPRAKKCSIEAAKIMreaaVAAGAPEGLIQWIEEPSIELT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966941000 216 EALVSHPEVPLISFTGSQPTAEritqlSAPHCKKLSLELG-GKNPAIIFEDANLDECIPATVRS-SFANqGEICLCTSRI 293
Cdd:cd07122 171 QELMKHPDVDLILATGGPGMVK-----AAYSSGKPAIGVGpGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQSV 244
|
170
....*....|....*.
gi 966941000 294 FVQKSIYTEFLKRFVE 309
Cdd:cd07122 245 IVDDEIYDEVRAELKR 260
|
|
| |
