|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
1-362 |
0e+00 |
|
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: 725.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07085 116 LKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07085 196 LNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAG 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMALSTAILVG-EAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGY 239
Cdd:cd07085 276 QRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGY 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 ENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd07085 356 ENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINV 435
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1039739590 320 PIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 362
Cdd:cd07085 436 PIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
1-362 |
0e+00 |
|
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: 692.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:TIGR01722 116 LKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:TIGR01722 196 LNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAG 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMALSTAILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYE 240
Cdd:TIGR01722 276 QRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 241 NGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVP 320
Cdd:TIGR01722 356 EGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVP 435
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1039739590 321 IPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 362
Cdd:TIGR01722 436 IPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
2-378 |
0e+00 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 533.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 2 LGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PLN02419 230 MGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 82 NIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:PLN02419 310 NIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQ 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTAILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYEN 241
Cdd:PLN02419 390 RCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 242 GNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPI 321
Cdd:PLN02419 470 GNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI 549
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039739590 322 PVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSspaVVMPT 378
Cdd:PLN02419 550 PVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQKDIHSPFS---LAIPI 603
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
1-358 |
1.32e-136 |
|
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: 397.67 E-value: 1.32e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:pfam00171 107 LDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:pfam00171 186 LNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 160 GQRCMALSTAILVGEAK-KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkG 238
Cdd:pfam00171 266 GQVCTATSRLLVHESIYdEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGGEA----G 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 YENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:pfam00171 342 LDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWIN 421
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1039739590 319 VPIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:pfam00171 422 DYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ... |
1-364 |
6.89e-117 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and conversion];
Pssm-ID: 223944 [Multi-domain] Cd Length: 472 Bit Score: 347.75 E-value: 6.89e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:COG1012 114 LEGETIPT-DKGSKALVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPSEQTPLSALALAELAAEAGLPAGV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:COG1012 193 LNVVTGGgAEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAANLKPVTLELGGKSPAIVLEDADLDAAVDAAVFGAFFNA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 160 GQRCMALSTAILVGEAK-KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkg 238
Cdd:COG1012 273 GQRCTAASRLIVHESVYdEFVERLVARAASLKVGDPLDPSTDLGPLISEEQLDRVEGYIEDAVAEGARLLAGGKR----- 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 yENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:COG1012 348 -PGGYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIELANDTEYGLAAAIFTRDLARAFRVARRLEAGMVGIN 426
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1039739590 319 VPIP-VPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTITSQWKE 364
Cdd:COG1012 427 DYTGgADIAYLPFGGVKQS--GLGREGGKYGLEEFTEVKTVTIKLGP 471
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
1-359 |
4.33e-110 |
|
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: 328.78 E-value: 4.33e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07078 76 LHGEVIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:cd07078 156 LNVVTGdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 160 GQRCMALStAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIkvk 237
Cdd:cd07078 236 GQVCTAAS-RLLVHEsiYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRL--- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 238 GYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGV 317
Cdd:cd07078 312 EGGKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWI 391
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1039739590 318 NVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07078 392 NDYSVGAEPSAPFGGVKQS--GIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
1-359 |
4.65e-105 |
|
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 Cd Length: 478 Bit Score: 317.75 E-value: 4.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07131 115 LFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:cd07131 195 VNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTT 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 160 GQRCMALSTAIL-VGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG 238
Cdd:cd07131 275 GQRCTATSRLIVhESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 YENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07131 355 YEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN 434
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039739590 319 VPI---PVPLPmF-----SFTGSRSSfrgdtnfyGKQGIQFYTQLKTIT 359
Cdd:cd07131 435 APTigaEVHLP-FggvkkSGNGHREA--------GTTALDAFTEWKAVY 474
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
3-358 |
1.61e-92 |
|
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 Cd Length: 473 Bit Score: 285.30 E-value: 1.61e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07097 117 GETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07097 197 LVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTAILV-GEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKvkGYE 240
Cdd:cd07097 277 RCTASSRLIVTeGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLK--RPD 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 241 NGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVP 320
Cdd:cd07097 355 EGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLP 434
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1039739590 321 -----IPVPlpmfsFTGSRSSFRGdtnfYGKQG---IQFYTQLKTI 358
Cdd:cd07097 435 tagvdYHVP-----FGGRKGSSYG----PREQGeaaLEFYTTIKTV 471
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
3-320 |
1.70e-90 |
|
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: 280.22 E-value: 1.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----GATMLLAKLLQDSGAPD 78
Cdd:cd07086 115 GLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPltaiAVTKILAEVLEKNGLPP 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 79 GTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07086 195 GVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGT 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMALSTAIL-VGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIkvK 237
Cdd:cd07086 275 AGQRCTTTRRLIVhESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRI--D 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 238 GYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKY--AHMVDVGQV 315
Cdd:cd07086 353 GGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIV 432
|
....*
gi 1039739590 316 GVNVP 320
Cdd:cd07086 433 NVNIP 437
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
3-359 |
1.04e-87 |
|
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: 272.13 E-value: 1.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07093 100 GESYPQDGGALN-YVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07093 179 VVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMAlSTAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGY 239
Cdd:cd07093 259 VCLA-GSRILVQRsiYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATILTGGGRPELPDL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 ENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd07093 338 EGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNC 417
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1039739590 320 PIPVPLPMfSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07093 418 WLVRDLRT-PFGGVKAS--GIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
3-358 |
2.04e-81 |
|
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: 256.32 E-value: 2.04e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07114 101 GAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07114 181 VVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQ 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGY 239
Cdd:cd07114 261 TCVAGSR-LLVQRsiYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSGADL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 ENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd07114 340 GAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT 419
|
330 340 350
....*....|....*....|....*....|....*....
