|
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: 828.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 27 SYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARTVD 106
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 107 IPRAVYNFRFFASSILHHTTECTEMASmGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVT 186
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDG-GALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 187 AWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDA 266
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 267 DLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKKAK 346
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 347 AEGAKILCGEGVDSLALPAGnqkGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSS 426
Cdd:cd07093 320 AEGATILTGGGRPELPDLEG---GYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393110 427 NVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-487 |
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: 636.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 1 MAHSEallvLENFIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLAD 78
Cdd:COG1012 1 MTTPE----YPLFIGGEWVAAASgeTFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 79 LIEHDLEAFAQAESKDQGKTITFARtVDIPRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPL 158
Cdd:COG1012 77 LLEERREELAALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 159 YLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQR 238
Cdd:COG1012 156 ALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 239 ITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGN 318
Cdd:COG1012 236 IAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 319 PSDPTVDVGALISKEHLEKVRSYVKKAKAEGAKILCGeGVdslalPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTC 398
Cdd:COG1012 316 PLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTG-GR-----RPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 399 VVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCW-LVRDLNLPFGGMKASGIGREGAKDSYEFF 477
Cdd:COG1012 390 VIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGtTGAVPQAPFGGVKQSGIGREGGREGLEEY 469
|
490
....*....|
gi 2024393110 478 TEVKTITIKH 487
Cdd:COG1012 470 TETKTVTIRL 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: 606.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 20 PCSSYIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTI 99
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 100 TFARTvDIPRAVYNFRFFASSILHHTTECTEMaSMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKP 179
Cdd:pfam00171 84 AEARG-EVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 180 SEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNP 259
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 260 AIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVR 339
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 340 SYVKKAKAEGAKILCGeGvdslalPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGL 419
Cdd:pfam00171 322 KYVEDAKEEGAKLLTG-G------EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024393110 420 AATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDL-NLPFGGMKASGIGREGAKDSYEFFTEVKTI 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: 549.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 10 LENFIAGRFVPCSSYIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFP-IWSSKSPLEKSQILNKLADLIEHDLEAFA 88
Cdd:TIGR03216 1 IRNFINGAFVESGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAALKgPWGKMTVAERADLLYAVADEIERRFDDFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 89 QAESKDQGKTITFARTVDIPRAVYNFRFFASSILHHTTECTEMAS---MGCVHYTSRTPVGVAGLISPWNLPLYLLTWKI 165
Cdd:TIGR03216 81 AAEVADTGKPRSLASHLDIPRGAANFRVFADVVKNAPTECFEMATpdgKGALNYAVRKPLGVVGVISPWNLPLLLMTWKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 166 APAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTG-AKAGEALVCHPDVPLISFTGSTLTAQRITEKSA 244
Cdd:TIGR03216 161 GPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGpDSAGEFLTRHPGVDAITFTGETRTGSAIMKAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 245 PHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTV 324
Cdd:TIGR03216 241 DGVKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDPAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 325 DVGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDSlaLPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDT 404
Cdd:TIGR03216 321 NMGPLISAEHRDKVLSYYALAVEEGATVVTGGGVPD--FGDALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFDS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 405 EEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTIT 484
Cdd:TIGR03216 399 EEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNVC 478
|
..
gi 2024393110 485 IK 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: 536.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 48 EAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARTvDIPRAVYNFRFFASSILHHTTE 127
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 128 CTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMV 207
Cdd:cd07078 80 VIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 208 FGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEIC 287
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 288 LCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDslalpaGN 367
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRL------EG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 368 QKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNC 447
Cdd:cd07078 314 GKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIND 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 2024393110 448 WLV-RDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 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: 526.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSK--SPLEKSQILNKLADLIEHDLEAFA 88
Cdd:cd07091 7 FINNEFVDSVSgkTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRkmDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 89 QAESKDQGKTITFARTVDIPRAVYNFRFFA--SSILHHTTecteMASMGCVH-YTSRTPVGVAGLISPWNLPLYLLTWKI 165
Cdd:cd07091 87 ALESLDNGKPLEESAKGDVALSIKCLRYYAgwADKIQGKT----IPIDGNFLaYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 166 APAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA- 244
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 245 PHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTV 324
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 325 DVGALISKEHLEKVRSYVKKAKAEGAKILCGEGvdslalPAGNqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDT 404
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGE------RHGS-KGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 405 EEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTIT 484
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
|
.
gi 2024393110 485 I 485
Cdd:cd07091 476 I 476
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
27-485 |
8.70e-180 |
|
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: 511.71 E-value: 8.70e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 27 SYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAF--PIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFART 104
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 105 vDIPRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTS 184
Cdd:cd07114 81 -QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 185 VTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFD 264
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 265 DADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKK 344
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 345 AKAEGAKILCGEGVDSLalpAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVW 424
Cdd:cd07114 320 AREEGARVLTGGERPSG---ADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIW 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024393110 425 SSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07114 397 TRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
10-487 |
1.64e-177 |
|
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: 507.04 E-value: 1.64e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 10 LENFIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAF 87
Cdd:TIGR02299 1 IGHFIDGEFVPSESgeTFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKRWAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 88 AQAESKDQGKTITFARTVdIPRAVYNFRFFASSILH----HTTECTEMasmgcVHYTSRTPVGVAGLISPWNLPLYLLTW 163
Cdd:TIGR02299 81 AVLECLDCGQPLRQTRQQ-VIRAAENFRFFADKCEEamdgRTYPVDTH-----LNYTVRVPVGPVGLITPWNAPFMLSTW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 164 KIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKS 243
Cdd:TIGR02299 155 KIAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 244 APHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPT 323
Cdd:TIGR02299 235 ADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 324 VDVGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDSLALPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFD 403
Cdd:TIGR02299 315 TEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPTFRGEDLGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 404 TEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:TIGR02299 395 DEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNV 474
|
....
gi 2024393110 484 TIKH 487
Cdd:TIGR02299 475 ALAL 478
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
28-485 |
4.27e-172 |
|
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: 491.95 E-value: 4.27e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 28 YNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARtVDI 107
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 108 PRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTA 187
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 188 WMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDAD 267
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 268 LSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKKAKA 347
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 348 EGAKILCGEGVDSLalpagnqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSN 427
Cdd:cd07103 321 KGAKVLTGGKRLGL-------GGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393110 428 VGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07103 394 LARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
13-485 |
2.58e-171 |
|
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: 491.06 E-value: 2.58e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAF--PIWSSKSPLEKSQILNKLADLIEHDLEAFA 88
Cdd:cd07119 1 YIDGEWVEAASgkTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 89 QAESKDQGKTITFARTvDIPRAVYNFRFFASSIlhhTTECTEMASMG--CVHYTSRTPVGVAGLISPWNLPLYLLTWKIA 166
Cdd:cd07119 81 RLETLNTGKTLRESEI-DIDDVANCFRYYAGLA---TKETGEVYDVPphVISRTVREPVGVCGLITPWNYPLLQAAWKLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 167 PAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPH 246
Cdd:cd07119 157 PALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 247 CKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDV 326
Cdd:cd07119 237 VKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 327 GALISKEHLEKVRSYVKKAKAEGAKILCGEgvdslALPAGN--QKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDT 404
Cdd:cd07119 317 GPLVSAEHREKVLSYIQLGKEEGARLVCGG-----KRPTGDelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 405 EEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTIT 484
Cdd:cd07119 392 EEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHIN 471
|
.
gi 2024393110 485 I 485
Cdd:cd07119 472 I 472
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
26-485 |
7.95e-168 |
|
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: 481.33 E-value: 7.95e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 26 DSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFP--IWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFAR 103
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 104 TVDIPRAVYNFRFFASSI--LHHTTECTEMASMGCVhytSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSE 181
Cdd:cd07112 85 AVDVPSAANTFRWYAEAIdkVYGEVAPTGPDALALI---TREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 182 MTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA-PHCKKLSLELGGKNPA 260
Cdd:cd07112 162 QSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNLKRVWLECGGKSPN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 261 IIFDDA-DLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVR 339
Cdd:cd07112 242 IVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 340 SYVKKAKAEGAKILCGEGVDSLAlpagnQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGL 419
Cdd:cd07112 322 GYIESGKAEGARLVAGGKRVLTE-----TGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393110 420 AATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07112 397 AASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
11-485 |
9.72e-168 |
|
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: 481.84 E-value: 9.72e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 11 ENFIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFA 88
Cdd:cd07559 2 DNFINGEWVAPSKgeYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 89 QAESKDQGKTITFARTVDIPRAVYNFRFFASSILHHTTECTEMASmGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDE-DTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 169 IACGNTVVAKPSEMTSVTAWMMCKLLEKAgMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCK 248
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 249 KLSLELGGKNPAIIFDDA-DLSQCIPTTLRSSFA----NQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPT 323
Cdd:cd07559 240 PVTLELGGKSPNIFFDDAmDADDDFDDKAEEGQLgfafNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 324 VDVGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDSLalpAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFD 403
Cdd:cd07559 320 TMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTL---GGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 404 TEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
..
gi 2024393110 484 TI 485
Cdd:cd07559 477 LV 478
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-484 |
1.02e-167 |
|
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: 481.23 E-value: 1.02e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 12 NFIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQ 89
Cdd:cd07138 1 FYIDGAWVAPAGteTIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 90 AESKDQGKTITFARTVDIPRAVYNFRFFASSIlhHTTECTEMASMGCVhytSRTPVGVAGLISPWNLPLYLLTWKIAPAI 169
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADAL--KDFEFEERRGNSLV---VREPIGVCGLITPWNWPLNQIVLKVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 170 ACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKK 249
Cdd:cd07138 156 AAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 250 LSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGAL 329
Cdd:cd07138 236 VALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 330 ISKEHLEKVRSYVKKAKAEGAKILCGeGVDslaLPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVV 409
Cdd:cd07138 316 ASAAQFDRVQGYIQKGIEEGARLVAG-GPG---RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAI 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024393110 410 KRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNcWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTIT 484
Cdd:cd07138 392 AIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
29-483 |
9.47e-166 |
|
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: 475.78 E-value: 9.47e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 29 NPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARTVDIP 108
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 109 RAVYNFRFFASSilhhtteCTEMA------SMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEM 182
Cdd:cd07115 83 RAADTFRYYAGW-------ADKIEgevipvRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 183 TSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAII 262
Cdd:cd07115 156 TPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 263 FDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYV 342
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 343 KKAKAEGAKILCGEGVDSlalpagnQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAAT 422
Cdd:cd07115 316 DVGREEGARLLTGGKRPG-------ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024393110 423 VWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:cd07115 389 VWTRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
28-483 |
1.03e-164 |
|
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: 473.33 E-value: 1.03e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 28 YNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARtVDI 107
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 108 PRAVYNFRFFASSILHHTTECTEMASmGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTA 187
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPG-GSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 188 WMMCKLLEKAGMPHGVVNMVFGtGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDAD 267
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 268 LSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKKAKA 347
Cdd:cd07090 239 LENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 348 EGAKILCGEgvDSLALPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSN 427
Cdd:cd07090 319 EGAKVLCGG--ERVVPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393110 428 VGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
28-485 |
1.70e-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: 459.87 E-value: 1.70e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 28 YNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARTVDI 107
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 108 PRAVYNFRFFASSILH-HTTECTEMASmGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVT 186
Cdd:cd07092 82 PGAVDNFRFFAGAARTlEGPAAGEYLP-GHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 187 AWMMCKLLEKaGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDA 266
Cdd:cd07092 161 TLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 267 DLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKKAK 346
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 347 AeGAKILCGEGvdslalpAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSS 426
Cdd:cd07092 320 A-HARVLTGGR-------RAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393110 427 NVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
11-487 |
4.38e-159 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 459.76 E-value: 4.38e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 11 ENFIAGRFVPCS-SYIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQ 89
Cdd:PRK13473 4 KLLINGELVAGEgEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 90 AESKDQGKTITFARTVDIPRAVYNFRFFASSilhhtTECTEMASMG--CVHYTS---RTPVGVAGLISPWNLPLYLLTWK 164
Cdd:PRK13473 84 LESLNCGKPLHLALNDEIPAIVDVFRFFAGA-----ARCLEGKAAGeyLEGHTSmirRDPVGVVASIAPWNYPLMMAAWK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 165 IAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAgMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA 244
Cdd:PRK13473 159 LAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 245 PHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTV 324
Cdd:PRK13473 238 DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 325 DVGALISKEHLEKVRSYVKKAKAEG-AKILCGEGVdslalPAGnqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFD 403
Cdd:PRK13473 318 ELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEA-----PDG--KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 404 TEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:PRK13473 391 DEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
....
gi 2024393110 484 TIKH 487
Cdd:PRK13473 471 MVKH 474
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
11-483 |
1.24e-156 |
|
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: 453.24 E-value: 1.24e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 11 ENFIAGRFVPCSSYIDSYNPS-TGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQ 89
Cdd:cd07097 2 RNYIDGEWVAGGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 90 AESKDQGKTITFARTvDIPRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAI 169
Cdd:cd07097 82 LLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 170 ACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKK 249
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 250 LSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGAL 329
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 330 ISKEHLEKVRSYVKKAKAEGAKILCGEGvdslALPaGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVV 409
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGAKLVYGGE----RLK-RPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEAL 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393110 410 KRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVR-DLNLPFGGMKASGIG-REGAKDSYEFFTEVKTI 483
Cdd:cd07097 396 AIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGvDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
13-485 |
1.29e-156 |
|
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: 453.79 E-value: 1.29e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCS--SYIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSK-SPLEKSQILNKLADLIEHDLEAFAQ 89
Cdd:cd07144 11 FINNEFVKSSdgETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 90 AESKDQGKTITFARTVDIPRAVYNFRFFASSI--LHHTTECTEMASMGcvhYTSRTPVGVAGLISPWNLPLYLLTWKIAP 167
Cdd:cd07144 91 IEALDSGKPYHSNALGDLDEIIAVIRYYAGWAdkIQGKTIPTSPNKLA---YTLHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 168 AIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHC 247
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 248 KKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKK-WKVGNPSDPTVDV 326
Cdd:cd07144 248 KAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 327 GALISKEHLEKVRSYVKKAKAEGAKILCGEgvdsLALPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEE 406
Cdd:cd07144 328 GPQVSKTQYDRVLSYIEKGKKEGAKLVYGG----EKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYE 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393110 407 EVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07144 404 EAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
30-485 |
1.48e-154 |
|
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: 447.17 E-value: 1.48e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 30 PSTGDVYCRVPDSGKEEVEAAVRAAKNAFPI--WSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARTvDI 107
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 108 PRAVYNFRFFAS--SILH---HTTECTEMASMgcvhyTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEM 182
Cdd:cd07118 83 EGAADLWRYAASlaRTLHgdsYNNLGDDMLGL-----VLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 183 TSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAII 262
Cdd:cd07118 158 TSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 263 FDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYV 342
Cdd:cd07118 238 FADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 343 KKAKAEGAKILCGEGVDSLAlpagnqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAAT 422
Cdd:cd07118 318 DAGRAEGATLLLGGERLASA------AGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024393110 423 VWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07118 392 VWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
13-486 |
1.45e-153 |
|
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: 445.64 E-value: 1.45e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPI---WSSKSPLEKSQILNKLADLIEHDLEAF 87
Cdd:cd07141 10 FINNEWHDSVSgkTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 88 AQAESKDQGKTITFARTVDIPRAVYNFRFFA--SSILHHTTecteMASMGCVH-YTSRTPVGVAGLISPWNLPLYLLTWK 164
Cdd:cd07141 90 ASLETLDNGKPFSKSYLVDLPGAIKVLRYYAgwADKIHGKT----IPMDGDFFtYTRHEPVGVCGQIIPWNFPLLMAAWK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 165 IAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA 244
Cdd:cd07141 166 LAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 245 -PHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPT 323
Cdd:cd07141 246 kSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 324 VDVGALISKEHLEKVRSYVKKAKAEGAKILCGEGvdslalPAGNqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFD 403
Cdd:cd07141 326 TEQGPQIDEEQFKKILELIESGKKEGAKLECGGK------RHGD-KGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 404 TEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:cd07141 399 TIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
...
gi 2024393110 484 TIK 486
Cdd:cd07141 479 TIK 481
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
28-485 |
8.51e-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: 440.04 E-value: 8.51e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 28 YNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARTvDI 107
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-EV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 108 PRAVYNFRFFAS-----SILHHTTECTEmasmgcvhYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEM 182
Cdd:cd07106 81 GGAVAWLRYTASldlpdEVIEDDDTRRV--------ELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 183 TSVTAWMMCKLLEKAgMPHGVVNMVFGtGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAII 262
Cdd:cd07106 153 TPLCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 263 FDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYV 342
Cdd:cd07106 231 LPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 343 KKAKAEGAKILCGEGVDslalpagNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAAT 422
Cdd:cd07106 311 EDAKAKGAKVLAGGEPL-------DGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGAS 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024393110 423 VWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07106 384 VWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
13-485 |
9.91e-151 |
|
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: 438.43 E-value: 9.91e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQA 90
Cdd:cd07117 4 FINGEWVKGSSgeTIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 91 ESKDQGKTITFARTVDIPRAVYNFRFFASSILHHTTECTEM--ASMGCVhytSRTPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07117 84 ETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIdeDTLSIV---LREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 169 IACGNTVVAKPSEMTSVTAWMMCKLLEKAgMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCK 248
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 249 KLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGA 328
Cdd:cd07117 240 PATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 329 LISKEHLEKVRSYVKKAKAEGAKILCGeGVDSLAlpAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEV 408
Cdd:cd07117 320 QVNKDQLDKILSYVDIAKEEGAKILTG-GHRLTE--NGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393110 409 VKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
13-483 |
1.44e-150 |
|
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: 438.08 E-value: 1.44e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPI--WSSKSPLEKSQILNKLADLIEHDLEAFA 88
Cdd:cd07142 7 FINGQFVDAASgkTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 89 QAESKDQGKTITFARTVDIPRAVYNFRFFA--SSILHHTTecteMASMGCVH-YTSRTPVGVAGLISPWNLPLYLLTWKI 165
Cdd:cd07142 87 ALETWDNGKPYEQARYAEVPLAARLFRYYAgwADKIHGMT----LPADGPHHvYTLHEPIGVVGQIIPWNFPLLMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 166 APAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA- 244
Cdd:cd07142 163 GPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 245 PHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTV 324
Cdd:cd07142 243 SNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 325 DVGALISKEHLEKVRSYVKKAKAEGAKILCGegvdslalpaGNQ---KGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVA 401
Cdd:cd07142 323 EQGPQVDKEQFEKILSYIEHGKEEGATLITG----------GDRigsKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 402 FDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVK 481
Cdd:cd07142 393 FKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
..
gi 2024393110 482 TI 483
Cdd:cd07142 473 AV 474
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
12-483 |
1.58e-150 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 438.16 E-value: 1.58e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 12 NFIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQ 89
Cdd:PRK13252 9 LYIDGAYVEATSgeTFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 90 AESKDQGKTITFARTVDIPRAVYNFRFFASSILHHTTECTEMASmGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAI 169
Cdd:PRK13252 89 LETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRG-GSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 170 ACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAkAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKK 249
Cdd:PRK13252 168 AAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 250 LSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGAL 329
Cdd:PRK13252 247 VTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 330 ISKEHLEKVRSYVKKAKAEGAKILC-GEGVDslalPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEV 408
Cdd:PRK13252 327 VSFAHRDKVLGYIEKGKAEGARLLCgGERLT----EGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEV 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024393110 409 VKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:PRK13252 403 IARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
13-485 |
3.16e-150 |
|
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: 437.01 E-value: 3.16e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAF--PIWSSKSPLEKSQILNKLADLIEHDLEAFA 88
Cdd:cd07139 2 FIGGRWVAPSGseTIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 89 QAESKDQGKTITFARTVDIPRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 169 IACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGtGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCK 248
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 249 KLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGA 328
Cdd:cd07139 241 RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 329 LISKEHLEKVRSYVKKAKAEGAKILCGEGVdslalPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEV 408
Cdd:cd07139 321 LASARQRERVEGYIAKGRAEGARLVTGGGR-----PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393110 409 VKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNcWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
13-486 |
5.81e-150 |
|
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: 436.57 E-value: 5.81e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPC--SSYIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPI-WSSK-SPLEKSQILNKLADLIEHDLEAFA 88
Cdd:cd07143 10 FINGEFVDSvhGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGLKvSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 89 QAESKDQGKTITFARTVDIPRAVYNFRFF---ASSILHHTTECTEMAsmgcVHYTSRTPVGVAGLISPWNLPLYLLTWKI 165
Cdd:cd07143 90 SIEALDNGKTFGTAKRVDVQASADTFRYYggwADKIHGQVIETDIKK----LTYTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 166 APAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA- 244
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 245 PHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTV 324
Cdd:cd07143 246 SNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 325 DVGALISKEHLEKVRSYVKKAKAEGAKILCGegvdslALPAGNqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDT 404
Cdd:cd07143 326 FQGPQVSQIQYERIMSYIESGKAEGATVETG------GKRHGN-EGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 405 EEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTIT 484
Cdd:cd07143 399 EEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVH 478
|
..
gi 2024393110 485 IK 486
Cdd:cd07143 479 IN 480
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
13-481 |
7.39e-149 |
|
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: 433.47 E-value: 7.39e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQA 90
Cdd:TIGR01804 1 FIDGEYVEDSAgtTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 91 ESKDQGKTITFARTVDIPRAVYNFRFFASSILHHTTECTEMASMGCVhYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:TIGR01804 81 ETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFA-YTIREPLGVCVGIGAWNYPLQIASWKIAPALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 171 CGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKL 250
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 251 SLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALI 330
Cdd:TIGR01804 240 TMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 331 SKEHLEKVRSYVKKAKAEGAKILCGEGVDSLalpAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVK 410
Cdd:TIGR01804 320 SAAHRDKVLSYIEKGKAEGATLATGGGRPEN---VGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024393110 411 RANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVK 481
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
27-485 |
3.01e-148 |
|
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: 431.27 E-value: 3.01e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 27 SYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSK-SPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARTv 105
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 106 DIPRAVYNFRFFASSI--LHHTTecteMASM-GCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEM 182
Cdd:cd07109 80 DVEAAARYFEYYGGAAdkLHGET----IPLGpGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 183 TSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAII 262
Cdd:cd07109 156 APLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 263 FDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDpTVDVGALISKEHLEKVRSYV 342
Cdd:cd07109 236 FADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 343 KKAKAEGAKILCGEGVDSLALPagnqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAAT 422
Cdd:cd07109 315 ARARARGARIVAGGRIAEGAPA----GGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAG 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024393110 423 VWSSNVGRVHRVARRLQSGLVWTNCW-LVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07109 391 VWTRDGDRALRVARRLRAGQVFVNNYgAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-487 |
3.02e-148 |
|
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: 432.16 E-value: 3.02e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 12 NFIAGRFVPCSS--YIDSYNPSTG-DVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFA 88
Cdd:cd07131 1 NYIGGEWVDSASgeTFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 89 QAESKDQGKTITFARTvDIPRAVYNFRFFASS--ILHHTTECTEMASMGCvhYTSRTPVGVAGLISPWNLPLYLLTWKIA 166
Cdd:cd07131 81 RLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEgrRLFGETVPSELPNKDA--MTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 167 PAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPH 246
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 247 CKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDV 326
Cdd:cd07131 238 NKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 327 GALISKEHLEKVRSYVKKAKAEGAKILCGegvDSLALPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEE 406
Cdd:cd07131 318 GPLINEAQLEKVLNYNEIGKEEGATLLLG---GERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 407 EVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLV-RDLNLPFGGMKASGIG-REGAKDSYEFFTEVKTIT 484
Cdd:cd07131 395 EAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVY 474
|
...