gi 1039739590 320 PIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07114 420 YRALS-PSSPFGGFKDSGIGREN--GIEAIREYTQTKSV 455
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
1-359 |
4.36e-79 |
|
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: 247.14 E-value: 4.36e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd06534 72 LGGPELPSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAA 159
Cdd:cd06534 152 VNVVPGgGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 160 GQRCMALSTaILVGEAKKwlPELVDRAKnlrvnagdqpgadlgplitpqakervcnlidsgtkegasilldgrrikvkgy 239
Cdd:cd06534 232 GQICTAASR-LLVHESIY--DEFVEKLV---------------------------------------------------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 engnfvgpTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd06534 257 --------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYIND 328
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1039739590 320 PIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd06534 329 SSIGVGPEAPFGGVKNSGIGREG--GPYGLEEYTRTKTVV 366
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
3-359 |
4.65e-78 |
|
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: 247.35 E-value: 4.65e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:cd07103 99 GRTIPSPAPGKRILVIKQPVGVVAAITPWNFPaAMITRKIAP-ALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 82 NIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAknHG--VVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07103 178 NVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG--NApfIVFDDADLDKAVDGAIASKFRN 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMAlSTAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKV 236
Cdd:cd07103 256 AGQTCVC-ANRIYVHEsiYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKGAKVLTGGKRLGL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 237 KGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVG 316
Cdd:cd07103 335 GGY----FYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVG 410
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1039739590 317 VNVPIPvPLPMFSFTGSRSSfrGdtnfYG----KQGIQFYTQLKTIT 359
Cdd:cd07103 411 INTGLI-SDAEAPFGGVKES--G----LGreggKEGLEEYLETKYVS 450
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
1-359 |
3.73e-77 |
|
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: 244.36 E-value: 3.73e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKLLQDSGAPDG 79
Cdd:cd07104 78 PEGEILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 80 TLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07104 158 VLNVVPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLH 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRi 234
Cdd:cd07104 238 QGQICMAAGR-ILVHEsvYDEFVEKLVAKAKALPV--GDPrdPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 235 kvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQ 314
Cdd:cd07104 314 ------EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGM 387
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1039739590 315 VGVNVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07104 388 VHINDQTVNDEPHVPFGGVKAS--GGGRFGGPASLEEFTEWQWIT 430
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
3-318 |
1.34e-75 |
|
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: 241.83 E-value: 1.34e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07119 117 GEVYDV-PPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVN 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07119 196 LVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQ 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGY 239
Cdd:cd07119 276 VCSAGSR-LLVEEsiHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDEL 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039739590 240 ENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07119 355 AKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN 433
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
3-359 |
1.98e-74 |
|
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: 238.65 E-value: 1.98e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07091 124 GKTIPIDGNFLA-YTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVN 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07091 203 IVPGFgPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQG 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG 238
Cdd:cd07091 283 QCCCAGSR-IFVQESiyDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 YengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07091 362 Y----FIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN 437
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1039739590 319 VpIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07091 438 T-YNVFDAAVPFGGFKQSGFGREL--GEEGLEEYTQVKAVT 475
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
16-358 |
8.25e-73 |
|
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: 233.74 E-value: 8.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFIC 95
Cdd:cd07090 111 YTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGGETGQLLC 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 96 DHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVGEA 175
Cdd:cd07090 191 EHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSN-GTRVFVQRS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 --KKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVK-GYENGNFVGPTII 250
Cdd:cd07090 270 ikDEFTERLVERTKKIRI--GDplDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLCGGERVVPEdGLENGFYVSPCVL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 251 SNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN----VPIPVPlp 326
Cdd:cd07090 348 TDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINtyniSPVEVP-- 425
|
330 340 350
....*....|....*....|....*....|..