gi 2024393110 485 IKH 487
Cdd:cd07131 475 VDY 477
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
46-485 |
5.01e-147 |
|
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: 427.33 E-value: 5.01e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 46 EVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTItfartvdiPRAVYNFRFFASSILHHT 125
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTR--------PKAAFEVGAAIAILREAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 126 TECTEM-------ASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMM-CKLLEKA 197
Cdd:cd07104 73 GLPRRPegeilpsDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLiAEIFEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 198 GMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLR 277
Cdd:cd07104 153 GLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 278 SSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKKAKAEGAKILCGEG 357
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 358 VDslalpagnqkGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARR 437
Cdd:cd07104 313 YE----------GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAER 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2024393110 438 LQSGLVWTNCWLVRDL-NLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07104 383 LETGMVHINDQTVNDEpHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
13-483 |
4.89e-146 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 427.31 E-value: 4.89e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFP--IWSSKSPLEKSQILNKLADLIEHDLEAFA 88
Cdd:PLN02766 24 FINGEFVDAASgkTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 89 QAESKDQGKTITFARTVDIPRAVYNFRFFASSILHHTTECTEMASMgCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQ-LQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 169 IACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA-PHC 247
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAtSNL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 248 KKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVG 327
Cdd:PLN02766 263 KQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 328 ALISKEHLEKVRSYVKKAKAEGAKILCGegvdslALPAGNqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEE 407
Cdd:PLN02766 343 PQVDKQQFEKILSYIEHGKREGATLLTG------GKPCGD-KGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393110 408 VVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
13-485 |
7.16e-145 |
|
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: 423.21 E-value: 7.16e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQA 90
Cdd:cd07088 1 YINGEFVPSSSgeTIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 91 ESKDQGKTITFARtVDIPRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:cd07088 81 IVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 171 CGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKL 250
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 251 SLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALI 330
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 331 SKEHLEKVRSYVKKAKAEGAKILCGEGvdslalPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVK 410
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGATLLTGGK------RPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024393110 411 RANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
29-484 |
4.30e-144 |
|
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: 420.60 E-value: 4.30e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 29 NPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFArTVDIP 108
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 109 RAVYNFRFFAS---SILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSV 185
Cdd:cd07110 82 DVAGCFEYYADlaeQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 186 TAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDD 265
Cdd:cd07110 162 TELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 266 ADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKKA 345
Cdd:cd07110 242 ADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 346 KAEGAKILCGEGVdslalPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWS 425
Cdd:cd07110 322 KEEGARLLCGGRR-----PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393110 426 SNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTIT 484
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
28-483 |
1.36e-143 |
|
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: 419.73 E-value: 1.36e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 28 YNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWS-SKSPLEKSQILNKLADLIEHDLEAFA---QAESkdqGKTITFAR 103
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRallVAEV---GAPVMTAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 104 TVDIPRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRT----PVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKP 179
Cdd:cd07089 79 AMQVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRRVvrrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 180 SEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNP 259
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 260 AIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVR 339
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 340 SYVKKAKAEGAKILCGEGVdslalPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGL 419
Cdd:cd07089 319 GYIARGRDEGARLVTGGGR-----PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024393110 420 AATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:cd07089 394 SGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
25-485 |
2.28e-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: 413.67 E-value: 2.28e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 25 IDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARt 104
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 105 VDIPRAVYNFRFFASSILHHTTECTEM----ASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPS 180
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVdayeYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 181 EMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPA 260
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 261 IIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRS 340
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 341 YVKKAKAEGAKILCGegvdslalpaGN-QKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGL 419
Cdd:cd07145 320 LVNDAVEKGGKILYG----------GKrDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393110 420 AATVWSSNVGRVHRVARRLQSGLVWTN-CWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07145 390 QASVFTNDINRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
26-485 |
6.13e-141 |
|
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: 412.49 E-value: 6.13e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 26 DSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFA--- 102
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAwfe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 103 --RTVDIPRAvynfrffASSILHHTT-ECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKP 179
Cdd:cd07150 82 ttFTPELLRA-------AAGECRRVRgETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 180 SEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNP 259
Cdd:cd07150 155 SEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 260 AIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVR 339
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 340 SYVKKAKAEGAKILCGEGVDslalpagnqkGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGL 419
Cdd:cd07150 315 RQVEDAVAKGAKLLTGGKYD----------GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393110 420 AATVWSSNVGRVHRVARRLQSGLVWTNCWLVRD-LNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07150 385 SAAILTNDLQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
29-485 |
3.24e-140 |
|
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: 410.98 E-value: 3.24e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 29 NPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTItfaRTVDIP 108
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNAL---RTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 109 RAVYN---FRFF---ASSILHHTTECTEmasmGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEM 182
Cdd:cd07108 80 EAAVLadlFRYFgglAGELKGETLPFGP----DVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 183 TSVTAWMMCKLLEKAgMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAII 262
Cdd:cd07108 156 APLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 263 FDDADLSQCIPTTLRSS-FANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSY 341
Cdd:cd07108 235 FPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 342 VKKAKAE-GAKIL-CGegvdSLALPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGL 419
Cdd:cd07108 315 IDLGLSTsGATVLrGG----PLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393110 420 AATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSY-EFFTEVKTITI 485
Cdd:cd07108 391 AAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMlEHFTQKKTVNI 457
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
27-484 |
6.57e-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: 410.20 E-value: 6.57e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 27 SYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAF--PIWSSkSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARt 104
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 105 VDIPRAVYNFRFFASSILHHTTECTEMASmGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTS 184
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIEPEP-GSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 185 VTAWMMCKLL-EKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIF 263
Cdd:cd07120 158 QINAAIIRILaEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 264 DDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVK 343
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 344 KAKAEGAKILC-GEGVDSlalpaGNQKGYFMLPTVIaEIKDESC-CMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAA 421
Cdd:cd07120 318 RAIAAGAEVVLrGGPVTE-----GLAKGAFLRPTLL-EVDDPDAdIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024393110 422 TVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTIT 484
Cdd:cd07120 392 SVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
52-485 |
1.22e-136 |
|
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: 398.53 E-value: 1.22e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 52 RAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITfARTVDIPRAVYNFRFFASSILHHTTECTEM 131
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIE-EALGEVARAIDTFRYAAGLADKLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 132 ASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTG 211
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 212 AKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTS 291
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 292 RIFVQRGIYSEFVKRFVaetkkwkvgnpsdptvdvgaliskehlekvrsyvkkakaegakilcgegvdslalpagnqkgy 371
Cdd:cd06534 240 RLLVHESIYDEFVEKLV--------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 372 fmlpTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLV- 450
Cdd:cd06534 257 ----TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIg 332
|
410 420 430
....*....|....*....|....*....|....*
gi 2024393110 451 RDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd06534 333 VGPEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-481 |
2.27e-136 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 402.53 E-value: 2.27e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 7 LLVLENFIAGRFVPC--SSYIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDL 84
Cdd:PLN02278 22 LLRTQGLIGGKWTDAydGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 85 EAFAQAESKDQGKTITFARTvDIPRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWK 164
Cdd:PLN02278 102 EDLAQLMTLEQGKPLKEAIG-EVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 165 IAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA 244
Cdd:PLN02278 181 VGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 245 PHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTV 324
Cdd:PLN02278 261 ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 325 DVGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDSLAlpagnqkGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDT 404
Cdd:PLN02278 341 TQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLG-------GTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKT 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393110 405 EEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVK 481
Cdd:PLN02278 414 EEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
25-485 |
5.55e-136 |
|
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: 400.05 E-value: 5.55e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 25 IDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARt 104
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 105 VDIPRAVYNFRFFASSILHHTTECTEMASM----GCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPS 180
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRLAGETIPFDASpggeGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 181 EMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAphCKKLSLELGGKNPA 260
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 261 IIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRS 340
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 341 YVKKAKAEGAKILCGegvdslalpaGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLA 420
Cdd:cd07149 318 WVEEAVEGGARLLTG----------GKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393110 421 ATVWSSNVGRVHRVARRLQSGLVWTNcWL--VRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07149 388 AGVFTNDLQKALKAARELEVGGVMIN-DSstFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
11-487 |
2.03e-135 |
|
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: 399.52 E-value: 2.03e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 11 ENFIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFA 88
Cdd:cd07116 2 DNFIGGEWVAPVKgeYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 89 QAESKDQGKTITFARTVDIPRAVYNFRFFASSILHHTTECTEMASmGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDE-NTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 169 IACGNTVVAKPSEMTSVTAWMMCKLLEKAgMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCK 248
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 249 KLSLELGGKNPAIIF------DDADLSQCIPTTLRSSFaNQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDP 322
Cdd:cd07116 240 PVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 323 TVDVGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDSLalpAGNQKGYFMLPTVIAEIKDEScCMQEEIFGPVTCVVAF 402
Cdd:cd07116 319 ETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNEL---GGLLGGGYYVPTTFKGGNKMR-IFQEEIFGPVLAVTTF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 403 DTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKT 482
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKN 474
|
....*
gi 2024393110 483 ITIKH 487
Cdd:cd07116 475 LLVSY 479
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
13-487 |
1.15e-134 |
|
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: 397.58 E-value: 1.15e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPI-WSSKSPLEKSQILNKLADLIEHDLEAFAQ 89
Cdd:cd07113 3 FIDGRPVAGQSekRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 90 AESKDQGKTITFARTVDIPRAVYNFRFFA--SSILHHTTECTEMASMGCVHYTS---RTPVGVAGLISPWNLPLYLLTWK 164
Cdd:cd07113 83 LETLCSGKSIHLSRAFEVGQSANFLRYFAgwATKINGETLAPSIPSMQGERYTAftrREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 165 IAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAkAGEALVCHPDVPLISFTGSTLTAQRITEKSA 244
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 245 PHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTV 324
Cdd:cd07113 242 SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 325 DVGALISKEHLEKVRSYVKKAKAEGAKILCG-EGVDslalpagnQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFD 403
Cdd:cd07113 322 MFGPLANQPHFDKVCSYLDDARAEGDEIVRGgEALA--------GEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 404 TEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:cd07113 394 DEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
....
gi 2024393110 484 TIKH 487
Cdd:cd07113 474 MIRY 477
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
13-476 |
1.67e-132 |
|
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: 392.14 E-value: 1.67e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCS--SYIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQA 90
Cdd:cd07111 25 FINGKWVKPEnrKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 91 ESKDQGKTITFARTVDIPRAVYNFRFFAssILHHTTEcTEMASmgcvhytsRTPVGVAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:cd07111 105 ESLDNGKPIRESRDCDIPLVARHFYHHA--GWAQLLD-TELAG--------WKPVGVVGQIVPWNFPLLMLAWKICPALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 171 CGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAkAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKL 250
Cdd:cd07111 174 MGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 251 SLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALI 330
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 331 SKEHLEKVRSYVKKAKAEGAKILCGEGvdslALPAgnqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVK 410
Cdd:cd07111 333 DPAQLKRIRELVEEGRAEGADVFQPGA----DLPS---KGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVA 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393110 411 RANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDS-YEF 476
Cdd:cd07111 406 LANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGlYEY 472
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
13-483 |
8.48e-129 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 384.54 E-value: 8.48e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAF---PiWSSKSPLEKSQILNKLADLIEHDLEAF 87
Cdd:PLN02466 61 LINGQFVDAASgkTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFdegP-WPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 88 AQAESKDQGKTITFARTVDIPRAVYNFRFFA--SSILHHTTecteMASMGCVH-YTSRTPVGVAGLISPWNLPLYLLTWK 164
Cdd:PLN02466 140 AALETWDNGKPYEQSAKAELPMFARLFRYYAgwADKIHGLT----VPADGPHHvQTLHEPIGVAGQIIPWNFPLLMFAWK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 165 IAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA 244
Cdd:PLN02466 216 VGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 245 -PHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPT 323
Cdd:PLN02466 296 kSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 324 VDVGALISKEHLEKVRSYVKKAKAEGAKILCGegvdslalpaGNQ---KGYFMLPTVIAEIKDESCCMQEEIFGPVTCVV 400
Cdd:PLN02466 376 VEQGPQIDSEQFEKILRYIKSGVESGATLECG----------GDRfgsKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSIL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 401 AFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEV 480
Cdd:PLN02466 446 KFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQV 525
|
...
gi 2024393110 481 KTI 483
Cdd:PLN02466 526 KAV 528
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
29-485 |
1.65e-128 |
|
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: 380.95 E-value: 1.65e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 29 NPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARTvDIP 108
Cdd:cd07107 3 NPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-DVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 109 RAVYNFRFFASSILHHTTEcTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAW 188
Cdd:cd07107 82 VAAALLDYFAGLVTELKGE-TIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 189 MMCKLLEKAgMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADL 268
Cdd:cd07107 161 RLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 269 SQCIPTTLRS-SFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKKAKA 347
Cdd:cd07107 240 EAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 348 EGAKILCGEGVDSLALPAGnqkGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSN 427
Cdd:cd07107 320 EGARLVTGGGRPEGPALEG---GFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393110 428 VGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07107 397 ISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
12-487 |
8.90e-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: 379.99 E-value: 8.90e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 12 NFIAGRFVPCSS-YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQA 90
Cdd:cd07086 1 GVIGGEWVGSGGeTFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 91 ESKDQGKTITFAR-----TVDIPravynfrFFA---SSILHHTTECTEMAsmGCVHYTSRTPVGVAGLISPWNLPLYLLT 162
Cdd:cd07086 81 VSLEMGKILPEGLgevqeMIDIC-------DYAvglSRMLYGLTIPSERP--GHRLMEQWNPLGVVGVITAFNFPVAVPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 163 WKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKA----GMPHGVVNMVFGtGAKAGEALVCHPDVPLISFTGSTLTAQR 238
Cdd:cd07086 152 WNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 239 ITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGN 318
Cdd:cd07086 231 VGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 319 PSDPTVDVGALISKEHLEKVRSYVKKAKAEGAKILCGEGVdslalPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTC 398
Cdd:cd07086 311 PLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKR-----IDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 399 VVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQS--GLVWTNcwlV----RDLNLPFGGMKASGIGREGAKD 472
Cdd:cd07086 386 VIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVN---IptsgAEIGGAFGGEKETGGGRESGSD 462
|
490
....*....|....*
gi 2024393110 473 SYEFFTEVKTITIKH 487
Cdd:cd07086 463 AWKQYMRRSTCTINY 477
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
13-487 |
1.18e-126 |
|
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: 377.22 E-value: 1.18e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPI--WSSKSPLEKSQILNKLADLIEHDLEAFA 88
Cdd:cd07140 9 FINGEFVDAEGgkTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 89 QAESKDQGKTITFARTVDIPRAVYNFRFFA---SSILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKI 165
Cdd:cd07140 89 TIESLDSGAVYTLALKTHVGMSIQTFRYFAgwcDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYPLMMLAWKM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 166 APAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA- 244
Cdd:cd07140 169 AACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAv 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 245 PHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTV 324
Cdd:cd07140 249 SNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRST 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 325 DVGALISKEHLEKVRSYVKKAKAEGAKILCGegvdslalpaGNQ---KGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVA 401
Cdd:cd07140 329 DHGPQNHKAHLDKLVEYCERGVKEGATLVYG----------GKQvdrPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 402 FDTE--EEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTE 479
Cdd:cd07140 399 FDDGdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLK 478
|
....*...
gi 2024393110 480 VKTITIKH 487
Cdd:cd07140 479 TKTVTIEY 486
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
16-487 |
1.74e-125 |
|
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: 373.56 E-value: 1.74e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 16 GRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESK 93
Cdd:cd07151 1 GEWRDGTSerTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 94 DQGKTITFArTVDIPRAVYNFRFFAS-------SILHHTTECTEmasmgcvHYTSRTPVGVAGLISPWNLPLYLLTWKIA 166
Cdd:cd07151 81 ESGSTRIKA-NIEWGAAMAITREAATfplrmegRILPSDVPGKE-------NRVYREPLGVVGVISPWNFPLHLSMRSVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 167 PAIACGNTVVAKPSEMTSVTA-WMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAP 245
Cdd:cd07151 153 PALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 246 HCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVD 325
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 326 VGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDslalpagnqkGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTE 405
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVEEGATLLVGGEAE----------GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 406 EEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDL-NLPFGGMKASGIGREGAKDSYEFFTEVKTIT 484
Cdd:cd07151 383 EEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEpHVPFGGEKNSGLGRFNGEWALEEFTTDKWIS 462
|
...
gi 2024393110 485 IKH 487
Cdd:cd07151 463 VQH 465
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
13-484 |
1.48e-124 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 372.53 E-value: 1.48e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCS--SYIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPI-----WSSKSPLEKSQILNKLADLIEHDLE 85
Cdd:PLN02467 11 FIGGEWREPVlgKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 86 AFAQAESKDQGKTITFARTvDIPRAVYNFRFFAS-----SILHHTTECTEMASMGCvhYTSRTPVGVAGLISPWNLPLYL 160
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAW-DMDDVAGCFEYYADlaealDAKQKAPVSLPMETFKG--YVLKEPLGVVGLITPWNYPLLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 161 LTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRIT 240
Cdd:PLN02467 168 ATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 241 EKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPS 320
Cdd:PLN02467 248 TAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 321 DPTVDVGALISKEHLEKVRSYVKKAKAEGAKILCGeGVDslalPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVV 400
Cdd:PLN02467 328 EEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCG-GKR----PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 401 AFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEV 480
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSV 482
|
....