gi 1039739590 327 mfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07090 426 ---FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
1-359 |
1.06e-72 |
|
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: 233.38 E-value: 1.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07118 99 LHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNqlvGAAFGA- 158
Cdd:cd07118 179 VNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAAD---AVVFGVy 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 --AGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGR 232
Cdd:cd07118 256 fnAGECCNSGSR-LLVHEsiADAFVAAVVARSRKVRV--GDplDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 233 RIkvkGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDV 312
Cdd:cd07118 333 RL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRA 409
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039739590 313 GQVGVNVPIP--VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07118 410 GTVWVNTFLDgsPELP---FGGFKQSGIGREL--GRYGVEEYTELKTVH 453
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
3-358 |
1.36e-72 |
|
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: 233.70 E-value: 1.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:cd07088 115 GEIIPSDRPNENIFIFKVPIGVVAGILPWNFPfFLIARKLAP-ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 82 NIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07088 194 NIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMAlSTAILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKV 236
Cdd:cd07088 274 QVCTC-AERVYVHEdiYDEFMEKLVEKMKAVKV--GDpfDAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 237 kgyENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVG 316
Cdd:cd07088 351 ---EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETY 427
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1039739590 317 VNVPIPVPLPMFSfTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07088 428 INRENFEAMQGFH-AGWKKSGLGGAD--GKHGLEEYLQTKVV 466
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
19-359 |
6.18e-72 |
|
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: 232.01 E-value: 6.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 19 RLPLGVCAGIAPFNFPA-MIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICD 96
Cdd:cd07138 128 REPIGVCGLITPWNWPLnQIVLKVAP-ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 97 HPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAILVGEAK 176
Cdd:cd07138 207 HPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAP-TRMLVPRSR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 177 kwLPELVDRAK----NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASiLLDGRRIKVKGYENGNFVGPTIISN 252
Cdd:cd07138 286 --YAEAEEIAAaaaeAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGAR-LVAGGPGRPEGLERGYFVKPTVFAD 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 253 VKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVPL-PmfsFT 331
Cdd:cd07138 363 VTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGaP---FG 439
|
330 340
....*....|....*....|....*...
gi 1039739590 332 GSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07138 440 GYKQS--GNGREWGRYGLEEFLEVKSIQ 465
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
3-356 |
1.15e-71 |
|
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: 231.24 E-value: 1.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDmDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:TIGR01804 116 GEIIPLGGPS-FAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:TIGR01804 195 VVQGDGAEVgPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQ 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTAILVGEAK-KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYE 240
Cdd:TIGR01804 275 VCSNGTRVFVHKKIKeRFLARLVERTERIKLGDPFDEATEMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 241 NGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV- 319
Cdd:TIGR01804 355 NGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTy 434
|
330 340 350
....*....|....*....|....*....|....*...
gi 1039739590 320 -PIPVPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLK 356
Cdd:TIGR01804 435 nLYPAEAP---FGGYKQSGIGREN--GKAALAHYTEVK 467
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
3-359 |
1.70e-71 |
|
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: 229.77 E-value: 1.70e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07105 80 GGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHGQ----HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07105 160 VVTHSpedaPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMalSTA-ILVGE--AKKWLPELVDRAKNLRvnagdQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRik 235
Cdd:cd07105 240 SGQICM--STErIIVHEsiADEFVEKLKAAAEKLF-----AGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLA-- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 236 vKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQV 315
Cdd:cd07105 311 -DESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAV 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1039739590 316 GVNVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07105 390 HINGMTVHDEPTLPHGGVKSS--GYGRFNGKWGIDEFTETKWIT 431
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
3-358 |
2.25e-71 |
|
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: 230.02 E-value: 2.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07115 100 GEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07115 179 VVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQ 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGY 239
Cdd:cd07115 259 MCTAGSR-LLVHEsiYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLTGGKRPGARGF 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 engnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd07115 338 ----FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINT 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1039739590 320 pipvplpmFSFTGSRSSFRG--DTNF---YGKQGIQFYTQLKTI 358
Cdd:cd07115 414 --------YNRFDPGSPFGGykQSGFgreMGREALDEYTEVKSV 449
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
19-358 |
3.28e-71 |
|
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: 229.34 E-value: 3.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHDAVNFICDHP 98
Cdd:cd07106 112 RKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHP 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 99 DIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA--K 176
Cdd:cd07106 191 DIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKR-LYVHESiyD 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 177 KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPS 256
Cdd:cd07106 270 EFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLDGPGY----FIPPTIVDDPPEG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 257 MTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNvPIPVPLPMFSFTGSRSS 336
Cdd:cd07106 346 SRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN-THGALDPDAPFGGHKQS 424
|
330 340
....*....|....*....|..