gi 2024393110 481 KTIT 484
Cdd:PLN02467 483 KQVT 486
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
13-484 |
8.08e-122 |
|
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: 365.78 E-value: 8.08e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSSYIDSYNPS-TGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAE 91
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 92 SKDQGKTITFArTVDIPRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRtPVGVAGLISPWNLPLYLLTWKIAPAIAC 171
Cdd:cd07124 116 VLEVGKNWAEA-DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTTAALVT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 172 GNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA------P 245
Cdd:cd07124 194 GNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkvqpgqK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 246 HCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVD 325
Cdd:cd07124 274 WLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVY 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 326 VGALISKEHLEKVRSYVKKAKAEGaKILCGEGVdslalPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTE 405
Cdd:cd07124 354 MGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEV-----LELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 406 EEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTN-----CWLVRDlnlPFGGMKASGIG-REGAKDSYEFFTE 479
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkitgALVGRQ---PFGGFKMSGTGsKAGGPDYLLQFMQ 504
|
....*
gi 2024393110 480 VKTIT 484
Cdd:cd07124 505 PKTVT 509
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
10-484 |
9.98e-121 |
|
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: 361.83 E-value: 9.98e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 10 LENFIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAF 87
Cdd:cd07085 1 LKLFINGEWVESKTteWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 88 AQAESKDQGKTITFARTvDIPRAVYNFRFfASSILHHTT-ECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIA 166
Cdd:cd07085 81 ARLITLEHGKTLADARG-DVLRGLEVVEF-ACSIPHLLKgEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 167 PAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGtGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPH 246
Cdd:cd07085 159 MAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 247 CKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDV 326
Cdd:cd07085 238 GKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 327 GALISKEHLEKVRSYVKKAKAEGAKILC-GEGVDslalPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTE 405
Cdd:cd07085 318 GPVISPAAKERIEGLIESGVEEGAKLVLdGRGVK----VPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 406 EEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVwtncwlvrDLNLP---------FGGMKASGIGREGA--KDSY 474
Cdd:cd07085 394 DEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMV--------GINVPipvplaffsFGGWKGSFFGDLHFygKDGV 465
|
490
....*....|
gi 2024393110 475 EFFTEVKTIT 484
Cdd:cd07085 466 RFYTQTKTVT 475
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
25-485 |
2.43e-119 |
|
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: 357.51 E-value: 2.43e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 25 IDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARt 104
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 105 VDIPRAVYNFRFFASSILHHTTECTEM----ASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPS 180
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRGEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 181 EMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAphCKKLSLELGGKNPA 260
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 261 IIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRS 340
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 341 YVKKAKAEGAKILCGegvdslalpaGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLA 420
Cdd:cd07094 318 WVEEAVEAGARLLCG----------GERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393110 421 ATVWSSNVGRVHRVARRLQSGLVWTN-CWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07094 388 AGIFTRDLNVAFKAAEKLEVGGVMVNdSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
46-485 |
6.28e-119 |
|
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: 355.73 E-value: 6.28e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 46 EVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARtVDIPRAVYNFRFFASSILHHT 125
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAG-FNVDLAAGMLREAASLITQII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 126 TECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVN 205
Cdd:cd07105 80 GGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 206 MVF---GTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFAN 282
Cdd:cd07105 160 VVThspEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 283 QGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNpsdptVDVGALISKEHLEKVRSYVKKAKAEGAKILCGegvdslA 362
Cdd:cd07105 240 SGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVG------G 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 363 LPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGL 442
Cdd:cd07105 309 LADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2024393110 443 VWTNCWLVRD-LNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07105 389 VHINGMTVHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
33-485 |
1.73e-116 |
|
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: 349.67 E-value: 1.73e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 33 GDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTItfartvdiPRAVY 112
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIR--------PKAGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 113 NFRFfASSILHhttECTEMASM----------GCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEM 182
Cdd:cd07152 73 EVGA-AIGELH---EAAGLPTQpqgeilpsapGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 183 TSVTAWMM-CKLLEKAGMPHGVVNMVFGtGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAI 261
Cdd:cd07152 149 TPVSGGVViARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 262 IFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSY 341
Cdd:cd07152 228 VLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 342 VKKAKAEGAKILCGegvdslalpaGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAA 421
Cdd:cd07152 308 VDDSVAAGARLEAG----------GTYDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSA 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393110 422 TVWSSNVGRVHRVARRLQSGLVWTNCWLVRD-LNLPFGGMKASGIG-REGAKDSYEFFTEVKTITI 485
Cdd:cd07152 378 GIISRDVGRAMALADRLRTGMLHINDQTVNDePHNPFGGMGASGNGsRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
28-485 |
1.86e-115 |
|
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: 347.29 E-value: 1.86e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 28 YNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARtVDI 107
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 108 PRAVYNFRFFASS---ILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTS 184
Cdd:cd07099 80 LLALEAIDWAARNaprVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 185 VTAWMMCKLLEKAGMPHGVVNMVFGTGAkAGEALVCHPdVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFD 264
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGA-TGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 265 DADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKK 344
Cdd:cd07099 238 DADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 345 AKAEGAKILCGeGVDSlalpagNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVW 424
Cdd:cd07099 318 AVAKGAKALTG-GARS------NGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024393110 425 SSNVGRVHRVARRLQSGLVWTNCWLVRDLN--LPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07099 391 SRDLARAEAIARRLEAGAVSINDVLLTAGIpaLPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
3-485 |
8.52e-115 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 347.27 E-value: 8.52e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 3 HSEALLVLEN--FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFP--IWSSKSPLEKSQILNKL 76
Cdd:PRK09847 11 DKALSLAIENrlFINGEYTAAAEneTFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 77 ADLIEHDLEAFAQAESKDQGKTITFARTVDIPRAVYNFRFFASSI--LHHTTECTEMASMGCVhytSRTPVGVAGLISPW 154
Cdd:PRK09847 91 ADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIdkVYGEVATTSSHELAMI---VREPVGVIAAIVPW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 155 NLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTL 234
Cdd:PRK09847 168 NFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 235 TA-QRITEKSAPHCKKLSLELGGKNPAIIFDDA-DLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETK 312
Cdd:PRK09847 248 TGkQLLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 313 KWKVGNPSDPTVDVGALISKEHLEKVRSYVKKAKAEGAKILCGEgvdSLALPAgnqkgyFMLPTVIAEIKDESCCMQEEI 392
Cdd:PRK09847 328 NWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGR---NAGLAA------AIGPTIFVDVDPNASLSREEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 393 FGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKD 472
Cdd:PRK09847 399 FGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLH 478
|
490
....*....|...
gi 2024393110 473 SYEFFTEVKTITI 485
Cdd:PRK09847 479 ALEKFTELKTIWI 491
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
25-485 |
2.03e-108 |
|
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: 329.21 E-value: 2.03e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 25 IDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARt 104
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 105 VDIPRAVYNFRFFASSILHHTTECTEM----ASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPS 180
Cdd:cd07147 80 GEVARAIDTFRIAAEEATRIYGEVLPLdisaRGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 181 EMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAgEALVCHPDVPLISFTGSTLTAQRITEKsAPHcKKLSLELGGKNPA 260
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPCSRDDA-DLLVTDERIKLLSFTGSPAVGWDLKAR-AGK-KKVVLELGGNAAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 261 IIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRS 340
Cdd:cd07147 237 IVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 341 YVKKAKAEGAKILCGegvdslalpaGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLA 420
Cdd:cd07147 317 WVNEAVDAGAKLLTG----------GKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQ 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393110 421 ATVWSSNVGRVHRVARRLQSGLVWTN---CWLVrDlNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07147 387 AGVFTRDLEKALRAWDELEVGGVVINdvpTFRV-D-HMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
29-485 |
6.24e-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: 328.16 E-value: 6.24e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 29 NPSTGDVYCRVPDSGKEEVEAAVRAAKNaFPiwSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARtVDIP 108
Cdd:cd07146 5 NPYTGEVVGTVPAGTEEALREALALAAS-YR--STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR-YEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 109 RAVYNFRFFASSILHHTTEC--TEMASMGCVH--YTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTS 184
Cdd:cd07146 81 RAADVLRFAAAEALRDDGESfsCDLTANGKARkiFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 185 VTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAphCKKLSLELGGKNPAIIFD 264
Cdd:cd07146 161 LSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIVMD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 265 DADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKK 344
Cdd:cd07146 239 DADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 345 AKAEGAKILCGegvdslalpaGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVW 424
Cdd:cd07146 319 AIAQGARVLLG----------NQRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVC 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024393110 425 SSNVGRVHRVARRLQSGLVwtNCWLV---RDLNLPFGGMKASGIG-REGAKDSYEFFTEVKTITI 485
Cdd:cd07146 389 TNDLDTIKRLVERLDVGTV--NVNEVpgfRSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
30-484 |
7.60e-107 |
|
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: 325.42 E-value: 7.60e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 30 PSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLI---EHDLEAFAQAESkdqGKT--ITFART 104
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVlerRDELLDLIQLET---GKArrHAFEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 105 VDiprAVYNFRFFASS---------------ILHHTTECtemasmgcvhytsRTPVGVAGLISPWNLPLYLLTWKIAPAI 169
Cdd:cd07101 80 LD---VAIVARYYARRaerllkprrrrgaipVLTRTTVN-------------RRPKGVVGVISPWNYPLTLAVSDAIPAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 170 ACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDvpLISFTGSTLTAQRITEKSAPHCKK 249
Cdd:cd07101 144 LAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNAD--YVMFTGSTATGRVVAERAGRRLIG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 250 LSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGAL 329
Cdd:cd07101 222 CSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 330 ISKEHLEKVRSYVKKAKAEGAKILCGeGVdslALPagNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVV 409
Cdd:cd07101 302 ISQAQLDRVTAHVDDAVAKGATVLAG-GR---ARP--DLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 410 KRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTN-----CWLVRDlnLPFGGMKASGIGREGAKDSYEFFTEVKTIT 484
Cdd:cd07101 376 ELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNegyaaAWASID--APMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
25-484 |
6.64e-105 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 322.60 E-value: 6.64e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 25 IDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLI---EHDLEAFAQAESkdqGKtitf 101
Cdd:PRK09407 34 REVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVlenREELLDLVQLET---GK---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 102 AR------TVDIPravYNFRFFASS---------------ILHHTTECtemasmgcvhytsRTPVGVAGLISPWNLPLYL 160
Cdd:PRK09407 107 ARrhafeeVLDVA---LTARYYARRapkllaprrragalpVLTKTTEL-------------RQPKGVVGVISPWNYPLTL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 161 LTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDvpLISFTGSTLTAQRIT 240
Cdd:PRK09407 171 AVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDNAD--YLMFTGSTATGRVLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 241 EKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPS 320
Cdd:PRK09407 249 EQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 321 DPTVDVGALISKEHLEKVRSYVKKAKAEGAKILCGeGVdslALPagNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVV 400
Cdd:PRK09407 329 DYSADMGSLISEAQLETVSAHVDDAVAKGATVLAG-GK---ARP--DLGPLFYEPTVLTGVTPDMELAREETFGPVVSVY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 401 AFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTN-----CWLVRDlnLPFGGMKASGIGREGAKDSYE 475
Cdd:PRK09407 403 PVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVD--APMGGMKDSGLGRRHGAEGLL 480
|
....*....
gi 2024393110 476 FFTEVKTIT 484
Cdd:PRK09407 481 KYTESQTIA 489
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
9-486 |
1.97e-104 |
|
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: 319.90 E-value: 1.97e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 9 VLENFIAGRFVPCS-SYIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEK-SQILNKLADLIEHDLEA 86
Cdd:cd07082 1 QFKYLINGEWKESSgKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLEErIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 87 FAQAESKDQGKT-----ITFARTVD-IPRAVYNF-RFFASSILHHTTECTEmasmGCVHYTSRTPVGVAGLISPWNLPLY 159
Cdd:cd07082 81 VANLLMWEIGKTlkdalKEVDRTIDyIRDTIEELkRLDGDSLPGDWFPGTK----GKIAQVRREPLGVVLAIGPFNYPLN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 160 LLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRI 239
Cdd:cd07082 157 LTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 240 TEKSapHCKKLSLELGGKNPAIIFDDADL----SQCIPTTLrsSFANQgeicLCTS--RIFVQRGIYSEFVKRFVAETKK 313
Cdd:cd07082 237 KKQH--PMKRLVLELGGKDPAIVLPDADLelaaKEIVKGAL--SYSGQ----RCTAikRVLVHESVADELVELLKEEVAK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 314 WKVGNPSDPTVDVGALISKEHLEKVRSYVKKAKAEGAKILCGEgvdslalpaGNQKGYFMLPTVIAEIKDESCCMQEEIF 393
Cdd:cd07082 309 LKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG---------GREGGNLIYPTLLDPVTPDMRLAWEEPF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 394 GPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVR--DlNLPFGGMKASGIGREGAK 471
Cdd:cd07082 380 GPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRgpD-HFPFLGRKDSGIGTQGIG 458
|
490
....*....|....*
gi 2024393110 472 DSYEFFTEVKTITIK 486
Cdd:cd07082 459 DALRSMTRRKGIVIN 473
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
13-485 |
8.09e-100 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 308.37 E-value: 8.09e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQA 90
Cdd:PRK11241 14 LINGEWLDANNgeVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 91 ESKDQGKTITFARTvDIPRAVYNFRFFAS--------SILHHTTECTEMasmgcvhyTSRTPVGVAGLISPWNLPLYLLT 162
Cdd:PRK11241 94 MTLEQGKPLAEAKG-EISYAASFIEWFAEegkriygdTIPGHQADKRLI--------VIKQPIGVTAAITPWNFPAAMIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 163 WKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEK 242
Cdd:PRK11241 165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 243 SAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDP 322
Cdd:PRK11241 245 CAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 323 TVDVGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDSLAlpagnqkGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAF 402
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELG-------GNFFQPTILVDVPANAKVAKEETFGPLAPLFRF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 403 DTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKT 482
Cdd:PRK11241 398 KDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKY 477
|
...
gi 2024393110 483 ITI 485
Cdd:PRK11241 478 MCI 480
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
47-485 |
1.17e-97 |
|
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: 300.92 E-value: 1.17e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 47 VEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFART-VDIPRAVynFRFFA---SSIL 122
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAeVEKCAWI--CRYYAenaEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 123 hhttECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHG 202
Cdd:cd07100 79 ----ADEPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 203 VVNMVFGTGAKAgEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFAN 282
Cdd:cd07100 155 VFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 283 QGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDsla 362
Cdd:cd07100 234 AGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRP--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 363 lpagNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGL 442
Cdd:cd07100 311 ----DGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2024393110 443 VWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07100 387 VFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
14-484 |
6.97e-97 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 301.85 E-value: 6.97e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 14 IAGRFVPCSSYIDSYNPS-TGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLI---EHDLEAFaq 89
Cdd:PRK03137 41 IGGERITTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIrrrKHEFSAW-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 90 aESKDQGKTITFArTVDIPRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAI 169
Cdd:PRK03137 119 -LVKEAGKPWAEA-DADTAEAIDFLEYYARQMLKLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 170 ACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA---P- 245
Cdd:PRK03137 197 VAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAkvqPg 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 246 --HCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPT 323
Cdd:PRK03137 277 qiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 324 vDVGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDSlalpagnqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFD 403
Cdd:PRK03137 357 -YMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDS--------KGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAK 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 404 TEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGlvwtNCWLVRDLN------LPFGGMKASGI-GREGAKDSYEF 476
Cdd:PRK03137 428 DFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVG----NLYFNRGCTgaivgyHPFGGFNMSGTdSKAGGPDYLLL 503
|
....*...
gi 2024393110 477 FTEVKTIT 484
Cdd:PRK03137 504 FLQAKTVS 511
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
28-483 |
1.11e-94 |
|
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: 294.15 E-value: 1.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 28 YNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFAR---T 104
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGgeiR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 105 VDIPRAVYNFRFFASSILHHTTECTEmasmGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTS 184
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKD----GFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 185 VTAWMMCKLLEKAGMPHGVVNMVFGTGAkAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFD 264
Cdd:cd07102 157 LCGERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 265 DADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKK 344
Cdd:cd07102 236 DADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 345 AKAEGAKILCGEGVdslaLPAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVW 424
Cdd:cd07102 316 AIAKGARALIDGAL----FPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVW 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393110 425 SSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:cd07102 392 TKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
13-484 |
9.34e-94 |
|
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: 293.70 E-value: 9.34e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSSYIDSYNPS-TGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAE 91
Cdd:TIGR01237 36 VINGERVETENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 92 SKDQGKTITFArTVDIPRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIAC 171
Cdd:TIGR01237 116 VKEVGKPWNEA-DAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 172 GNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA------P 245
Cdd:TIGR01237 195 GNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvqpgqK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 246 HCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVD 325
Cdd:TIGR01237 275 HLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 326 VGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDSlalpagnqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTE 405
Cdd:TIGR01237 355 VGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDS--------KGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 406 EEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGlvwtNCWLVRDLN------LPFGGMKASGIG-REGAKDSYEFFT 478
Cdd:TIGR01237 427 DEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVG----NLYFNRNITgaivgyQPFGGFKMSGTDsKAGGPDYLALFM 502
|
....*.
gi 2024393110 479 EVKTIT 484
Cdd:TIGR01237 503 QAKTVT 508
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
73-466 |
1.87e-93 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 289.33 E-value: 1.87e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 73 LNKLADLIEHDLEAFAQAESKDQGKTITFARTVDIPRAVYnFRFFASSILHHTTECTEMASMGCVHYTSRTPVGVAGLIS 152
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADY-IDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 153 PWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGS 232
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 233 TLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETK 312
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 313 KWKVGNPSD-PTVDVGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDslalpagNQKGYFMLPTVIAEIKDESCCMQEE 391
Cdd:PRK10090 240 AVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAV-------EGKGYYYPPTLLLDVRQEMSIMHEE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024393110 392 IFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIG 466
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIG 387
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-484 |
9.92e-93 |
|
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: 289.58 E-value: 9.92e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 28 YNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARTVDI 107
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 108 PRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRT---PVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTS 184
Cdd:cd07098 81 LVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVeyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 185 -VTAW---MMCKLLEKAGMPHGVVNMVFGTGaKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPA 260
Cdd:cd07098 161 wSSGFflsIIRECLAACGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 261 IIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRS 340
Cdd:cd07098 240 IVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 341 YVKKAKAEGAKILC-GEGVDSLALPagnqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGL 419
Cdd:cd07098 320 LVADAVEKGARLLAgGKRYPHPEYP----QGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393110 420 AATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLN--LPFGGMKASGIGREGAKDSYEFFTEVKTIT 484
Cdd:cd07098 396 GASVFGKDIKRARRIASQLETGMVAINDFGVNYYVqqLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
13-466 |
8.63e-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: 270.61 E-value: 8.63e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSSYIDSYNPSTGD-VYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEH---DLEAFA 88
Cdd:cd07125 36 IINGEETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEAnrgELIALA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 89 QAESkdqGKTITFArTVDIPRAVyNF-RFFASSILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAP 167
Cdd:cd07125 116 AAEA---GKTLADA-DAEVREAI-DFcRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 168 AIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHC 247
Cdd:cd07125 191 ALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 248 K---KLSLELGGKNpAIIFDD-ADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPT 323
Cdd:cd07125 271 GpilPLIAETGGKN-AMIVDStALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 324 VDVGALISKEHLEKVRSYVKKAKAEgAKILCgegvdslALPAGNQKGYFMLPTVIaEIkDESCCMQEEIFGPVTCVVAFD 403
Cdd:cd07125 350 TDVGPLIDKPAGKLLRAHTELMRGE-AWLIA-------PAPLDDGNGYFVAPGII-EI-VGIFDLTTEVFGPILHVIRFK 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024393110 404 TE--EEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGlvwtNCWLVRD------LNLPFGGMKASGIG 466
Cdd:cd07125 420 AEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG----NLYINRNitgaivGRQPFGGWGLSGTG 486
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
13-484 |
3.04e-81 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 260.20 E-value: 3.04e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSS--YIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQA 90
Cdd:TIGR01722 4 WIGGKFAEGASgtYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 91 ESKDQGKTITFARTvDIPRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:TIGR01722 84 ITAEHGKTHSDALG-DVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 171 CGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGtGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKL 250
Cdd:TIGR01722 163 CGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 251 SLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIfVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALI 330
Cdd:TIGR01722 242 QALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAA-VLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 331 SKEHLEKVRSYVKKAKAEGAKILC-GEGVDSlalpAGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVV 409
Cdd:TIGR01722 321 TPQAKDRVASLIAGGAAEGAEVLLdGRGYKV----DGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393110 410 KRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNL-PFGGMKASGIGREGA--KDSYEFFTEVKTIT 484
Cdd:TIGR01722 397 ALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYfSFTGWKDSFFGDHHIygKQGTHFYTRGKTVT 474
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
13-487 |
1.02e-79 |
|
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: 256.74 E-value: 1.02e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSSYIDSYNPS-TGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAE 91
Cdd:cd07083 22 VIGGEWVDTKERMVSVSPFaPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 92 SKDQGKTITFArTVDIPRAVYNFRFFASSILHHTTECTEMASM-GCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIA 170
Cdd:cd07083 102 TYEVGKNWVEA-IDDVAEAIDFIRYYARAALRLRYPAVEVVPYpGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 171 CGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHC--- 247
Cdd:cd07083 181 VGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLApgq 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 248 ---KKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTV 324
Cdd:cd07083 261 twfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 325 DVGALISKEHLEKVRSYVKKAKAEGAKILCGEgvdslaLPAGNqkGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDT 404
Cdd:cd07083 341 DLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGK------RLEGE--GYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 405 EE--EVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDL--NLPFGGMKASGIG-REGAKDSYEFFTE 479
Cdd:cd07083 413 DDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALvgVQPFGGFKLSGTNaKTGGPHYLRRFLE 492
|
....*...
gi 2024393110 480 VKTITIKH 487
Cdd:cd07083 493 MKAVAERF 500
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
15-487 |
6.05e-78 |
|
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: 251.36 E-value: 6.05e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 15 AGRFVPCSSYIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKD 94
Cdd:cd07130 4 DGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 95 QGKTITFAR-----TVDI-PRAVYNFRFFASSILHhttecTEMAsmGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPA 168
Cdd:cd07130 84 MGKILPEGLgevqeMIDIcDFAVGLSRQLYGLTIP-----SERP--GHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 169 IACGNTVVAKPSEMTSVTAWMMCKL----LEKAGMPHGVVNMVFGtGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSA 244
Cdd:cd07130 157 LVCGNVVVWKPSPTTPLTAIAVTKIvarvLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 245 PHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTV 324
Cdd:cd07130 236 ARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 325 DVGALISKEHLEKVRSYVKKAKAEGAKILCGegvdslalpaGNQ---KGYFMLPTvIAEIKDESCCMQEEIFGPVTCVVA 401
Cdd:cd07130 316 LVGPLHTKAAVDNYLAAIEEAKSQGGTVLFG----------GKVidgPGNYVEPT-IVEGLSDAPIVKEETFAPILYVLK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 402 FDTEEEVVKRANGVKYGLAATVWSSNVGRVHRvarrlqsglvW-----TNCWLVrDLNLP---------FGGMKASGIGR 467
Cdd:cd07130 385 FDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFR----------WlgpkgSDCGIV-NVNIGtsgaeiggaFGGEKETGGGR 453
|
490 500
....*....|....*....|
gi 2024393110 468 EGAKDSYEFFTEVKTITIKH 487
Cdd:cd07130 454 ESGSDAWKQYMRRSTCTINY 473
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
25-485 |
5.41e-75 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 243.11 E-value: 5.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 25 IDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFART 104
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 105 vDIPRAVYNFRFFA---SSILhhTTECTEMASMGCVH-YTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPS 180
Cdd:PRK09406 83 -EALKCAKGFRYYAehaEALL--ADEPADAAAVGASRaYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 181 EMTSVTAWMMCKLLEKAGMPHGVvnmvFGT---GAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGK 257
Cdd:PRK09406 160 SNVPQTALYLADLFRRAGFPDGC----FQTllvGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 258 NPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEK 337
Cdd:PRK09406 236 DPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 338 VRSYVKKAKAEGAKILCGEgvdslALPAGNqkGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKY 417
Cdd:PRK09406 316 VEKQVDDAVAAGATILCGG-----KRPDGP--GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTF 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393110 418 GLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:PRK09406 389 GLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
46-470 |
7.19e-75 |
|
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: 242.18 E-value: 7.19e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 46 EVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFART--------VDIPRAVYNFRFf 117
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDISIKAYHERT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 118 assilhhTTECTEMASM-GCVHYTsrtPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEK 196
Cdd:cd07095 80 -------GERATPMAQGrAVLRHR---PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 197 AGMPHGVVNMVFGtGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKK-LSLELGGKNPAIIFDDADLSQCIPTT 275
Cdd:cd07095 150 AGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKiLALEMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 276 LRSSFANQGEICLCTSRIFVQRGIYS-EFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKKAKAEGAKILc 354
Cdd:cd07095 229 VQSAFLTAGQRCTCARRLIVPDGAVGdAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 355 gegvdsLALPAGNQKGYFMLPTVIaEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRV 434
Cdd:cd07095 308 ------LAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERF 380
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2024393110 435 ARRLQSGLVWTNcwlvRDLN-----LPFGGMKASGIGREGA 470
Cdd:cd07095 381 LARIRAGIVNWN----RPTTgasstAPFGGVGLSGNHRPSA 417
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
13-470 |
1.37e-71 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 235.24 E-value: 1.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSSY-IDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAE 91
Cdd:PRK09457 4 WINGDWIAGQGEaFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 92 SKDQGKTITFART--------VDIPRAVYNFRffassilhhtTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTW 163
Cdd:PRK09457 84 ARETGKPLWEAATevtaminkIAISIQAYHER----------TGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 164 KIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGtGAKAGEALVCHPDVPLISFTGSTLTAQRITEKS 243
Cdd:PRK09457 154 HIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 244 APHCKK-LSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSE-FVKRFVAETKKWKVGNP-S 320
Cdd:PRK09457 233 AGQPEKiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWdA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 321 DPTVDVGALISKEHLEKVRSYVKKAKAEGAKILcgegvdsLALPAGNQKGYFMLP-----TVIAEIKDesccmqEEIFGP 395
Cdd:PRK09457 313 EPQPFMGAVISEQAAQGLVAAQAQLLALGGKSL-------LEMTQLQAGTGLLTPgiidvTGVAELPD------EEYFGP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 396 VTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNcwlvRDLN-----LPFGGMKASGIGREGA 470
Cdd:PRK09457 380 LLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWN----KPLTgassaAPFGGVGASGNHRPSA 455
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
25-485 |
8.21e-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: 229.61 E-value: 8.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 25 IDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPL-EKSQILNKLADLIEHDLEAFAQAESKDQGKTITFAR 103
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWLPAhERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 104 tVDIPRAVYNFRFFASSILHHTTECTEM----ASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKP 179