gi 1039739590 337 FRGDTnfYGKQGIQFYTQLKTI 358
Cdd:cd07106 425 GIGVE--FGIEGLKEYTQTQVI 444
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
16-359 |
7.16e-71 |
|
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: 230.57 E-value: 7.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 16 YSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFI 94
Cdd:cd07124 162 YVYR-PLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 95 CDHPDIKAISFVGSNQAGEYIFER------GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALST 168
Cdd:cd07124 241 VEHPDVRFIAFTGSREVGLRIYERaakvqpGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSR 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 169 AILVGEA-KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRRIKVKgyENGNFVGP 247
Cdd:cd07124 321 VIVHESVyDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELA--AEGYFVQP 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 248 TIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVPLPM 327
Cdd:cd07124 398 TIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVG 477
|
330 340 350
....*....|....*....|....*....|....*...
gi 1039739590 328 F-SFTGSRSSfrGDTnfyGKQG-----IQFyTQLKTIT 359
Cdd:cd07124 478 RqPFGGFKMS--GTG---SKAGgpdylLQF-MQPKTVT 509
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
3-359 |
8.86e-71 |
|
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: 228.37 E-value: 8.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07150 101 GETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANkentLNQLVG-AAFGA-- 158
Cdd:cd07150 181 VVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD----LDYAVRaAAFGAfm 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 -AGQRCMAlSTAILVGEA--KKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILldgrr 233
Cdd:cd07150 257 hQGQICMS-ASRIIVEEPvyDEFVKKFVARASKLKV--GDprDPDTVIGPLISPRQVERIKRQVEDAVAKGAKLL----- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 234 ikVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVG 313
Cdd:cd07150 329 --TGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESG 406
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1039739590 314 QVGVNVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07150 407 MVHINDPTILDEAHVPFGGVKAS--GFGREGGEWSMEEFTELKWIT 450
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
3-359 |
7.69e-69 |
|
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: 224.15 E-value: 7.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSitkDMDLYSY-RL-PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07141 128 GKTIPM---DGDFFTYtRHePVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGV 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFER-GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07141 205 VNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAaGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFN 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKV 236
Cdd:cd07141 285 MGQCCCA-GSRTFVQESiyDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGD 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 237 KGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVG 316
Cdd:cd07141 364 KGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVW 439
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1039739590 317 VNVPIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07141 440 VNCYNVVS-PQAPFGGYKMSGNGREL--GEYGLQEYTEVKTVT 479
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
19-359 |
7.61e-68 |
|
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: 221.29 E-value: 7.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHP 98
Cdd:cd07139 135 REPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHP 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 99 DIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAILVGEAKK- 177
Cdd:cd07139 215 GVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVAL-TRILVPRSRYd 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 178 -WLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikVKGYENGNFVGPTIISNVKPS 256
Cdd:cd07139 294 eVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDND 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 257 MTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVP-LPmfsFTGSRS 335
Cdd:cd07139 372 MRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFgAP---FGGFKQ 448
|
330 340
....*....|....*....|....