Cdd:cd07148 81 -VEVTRAIDGVELAADELGQLGGREIPMgltpASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 180 SEMTSVTAWMMCKLLEKAGMPHGVVNMVFgTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHcKKLSLELGGKNP 259
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 260 AIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVR 339
Cdd:cd07148 238 VIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 340 SYVKKAKAEGAKILCGEGVDSLALPAgnqkgyfmlPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGL 419
Cdd:cd07148 318 EWVNEAVAAGARLLCGGKRLSDTTYA---------PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAF 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024393110 420 AATVWSSNVGRVHRVARRLQSGLVWTN-------CWlvrdlnLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07148 389 QAAVFTKDLDVALKAVRRLDATAVMVNdhtafrvDW------MPFAGRRQSGYGTGGIPYTMHDMTQEKMAVI 455
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
12-484 |
1.27e-68 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 230.40 E-value: 1.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 12 NFIAGRFVPC--SSYIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQ 89
Cdd:PLN02419 116 NLIGGSFVESqsSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 90 AESKDQGKTITFARTvDIPRAVYNFRFFASSILHHTTECTEMASMGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAI 169
Cdd:PLN02419 196 NITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 170 ACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAgEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKK 249
Cdd:PLN02419 275 TCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 250 LSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSR-IFVqrGIYSEFVKRFVAETKKWKVGNPSDPTVDVGA 328
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFV--GDAKSWEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 329 LISKEHLEKVRSYVKKAKAEGAKILCgEGVDsLALPaGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEV 408
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLL-DGRD-IVVP-GYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393110 409 VKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLN-LPFGGMKASGIGREG--AKDSYEFFTEVKTIT 484
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPfFSFTGNKASFAGDLNfyGKAGVDFFTQIKLVT 587
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
28-466 |
8.38e-66 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 229.82 E-value: 8.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 28 YNPS-TGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAF---AQAESkdqGKTITFA- 102
Cdd:COG4230 575 RNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELmalLVREA---GKTLPDAi 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 103 ---R-TVDipravynF-RFFASSILHHttectemasmgCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVA 177
Cdd:COG4230 652 aevReAVD-------FcRYYAAQARRL-----------FAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLA 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 178 KPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRI-------TEKSAPhckkL 250
Cdd:COG4230 714 KPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLInrtlaarDGPIVP----L 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 251 SLELGGKNpAIIFDD-ADLSQCIPTTLRSSFANQGEIClctS--RI-FVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDV 326
Cdd:COG4230 790 IAETGGQN-AMIVDSsALPEQVVDDVLASAFDSAGQRC---SalRVlCVQEDIADRVLEMLKGAMAELRVGDPADLSTDV 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 327 GALISKEHLEKVRSYVKKAKAEGAKIlcgegvDSLALPAGNQKGYFMLPTVIaEIK--DEsccMQEEIFGPVTCVVAFDT 404
Cdd:COG4230 866 GPVIDAEARANLEAHIERMRAEGRLV------HQLPLPEECANGTFVAPTLI-EIDsiSD---LEREVFGPVLHVVRYKA 935
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024393110 405 EE--EVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGlvwtNCWLVRdlNL--------PFGGMKASGIG 466
Cdd:COG4230 936 DEldKVIDAINATGYGLTLGVHSRIDETIDRVAARARVG----NVYVNR--NIigavvgvqPFGGEGLSGTG 1001
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
66-485 |
9.31e-64 |
|
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: 212.77 E-value: 9.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 66 PLE--KSQiLNKLADLIEHDLEAFAQAESKDQGKTITFA-------------------------RTVDIPRAVynfrFFA 118
Cdd:cd07087 18 SLEwrKAQ-LKALKRMLTENEEEIAAALYADLGKPPAEAylteiavvlgeidhalkhlkkwmkpRRVSVPLLL----QPA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 119 SSILHhttectemasmgcvhytsRTPVGVAGLISPWNLPLYLLtwkIAP---AIACGNTVVAKPSEMTSVTAWMMCKLLE 195
Cdd:cd07087 93 KAYVI------------------PEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 196 KAgMPHGVVNMVFGTGAKAGEALVCHPDvpLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLsqciPTT 275
Cdd:cd07087 152 KY-FDPEAVAVVEGGVEVATALLAEPFD--HIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANL----EVA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 276 LRS----SFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTvDVGALISKEHLEKVRSYVkkakaEGAK 351
Cdd:cd07087 225 ARRiawgKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRLASLL-----DDGK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 352 ILCGEGVDslalpagnQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRV 431
Cdd:cd07087 299 VVIGGQVD--------KEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQ 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024393110 432 HRVARRLQSGLVWTNcwlvrDL-------NLPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:cd07087 371 ERVLAETSSGGVCVN-----DVllhaaipNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
34-466 |
1.53e-63 |
|
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: 214.39 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 34 DVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFArTVDIPRAVYN 113
Cdd:TIGR01238 63 DIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNA-IAEVREAVDF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 114 FRFFASSILHHTTEctemasmgcvhyTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKL 193
Cdd:TIGR01238 142 CRYYAKQVRDVLGE------------FSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVEL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 194 LEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCK---KLSLELGGKNPAIIFDDADLSQ 270
Cdd:TIGR01238 210 MQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDapvPLIAETGGQNAMIVDSTALPEQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 271 CIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKKAKAEGA 350
Cdd:TIGR01238 290 VVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 351 KILCGEGVDSLAlpagNQKGYFMLPTVIaEIkDESCCMQEEIFGPVTCVVAFDTEE--EVVKRANGVKYGLAATVWSSNV 428
Cdd:TIGR01238 370 KIAQLTLDDSRA----CQHGTFVAPTLF-EL-DDIAELSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIE 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2024393110 429 GRVHRVARRLQSGlvwtNCWLVRDL------NLPFGGMKASGIG 466
Cdd:TIGR01238 444 TTYRWIEKHARVG----NCYVNRNQvgavvgVQPFGGQGLSGTG 483
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
27-483 |
4.84e-62 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 209.33 E-value: 4.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 27 SYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARTvD 106
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-E 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 107 IPRAVYNFRFFAS---SILhhTTECTEMASMGCVhyTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMT 183
Cdd:PRK13968 90 VAKSANLCDWYAEhgpAML--KAEPTLVENQQAV--IEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 184 SVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEAlVCHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIF 263
Cdd:PRK13968 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQM-INDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 264 DDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVK 343
Cdd:PRK13968 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 344 KAKAEGAKILCG-EGVdslalpAGnqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAAT 422
Cdd:PRK13968 325 ATLAEGARLLLGgEKI------AG--AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSAT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024393110 423 VWSSNVGRVHRVARRLQSGLVWTNCWLVRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
38-466 |
3.89e-60 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 213.14 E-value: 3.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 38 RVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLE---AFAQAESkdqGKTITFArtVDIPR-AVyN 113
Cdd:PRK11904 578 EVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAeliALCVREA---GKTLQDA--IAEVReAV-D 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 114 F-RFFASSILHHTTECTEMAS-MGCVHYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMC 191
Cdd:PRK11904 652 FcRYYAAQARRLFGAPEKLPGpTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAV 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 192 KLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRIT----EKSAPhckKLSL--ELGGKNpAIIFDD 265
Cdd:PRK11904 732 KLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINrtlaARDGP---IVPLiaETGGQN-AMIVDS 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 266 -ADLSQCIPTTLRSSFANQGEIClctS--RI-FVQRGIYS---EFVKRFVAETkkwKVGNPSDPTVDVGALISKEHLEKV 338
Cdd:PRK11904 808 tALPEQVVDDVVTSAFRSAGQRC---SalRVlFVQEDIADrviEMLKGAMAEL---KVGDPRLLSTDVGPVIDAEAKANL 881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 339 RSYVKKAKAEgAKILCgegvdSLALPAGNQKGYFMLPTVIaEIKDEScCMQEEIFGPVTCVVAFDTEE--EVVKRANGVK 416
Cdd:PRK11904 882 DAHIERMKRE-ARLLA-----QLPLPAGTENGHFVAPTAF-EIDSIS-QLEREVFGPILHVIRYKASDldKVIDAINATG 953
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393110 417 YGLAATVWSSNVGRVHRVARRLQSGlvwtNCWLVRdlNL--------PFGGMKASGIG 466
Cdd:PRK11904 954 YGLTLGIHSRIEETADRIADRVRVG----NVYVNR--NQigavvgvqPFGGQGLSGTG 1005
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
28-466 |
4.01e-60 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 213.57 E-value: 4.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 28 YNPS-TGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTItfARTVD 106
Cdd:PRK11905 572 LNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTL--ANAIA 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 107 IPR-AVYNFRFFASSIlhhttECTEMASmgcvhytSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSV 185
Cdd:PRK11905 650 EVReAVDFLRYYAAQA-----RRLLNGP-------GHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPL 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 186 TAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKK---LSLELGGKNpAII 262
Cdd:PRK11905 718 IAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPpvpLIAETGGQN-AMI 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 263 FDDADLS-QCIPTTLRSSFANQGEIClctS--RI-FVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKV 338
Cdd:PRK11905 797 VDSSALPeQVVADVIASAFDSAGQRC---SalRVlCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANI 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 339 RSYVKKAKAEGAKilcgegVDSLALPAGNQKGYFMLPTVIaEIKDEScCMQEEIFGPVTCVVAFDTEE--EVVKRANGVK 416
Cdd:PRK11905 874 EAHIEAMRAAGRL------VHQLPLPAETEKGTFVAPTLI-EIDSIS-DLEREVFGPVLHVVRFKADEldRVIDDINATG 945
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393110 417 YGLAATVWSSNVGRVHRVARRLQSGLVWTNcwlvRdlNL--------PFGGMKASGIG 466
Cdd:PRK11905 946 YGLTFGLHSRIDETIAHVTSRIRAGNIYVN----R--NIigavvgvqPFGGEGLSGTG 997
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
137-467 |
8.42e-60 |
|
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: 202.46 E-value: 8.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 137 VHYTSRtpvGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVnmVFGTGAKAGE 216
Cdd:cd07134 96 IRYEPK---GVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA--VFEGDAEVAQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 217 ALVchpDVPL--ISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIF 294
Cdd:cd07134 171 ALL---ELPFdhIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVF 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 295 VQRGIYSEFVKRFVAETKKWKVGNPSDP-TVDVGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDslalPAGNqkgyFM 373
Cdd:cd07134 248 VHESVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD----AAQR----YI 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 374 LPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVR-- 451
Cdd:cd07134 320 APTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHfl 399
|
330
....*....|....*.
gi 2024393110 452 DLNLPFGGMKASGIGR 467
Cdd:cd07134 400 NPNLPFGGVNNSGIGS 415
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
45-483 |
1.30e-59 |
|
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: 202.06 E-value: 1.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 45 EEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARTVDIpRAVYNFRFFASSILHH 124
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEV-SGVKNDILHMLKNLKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 125 TTECTEMASMGCVHYTSRT-----PVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAgM 199
Cdd:cd07135 84 WAKDEKVKDGPLAFMFGKPrirkePLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 200 PHGVVNMVFGTGAKAGEALVCHPDvpLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADlsqcIPTTLR-- 277
Cdd:cd07135 163 DPDAFQVVQGGVPETTALLEQKFD--KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNAD----LELAAKri 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 278 --SSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTvDVGALISKEHLEKVRSYVKKAKaeGAKILCG 355
Cdd:cd07135 237 lwGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSLLDTTK--GKVVIGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 356 EgvdslalpaGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVA 435
Cdd:cd07135 314 E---------MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHIL 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2024393110 436 RRLQSG-LVWTNCWLVRDL-NLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:cd07135 385 TRTRSGgVVINDTLIHVGVdNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
37-464 |
1.10e-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: 196.65 E-value: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 37 CRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIE----HDLEAfaqAESKDQGKTITFARTVDIPRAVY 112
Cdd:cd07123 61 ATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgkyrYELNA---ATMLGQGKNVWQAEIDAACELID 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 113 NFRF---FASSILHHTTECTEMASMGCVHYtsRTPVGVAGLISPWN-------LPLylltwkiAPAIAcGNTVVAKPSEM 182
Cdd:cd07123 138 FLRFnvkYAEELYAQQPLSSPAGVWNRLEY--RPLEGFVYAVSPFNftaiggnLAG-------APALM-GNVVLWKPSDT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 183 TSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITE---------KSAPhckKLSLE 253
Cdd:cd07123 208 AVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKqigenldryRTYP---RIVGE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 254 LGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKE 333
Cdd:cd07123 285 TGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEK 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 334 HLEKVRSYVKKAKAE-GAKILCG-EGVDSlalpagnqKGYFMLPTVIaEIKD-ESCCMQEEIFGPVTCVVAFDTE--EEV 408
Cdd:cd07123 365 AFDRIKGYIDHAKSDpEAEIIAGgKCDDS--------VGYFVEPTVI-ETTDpKHKLMTEEIFGPVLTVYVYPDSdfEET 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024393110 409 VKRANGV-KYGLAATVWSSNVGRVHRVARRLQ--SGLVWTNC----WLVRdlNLPFGGMKASG 464
Cdd:cd07123 436 LELVDTTsPYALTGAIFAQDRKAIREATDALRnaAGNFYINDkptgAVVG--QQPFGGARASG 496
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
28-485 |
2.73e-56 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 194.97 E-value: 2.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 28 YNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSsKSPLEK-SQILNKLADLIEHDLEAFAQAESKDQGKTITFARTvD 106
Cdd:PLN00412 36 TNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWA-KTPLWKrAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVT-E 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 107 IPR--------AVYNFRFFASSILHHT-----TECTEMasmgCVhyTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGN 173
Cdd:PLN00412 114 VVRsgdlisytAEEGVRILGEGKFLVSdsfpgNERNKY----CL--TSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 174 TVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTlTAQRITEKSA--PhckkLS 251
Cdd:PLN00412 188 AVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TGIAISKKAGmvP----LQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 252 LELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDpTVDVGALIS 331
Cdd:PLN00412 263 MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVVS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 332 KEHLEKVRSYVKKAKAEGAKiLCGEgvdslalpaGNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKR 411
Cdd:PLN00412 342 ESSANFIEGLVMDAKEKGAT-FCQE---------WKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHH 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024393110 412 ANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLN-LPFGGMKASGIGREGAKDSYEFFTEVKTITI 485
Cdd:PLN00412 412 CNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQGITNSINMMTKVKSTVI 486
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
66-487 |
1.75e-55 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 192.55 E-value: 1.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 66 PLE-KSQILNKLADLIEHDLEAFAQAESKDQGKTITFARTVDIPRAVYNFRFFASSILHHTTEctEMASMGCVH-----Y 139
Cdd:PTZ00381 27 PLEfRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKP--EKVDTVGVFgpgksY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 140 TSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAgMPHGVVNMVFGtGAKAGEALV 219
Cdd:PTZ00381 105 IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 220 CHP-DvpLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRG 298
Cdd:PTZ00381 183 KEPfD--HIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 299 IYSEFVKRFVAETKKWKVGNPSDPTvDVGALISKEHLEKVRSYVKKakaEGAKILCGEGVDSlalpagNQKgyFMLPTVI 378
Cdd:PTZ00381 261 IKDKFIEALKEAIKEFFGEDPKKSE-DYSRIVNEFHTKRLAELIKD---HGGKVVYGGEVDI------ENK--YVAPTII 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 379 AEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLN--LP 456
Cdd:PTZ00381 329 VNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNpnLP 408
|
410 420 430
....*....|....*....|....*....|.
gi 2024393110 457 FGGMKASGIGREGAKDSYEFFTEVKTITIKH 487
Cdd:PTZ00381 409 FGGVGNSGMGAYHGKYGFDTFSHPKPVLNKS 439
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
52-483 |
1.89e-53 |
|
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: 185.77 E-value: 1.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 52 RAA--KNAFPIWSsksplEKSQILNKLADLIEHDLEAFAQAESKDQGKtitfartvdipRAvynfrffassilHHTTECT 129
Cdd:cd07133 8 KAAflANPPPSLE-----ERRDRLDRLKALLLDNQDALAEAISADFGH-----------RS------------RHETLLA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 130 E-MASMGCVHYTSR--------------------------TPVGVAGLISPWNLPLYLLtwkIAP---AIACGNTVVAKP 179
Cdd:cd07133 60 EiLPSIAGIKHARKhlkkwmkpsrrhvgllflpakaeveyQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 180 SEMTSVTAWMMCKLLEKAGMPHGVVnmVFGTGAKAGEALVCHPDVPLIsFTGSTLTAQRITEKSAPHCKKLSLELGGKNP 259
Cdd:cd07133 137 SEFTPRTSALLAELLAEYFDEDEVA--VVTGGADVAAAFSSLPFDHLL-FTGSTAVGRHVMRAAAENLTPVTLELGGKSP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 260 AIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKW---KVGNPsdptvDVGALISKEHLE 336
Cdd:cd07133 214 AIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 337 KVRSYVKKAKAEGAKIL-CGEGVDSLalpAGNQKgyfMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGV 415
Cdd:cd07133 289 RLQGLLEDARAKGARVIeLNPAGEDF---AATRK---LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINAR 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 416 KYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWL--VRDLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:cd07133 363 PRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLlhVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
71-483 |
5.62e-53 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 185.02 E-value: 5.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 71 QILNKLADLIEHDLEAFAQAESKDQGKT---------------ITFA--------RTVDIPRAVYNFrfFASSilhhtte 127
Cdd:cd07136 24 EQLKKLKQAIKKYENEILEALKKDLGKSefeaymteigfvlseINYAikhlkkwmKPKRVKTPLLNF--PSKS------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 128 ctemasmgcvhYTSRTPVGVAGLISPWNLPLYLLtwkIAP---AIACGNTVVAKPSEMTSVTAWMMCKLLEKAgMPHGVV 204
Cdd:cd07136 95 -----------YIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 205 NMVFGtGAKAGEALVcHPDVPLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQG 284
Cdd:cd07136 160 AVVEG-GVEENQELL-DQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 285 EICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDpTVDVGALISKEHLEKVRSYVkkakaEGAKILCGEGVDSLALp 364
Cdd:cd07136 238 QTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGLL-----DNGKIVFGGNTDRETL- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 365 agnqkgyFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVW 444
Cdd:cd07136 311 -------YIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGC 383
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2024393110 445 TNCWLVR--DLNLPFGGMKASGIGREGAKDSYEFFTEVKTI 483
Cdd:cd07136 384 INDTIMHlaNPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
29-466 |
9.90e-52 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 189.03 E-value: 9.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 29 NPS-TGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTitFARTV-D 106
Cdd:PRK11809 665 NPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKT--FSNAIaE 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 107 IPRAVYNFRFFASSILHHTTECTemasmgcvHytsrTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVT 186
Cdd:PRK11809 743 VREAVDFLRYYAGQVRDDFDNDT--------H----RPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 187 AWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGST----LTAQRITEKSAP--HCKKLSLELGGKNpA 260
Cdd:PRK11809 811 AAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTevarLLQRNLAGRLDPqgRPIPLIAETGGQN-A 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 261 IIFDDADLS-QCIPTTLRSSFANQGEIC-----LCTSRIFVQRGIysEFVKRFVAEtkkWKVGNPSDPTVDVGALISKEH 334
Cdd:PRK11809 890 MIVDSSALTeQVVADVLASAFDSAGQRCsalrvLCLQDDVADRTL--KMLRGAMAE---CRMGNPDRLSTDIGPVIDAEA 964
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 335 LEKVRSYVKKAKAEGAKilcgegVDSLALPAG--NQKGYFMLPTVIaEIK--DEsccMQEEIFGPVTCVVAFDTEE--EV 408
Cdd:PRK11809 965 KANIERHIQAMRAKGRP------VFQAARENSedWQSGTFVPPTLI-ELDsfDE---LKREVFGPVLHVVRYNRNQldEL 1034
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393110 409 VKRANGVKYGLAATVWSSNVGRVHRVARRLQSGlvwtNCWLVRdlNL--------PFGGMKASGIG 466
Cdd:PRK11809 1035 IEQINASGYGLTLGVHTRIDETIAQVTGSAHVG----NLYVNR--NMvgavvgvqPFGGEGLSGTG 1094
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
25-464 |
1.96e-51 |
|
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: 182.68 E-value: 1.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 25 IDSYNPSTGD-VYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLI----EHDLEAfaqAESKDQGKTI 99
Cdd:TIGR01236 48 IPQVNPHNHQaVLAKATNATEEDAMKAVEAALDAKKDWSNLPFYDRAAIFLKAADLLsgpyRYEILA---ATMLGQSKTV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 100 TFARTVDIPRAVYNFRF---FASSILHHTTEctemASMGCVHYTSRTPV-GVAGLISPWNLPLYLLTWKIAPAIAcGNTV 175
Cdd:TIGR01236 125 YQAEIDAVAELIDFFRFnvkYARELYAQQPI----SAPGEWNRTEYRPLeGFVYAISPFNFTAIAGNLAGAPALM-GNTV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 176 VAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGSTLTAQRITEKSAPHCKK------ 249
Cdd:TIGR01236 200 VWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRyhnfpr 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 250 LSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGAL 329
Cdd:TIGR01236 280 IVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLLAELQSVKVGDPDDFRGFMGAV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 330 ISKEHLEKVRSYVKKAKA--EGAKILCGEGVDslalpagNQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEE- 406
Cdd:TIGR01236 360 IDEQSFDKIVKYIEDAKKdpEALTILYGGKYD-------DSQGYFVEPTVVESKDPDHPLMSEEIFGPVLTVYVYPDDKy 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393110 407 ----EVVKraNGVKYGLAATVWSSNVGRVHRVARRLQ--SGLVWTN--CWLVRDLNLPFGGMKASG 464
Cdd:TIGR01236 433 keilDLVD--STSQYGLTGAVFAKDRKAILEADKKLRfaAGNFYINdkCTGAVVGQQPFGGARMSG 496
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
13-487 |
1.06e-49 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 177.33 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 13 FIAGRFVPCSSYIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAES 92
Cdd:PLN02315 24 YVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 93 KDQGKTIT-----FARTVDI-PRAVYNFRFFASSILHHTTECTEMASMGcvhytsrTPVGVAGLISPWNLPLYLLTWKIA 166
Cdd:PLN02315 104 LEMGKILAegigeVQEIIDMcDFAVGLSRQLNGSIIPSERPNHMMMEVW-------NPLGIVGVITAFNFPCAVLGWNAC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 167 PAIACGNTVVAKPSEMTSVTAWMMCKL----LEKAGMPHGVVNMVFGtGAKAGEALVCHPDVPLISFTGSTLTAQRITEK 242
Cdd:PLN02315 177 IALVCGNCVVWKGAPTTPLITIAMTKLvaevLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 243 SAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDP 322
Cdd:PLN02315 256 VNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 323 TVDVGALISKEHLEKVRSYVKKAKAEGAKILCGegvDSLALPAGNqkgyFMLPTVIaEIKDESCCMQEEIFGPVTCVVAF 402
Cdd:PLN02315 336 GTLLGPLHTPESKKNFEKGIEIIKSQGGKILTG---GSAIESEGN----FVQPTIV-EISPDADVVKEELFGPVLYVMKF 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 403 DTEEEVVKRANGVKYGLAATVWSSNVGRVHRVArrlqsGLVWTNCWLVrDLNLP---------FGGMKASGIGREGAKDS 473
Cdd:PLN02315 408 KTLEEAIEINNSVPQGLSSSIFTRNPETIFKWI-----GPLGSDCGIV-NVNIPtngaeiggaFGGEKATGGGREAGSDS 481
|
490
....*....|....
gi 2024393110 474 YEFFTEVKTITIKH 487
Cdd:PLN02315 482 WKQYMRRSTCTINY 495
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
48-486 |
6.39e-41 |
|
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: 151.99 E-value: 6.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 48 EAAVRAAKNAFPiwSSKS-PLE-KSQILNKLADLIEHDLEAFAQAESKDQGKT--------ITFARTvDIPRAVYNFRFF 117
Cdd:cd07132 1 AEAVRRAREAFS--SGKTrPLEfRIQQLEALLRMLEENEDEIVEALAKDLRKPkfeavlseILLVKN-EIKYAISNLPEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 118 ASSILHHTTECTEMASMgcvhYTSRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKL---- 193
Cdd:cd07132 78 MKPEPVKKNLATLLDDV----YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELipky 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 194 LEKAGMPhgvvnmVFGTGAKAGEALVCHP-DvpLISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCI 272
Cdd:cd07132 154 LDKECYP------VVLGGVEETTELLKQRfD--YIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 273 PTTLRSSFANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNP-SDPtvDVGALISKEHLEKVRSYVkkakaEGAK 351
Cdd:cd07132 226 RRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPkESP--DYGRIINDRHFQRLKKLL-----SGGK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 352 ILCGEGVDslalpagnQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRV 431
Cdd:cd07132 299 VAIGGQTD--------EKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVI 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393110 432 HRVARRLQSGLVWTNCWLVRDL--NLPFGGMKASGIGREGAKDSYEFFTEVKTITIK 486
Cdd:cd07132 371 NKILSNTSSGGVCVNDTIMHYTldSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
144-483 |
1.22e-35 |
|
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: 137.54 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 144 PVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAgMPHGVVNMVFGtGAKAGEALVCHP- 222
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQKw 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 223 DVplISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSF-ANQGEICLCTSRIFVQRGIYS 301
Cdd:cd07137 179 DK--IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFAP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 302 EFVKRFVAETKKWKVGNPSDpTVDVGALISKEHLEKVRSYVKKAKAEgAKILCGEGVDslalpagnQKGYFMLPTVIAEI 381
Cdd:cd07137 257 TLIDALKNTLEKFFGENPKE-SKDLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGGERD--------EKNLYIEPTILLDP 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 382 KDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDLN--LPFGG 459
Cdd:cd07137 327 PLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIdtLPFGG 406
|
330 340
....*....|....*....|....
gi 2024393110 460 MKASGIGREGAKDSYEFFTEVKTI 483
Cdd:cd07137 407 VGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
47-439 |
1.09e-30 |
|
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: 123.81 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 47 VEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHD---LEAFAQAESkdqgkTITFAR-TVDIPRAVYNFRFFASSIL 122
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALgdeLVARAHAET-----GLPEARlQGELGRTTGQLRLFADLVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 123 HHT-------TECTEMASMGCVHYTSR-TPVGVAGLISPWNLPLYLLTW--KIAPAIACGNTVVAK--PSEM-TS-VTAW 188
Cdd:cd07129 76 EGSwldaridPADPDRQPLPRPDLRRMlVPLGPVAVFGASNFPLAFSVAggDTASALAAGCPVVVKahPAHPgTSeLVAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 189 MMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGST--------LTAQRiteksaPHCKKLSLELGGKNPA 260
Cdd:cd07129 156 AIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRrggralfdAAAAR------PEPIPFYAELGSVNPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 261 IIFDDAdLSQC---IPTTLRSSFA-NQGEICLCTSRIFVQRGIYSEfvkRFVAETKKwKVGnpsdpTVDVGALISKEHLE 336
Cdd:cd07129 230 FILPGA-LAERgeaIAQGFVGSLTlGAGQFCTNPGLVLVPAGPAGD---AFIAALAE-ALA-----AAPAQTMLTPGIAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 337 KVRSYVKKAKAEGakilcgeGVDSLALPAGNQKGYFMLPTVIAE-----IKDESccMQEEIFGPVTCVVAFDTEEEVVKR 411
Cdd:cd07129 300 AYRQGVEALAAAP-------GVRVLAGGAAAEGGNQAAPTLFKVdaaafLADPA--LQEEVFGPASLVVRYDDAAELLAV 370
|
410 420 430
....*....|....*....|....*....|
gi 2024393110 412 ANGVKYGLAATVWSSN--VGRVHRVARRLQ 439
Cdd:cd07129 371 AEALEGQLTATIHGEEddLALARELLPVLE 400
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
47-468 |
1.43e-29 |
|
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: 120.42 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 47 VEAAVRAAKNAFPIWSSkspLEKSQILNKLADLIEHdLEA----FAQAESKDQGKTITFArtVDIPRAVYNFRFFASSI- 121
Cdd:cd07084 1 PERALLAADISTKAARR---LALPKRADFLARIIQR-LAAksydIAAGAVLVTGKGWMFA--ENICGDQVQLRARAFVIy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 122 ---LHHTT--ECTEMASMGCVHYtsRTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEK 196
Cdd:cd07084 75 syrIPHEPgnHLGQGLKQQSHGY--RWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 197 AG-MPHGVVNMVFGTGaKAGEALVCHPDVPLISFTGSTLTAQRIteKSAPHCKKLSLELGGKNPAIIFDDAD-----LSQ 270
Cdd:cd07084 153 AGlLPPEDVTLINGDG-KTMQALLLHPNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQavdyvAWQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 271 CIpttlRSSFANQGEICLCTSRIFVqrgiYSEFVKRFVAETKKWKVGNPSDPtvdvGALISKEHLEKVRSYVKKAKAEGA 350
Cdd:cd07084 230 CV----QDMTACSGQKCTAQSMLFV----PENWSKTPLVEKLKALLARRKLE----DLLLGPVQTFTTLAMIAHMENLLG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 351 KILCGEGVDSLALPAGNQKGYFMLPTV---IAEIKDESCCMQEEIFGPVTCVVAF--DTEEEVVKRANGVKYGLAATVWS 425
Cdd:cd07084 298 SVLLFSGKELKNHSIPSIYGACVASALfvpIDEILKTYELVTEEIFGPFAIVVEYkkDQLALVLELLERMHGSLTAAIYS 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2024393110 426 SNVGRVHRVARRLQS-GLVWTNCWL---VRDLNLPFGGMKASGIGRE 468
Cdd:cd07084 378 NDPIFLQELIGNLWVaGRTYAILRGrtgVAPNQNHGGGPAADPRGAG 424
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
144-484 |
2.38e-29 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 120.22 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 144 PVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAgMPHGVVNMVFGtGAKAGEALVCHP- 222
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLLQHKw 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 223 DVplISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAiIFDDADLSQCIPTTLRSSFANQ-----GEICLCTSRIFVQR 297
Cdd:PLN02203 186 DK--IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPC-IVDSLSSSRDTKVAVNRIVGGKwgscaGQACIAIDYVLVEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 298 GIYSEFVKRFVAETKKWKVGNPSDPTvDVGALISKEHLEKVRSYVKKAKAEgAKILCGEGVDslalpagnQKGYFMLPTV 377
Cdd:PLN02203 263 RFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVA-ASIVHGGSID--------EKKLFIEPTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 378 IAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDL--NL 455
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAcdSL 412
|
330 340
....*....|....*....|....*....
gi 2024393110 456 PFGGMKASGIGREGAKDSYEFFTEVKTIT 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 ... |
146-442 |
1.18e-27 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 115.83 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 146 GVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAG-MPHGVVNMVFGTGAKAGEALVCHpDV 224
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQ-DV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 225 plISFTGSTLTAQR------ITEKSAPhckkLSLELGGKNPAIIFDDA-------DLsqCIPTTLRSSFANQGEICLCTS 291
Cdd:cd07128 225 --VAFTGSAATAAKlrahpnIVARSIR----FNAEADSLNAAILGPDAtpgtpefDL--FVKEVAREMTVKAGQKCTAIR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 292 RIFVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKKAKAEgAKILCGEGVDSLALPAGNQKGY 371
Cdd:cd07128 297 RAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAE-AEVVFGGPDRFEVVGADAEKGA 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024393110 372 FMLPTVI-AEIKDESCCMQE-EIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNvgrvHRVARRLQSGL 442
Cdd:cd07128 376 FFPPTLLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND----PAFARELVLGA 444
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
144-483 |
2.72e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 111.29 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 144 PVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAgMPHGVVNMVFGTGAKAGEALVCHPD 223
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 224 VplISFTGSTLTAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFA-NQGEICLCTSRIFVQRGIYSE 302
Cdd:PLN02174 191 K--IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYAPK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 303 FVKRFVAETKKWKVGNPSDpTVDVGALISKEHLEKVRSYVKKAKAEGAKILCGEgvdslalpaGNQKGYFMLPTVIAEIK 382
Cdd:PLN02174 269 VIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGE---------KDRENLKIAPTILLDVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 383 DESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNVGRVHRVARRLQSGLVWTNCWLVRDL--NLPFGGM 460
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTLPFGGV 418
|
330 340
....*....|....*....|...
gi 2024393110 461 KASGIGREGAKDSYEFFTEVKTI 483
Cdd:PLN02174 419 GESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
10-434 |
5.69e-26 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 110.95 E-value: 5.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 10 LENFIAGRFVPCS-SYIDSYNPSTGDVYCRVPDSG----------KEEVEAAVRAAKNAfpiwssksplEKSQILNKLAD 78
Cdd:PRK11903 5 LANYVAGRWQAGSgAGTPLFDPVTGEELVRVSATGldlaaafafaREQGGAALRALTYA----------QRAALLAAIVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 79 LIEHDLEAFAQAESKDQGKTITFArTVDIPRAVYNFRFFAS-----SILHHTTEcTEMASMG------CVHYTSRTPvGV 147
Cdd:PRK11903 75 VLQANRDAYYDIATANSGTTRNDS-AVDIDGGIFTLGYYAKlgaalGDARLLRD-GEAVQLGkdpafqGQHVLVPTR-GV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 148 AGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSemtSVTAWM---MCKLLEKAG-MPHGVVNMVFGTGAKAGEALvcHP- 222
Cdd:PRK11903 152 ALFINAFNFPAWGLWEKAAPALLAGVPVIVKPA---TATAWLtqrMVKDVVAAGiLPAGALSVVCGSSAGLLDHL--QPf 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 223 DVplISFTGSTLTAQRIteKSAP----HCKKLSLELGGKNPAIIFDDADLSQ-----CIPTTLRSSFANQGEICLCTSRI 293
Cdd:PRK11903 227 DV--VSFTGSAETAAVL--RSHPavvqRSVRVNVEADSLNSALLGPDAAPGSeafdlFVKEVVREMTVKSGQKCTAIRRI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 294 FVQRGIYSEFVKRFVAETKKWKVGNPSDPTVDVGALISKEHLEKVRSYVKKAKAEGAKILCGEGVDSLALPAGnqKGYFM 373
Cdd:PRK11903 303 FVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFALVDADPA--VAACV 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393110 374 LPTVI-AEIKDESCCMQE-EIFGPVTCVVAFDTEEEVVKRANGVKYGLAATVWSSNV--------------GRVHRV 434
Cdd:PRK11903 381 GPTLLgASDPDAATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAaflaaaaleladshGRVHVI 457
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
144-415 |
5.06e-11 |
|
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: 64.81 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 144 PVGVAGLISPWNLPlyllTWKIAPA----IACGNTVVAKPSEMTSVTAWMMCK----LLEKAGM-PHGVVNMVFGTGAKA 214
Cdd:cd07127 193 PRGVALVIGCSTFP----TWNGYPGlfasLATGNPVIVKPHPAAILPLAITVQvareVLAEAGFdPNLVTLAADTPEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 215 GEALVCHPDVPLISFTGSTLTAQRItEKSAPHcKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIF 294
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSNAFGDWL-EANARQ-AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIY 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 295 VQR-GI--------YSEFVKRFVAETKKWkVGNPSDPTVDVGALISkehlEKVRSYVKKAKAEGAKILCGEGVDSLALPa 365
Cdd:cd07127 347 VPRdGIqtddgrksFDEVAADLAAAIDGL-LADPARAAALLGAIQS----PDTLARIAEARQLGEVLLASEAVAHPEFP- 420
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2024393110 366 gnqKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRANGV 415
Cdd:cd07127 421 ---DARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARES 467
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
12-434 |
1.09e-10 |
|
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: 63.67 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 12 NFIAGRFVPCSSYIDSYNPSTGDVYCRVPDSGKEEVEAAVRAAK--------NAFpiwssKSP----------------L 67
Cdd:cd07126 1 NLVAGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRqcpksglhNPL-----KNPeryllygdvshrvaheL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 68 EKSQILNKLADLIEHDL-EAFAQAESKdqgktITFARtvdipRAVYNF-----RFFASSILHHTTECTEMASmgcvhyTS 141
Cdd:cd07126 76 RKPEVEDFFARLIQRVApKSDAQALGE-----VVVTR-----KFLENFagdqvRFLARSFNVPGDHQGQQSS------GY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 142 RTPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGaKAGEALVCH 221
Cdd:cd07126 140 RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDG-PTMNKILLE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 222 PDVPLISFTGStltaQRITEksaphckKLSLELGGKnpaIIFDDA---------DLS-------QCIpttlRSSFANQGE 285
Cdd:cd07126 219 ANPRMTLFTGS----SKVAE-------RLALELHGK---VKLEDAgfdwkilgpDVSdvdyvawQCD----QDAYACSGQ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 286 ICLCTSRIF-----VQRGIYSEFVKrfVAETKKWkvgnpSDPTvdVGALIS------KEHLEKVrsyvkkAKAEGAKILC 354
Cdd:cd07126 281 KCSAQSILFahenwVQAGILDKLKA--LAEQRKL-----EDLT--IGPVLTwtteriLDHVDKL------LAIPGAKVLF 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 355 -GEGVDSLALPAgnQKGYFmLPTVI----AEIKDESC--CMQEEIFGPVTCVVAFDTEEE--VVKRANGVKYGLAATVWS 425
Cdd:cd07126 346 gGKPLTNHSIPS--IYGAY-EPTAVfvplEEIAIEENfeLVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVS 422
|
....*....
gi 2024393110 426 SNVGRVHRV 434
Cdd:cd07126 423 NDIRFLQEV 431
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
53-322 |
1.14e-08 |
|
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: 56.85 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 53 AAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGKTITFARTVDIPR------AVYNFRFFASSI---LH 123
Cdd:cd07077 2 SAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMmgcsesKLYKNIDTERGItasVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 124 HTTECTEMASMGCvhYTSRTPVGVAGLISPWNLPLYLLTwKIAPAIACGNTVVAKPSEMTSVTAWMMCKLLEKAGMPHGV 203
Cdd:cd07077 82 HIQDVLLPDNGET--YVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 204 VNMVfGTGAKA----GEALVCHPDVPLISFTGSTlTAQRITEKSAPHckKLSLELGGKNPAIIFDDADLSQCIPTTLRSS 279
Cdd:cd07077 159 KILV-LYVPHPsdelAEELLSHPKIDLIVATGGR-DAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2024393110 280 FANQGEICLCTSRIFVQRGIYSEFVKRFVAETKKWKVGNPSDP 322
Cdd:cd07077 235 KFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQET 277
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
144-436 |
3.16e-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: 52.65 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 144 PVGVAGLISPWNLPLYLLTWKIAPAIACGNTVVAKP----SEMTSVTAWMMCKLLEKAGMPHGVVNMVFGTGAKAGEALV 219
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 220 CHPDVPLISFTGstltAQRITEKSAPHCKKLSLELGGKNPAIIFDDADLSQCIPTTLRSSFANQGEICLCTSRIFVQRGI 299
Cdd:cd07081 175 KFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 300 YSEFVKRFVAETkkwkvgnpsdptvdvGALISKEHLEKVRSYVKKAKAEGAKILcGEGVDSLALPAGnqkgyFMLPT--- 376
Cdd:cd07081 251 YDEVMRLFEGQG---------------AYKLTAEELQQVQPVILKNGDVNRDIV-GQDAYKIAAAAG-----LKVPQetr 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393110 377 -VIAEIK--DESCCMQEEIFGPVTCVVAFDTEEEVVKRANGVKY----GLAATVWSSNVGRVHRVAR 436
Cdd:cd07081 310 iLIGEVTslAEHEPFAHEKLSPVLAMYRAANFADADAKALALKLeggcGHTSAMYSDNIKAIENMNQ 376
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
144-356 |
3.40e-07 |
|
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: 52.49 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 144 PVGV-AGLI---SPWNLPLYlltwKIAPAIACGNTVVAKPSEMTSVTAWMMCKLL----EKAGMPHGVVNMVFGTGAKAG 215
Cdd:cd07122 95 PVGViAALIpstNPTSTAIF----KALIALKTRNAIIFSPHPRAKKCSIEAAKIMreaaVAAGAPEGLIQWIEEPSIELT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 216 EALVCHPDVPLISFTGSTltaqrITEKSAPHCKKLSLELG-GKNPAIIFDDADLSQCIPTTLRS-SFANqGEICLCTSRI 293
Cdd:cd07122 171 QELMKHPDVDLILATGGP-----GMVKAAYSSGKPAIGVGpGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQSV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 294 FVQRGIYSEFVKRFVAEtkkwkvGnpsdptvdvGALISKEHLEKVRSYV-------------KKAKA----------EGA 350
Cdd:cd07122 245 IVDDEIYDEVRAELKRR------G---------AYFLNEEEKEKLEKALfddggtlnpdivgKSAQKiaelagievpEDT 309
|
....*.
gi 2024393110 351 KILCGE 356
Cdd:cd07122 310 KVLVAE 315
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
45-439 |
3.12e-05 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 46.43 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 45 EEVEAAVRAAKNAFPIWSSKSPLEKSQILNKLADLIEHDLEAFAQAESKDQGktitFARTVDipravynfrffasSILHH 124
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETG----MGRVED-------------KIAKN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 125 T--------TEC--TEMAS----MGCVHYTsrtPVGVAGLISPWNLPLYLLTWKIAPAIACGNTVV------AKpsemtS 184
Cdd:PRK15398 99 VaaaektpgVEDltTEALTgdngLTLIEYA---PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVfsphpgAK-----K 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 185 VTAW---MMCKLLEKAGMPHGVVNMVFGTGAKAGEALVCHPDVPLISFTGST--LTAQRITEKSAphckklsLELGGKNP 259
Cdd:PRK15398 171 VSLRaieLLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPavVKAAMKSGKKA-------IGAGAGNP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 260 AIIFDDadlSQCIPTTLRS-----SFANQgEICLCTSRIFVQRGIYSEFVKRFVAEtkkwkvgnpsdptvdvGA-LISKE 333
Cdd:PRK15398 244 PVVVDE---TADIEKAARDivkgaSFDNN-LPCIAEKEVIVVDSVADELMRLMEKN----------------GAvLLTAE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393110 334 HLEKVRSYVKKAKAEGAKILCGEGVDSLALPAGnQKGYFMLPTVIAEIKDESCCMQEEIFGPVTCVVAFDTEEEVVKRAN 413
Cdd:PRK15398 304 QAEKLQKVVLKNGGTVNKKWVGKDAAKILEAAG-INVPKDTRLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAV 382
|
410 420
....*....|....*....|....*...
gi 2024393110 414 GVKYGL--AATVWSSNVGRVHRVARRLQ 439
Cdd:PRK15398 383 KLEHGNrhTAIMHSRNVDNLNKMARAIQ 410
|
|
| |