gi 1039739590 336 SfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07139 449 S--GIGREGGPEGLDAYLETKSIY 470
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
3-360 |
1.73e-67 |
|
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: 219.89 E-value: 1.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKdmdlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDsGAPDGTLN 82
Cdd:cd07092 104 GEYLPGHTS----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAE-VLPPGVVN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07092 179 VVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQ 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDsGTKEGASILLDGRRIKVKGY 239
Cdd:cd07092 259 DCTA-ACRVYVHESvyDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE-RAPAHARVLTGGRRAEGPGY 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 engnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:cd07092 337 ----FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT 412
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1039739590 320 PIPVPLPMfSFTGSRSSfrGdtnfYGKQ----GIQFYTQLKTITS 360
Cdd:cd07092 413 HIPLAAEM-PHGGFKQS--G----YGKDlsiyALEDYTRIKHVMV 450
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
16-359 |
3.30e-67 |
|
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: 219.39 E-value: 3.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFI 94
Cdd:cd07149 118 FTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVgDAL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 95 CDHPDIKAISFVGSNQAGEYIFERGsrnG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVG 173
Cdd:cd07149 198 VTDPRVRMISFTGSPAVGEAIARKA---GlKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQR-IFVH 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 EAKK--WLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkgyeNGNFVGPTI 249
Cdd:cd07149 274 EDIYdeFLERFVAATKKLVV--GDplDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLTGGKR-------DGAILEPTV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 250 ISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPipvplpmfs 329
Cdd:cd07149 345 LTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDS--------- 415
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1039739590 330 ftgsrSSFRGDTNFYG--------KQGIQF----YTQLKTIT 359
Cdd:cd07149 416 -----STFRVDHMPYGgvkesgtgREGPRYaieeMTEIKLVC 452
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
3-318 |
5.39e-67 |
|
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: 218.76 E-value: 5.39e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPD 78
Cdd:cd07145 101 GETIPVdayeYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 79 GTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFG 157
Cdd:cd07145 181 GVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 158 AAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRR 233
Cdd:cd07145 261 NAGQVCNAVKR-ILVEEevYDKFLKLLVEKVKKLKV--GDplDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGGKR 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 234 IKvkgyenGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVG 313
Cdd:cd07145 338 DE------GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAG 411
|
....*
gi 1039739590 314 QVGVN 318
Cdd:cd07145 412 GVVIN 416
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
3-359 |
8.06e-67 |
|
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: 218.26 E-value: 8.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:cd07109 100 GETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07109 179 VVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQ 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTaILVGEA--KKWLPELVDRAKNLRVNAG-DQPgaDLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKg 238
Cdd:cd07109 259 TCSAGSR-LLVHRSiyDEVLERLVERFRALRVGPGlEDP--DLGPLISAKQLDRVEGFVARARARGARIVAGGRIAEGA- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 YENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07109 335 PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVN 414
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1039739590 319 VPIP---VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07109 415 NYGAgggIELP---FGGVKKSGHGREK--GLEALYNYTQTKTVA 453
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
5-359 |
4.33e-66 |
|
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: 216.45 E-value: 4.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 5 TMPSitKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNII 84
Cdd:cd07110 106 PLPS--EDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 85 HGQHDAVNF-ICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRC 163
Cdd:cd07110 184 TGTGDEAGApLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQIC 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 164 MALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikVKGYEN 241
Cdd:cd07110 264 SATSR-LLVHEsiADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGARLLCGGRR--PAHLEK 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 242 GNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPI 321
Cdd:cd07110 341 GYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCSQ 420
|
330 340 350
....*....|....*....|....*....|....*....
gi 1039739590 322 PVpLPMFSFTG-SRSSFRGDtnfYGKQGIQFYTQLKTIT 359
Cdd:cd07110 421 PC-FPQAPWGGyKRSGIGRE---LGEWGLDNYLEVKQIT 455
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
16-358 |
6.62e-66 |
|
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: 216.63 E-value: 6.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFI 94
Cdd:cd07143 139 YTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAI 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 95 CDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVG 173
Cdd:cd07143 219 SSHMDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCA-GSRIYVQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 EA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIIS 251
Cdd:cd07143 298 EGiyDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY----FIEPTIFT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 252 NVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVPlPMFSFT 331
Cdd:cd07143 374 DVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLH-HQVPFG 452
|
330 340
....*....|....*....|....*..
gi 1039739590 332 GSRSSFRGDTnfYGKQGIQFYTQLKTI 358
Cdd:cd07143 453 GYKQSGIGRE--LGEYALENYTQIKAV 477
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
18-318 |
9.85e-66 |
|
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: 215.90 E-value: 9.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 18 YRLPLGVCAGIAPFNFP------AMIPlwmfpmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HDA 90
Cdd:cd07082 138 RREPLGVVLAIGPFNYPlnltvsKLIP------ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 91 VNFICDHPDIKAISFVGSNQAGEYIFERGSRngKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaI 170
Cdd:cd07082 212 GDPLVTHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-V 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 171 LVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkgyENGNFVGPT 248
Cdd:cd07082 289 LVHEsvADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR------EGGNLIYPT 362
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 249 IISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07082 363 LLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN 432
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
3-359 |
3.31e-65 |
|
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: 214.61 E-value: 3.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETM-PSIT----KDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPgATML-LAKLLQDSGA 76
Cdd:cd07113 119 GETLaPSIPsmqgERYTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTP-LTLLrVAELAKEAGI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 77 PDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAF 156
Cdd:cd07113 198 PDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGF 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 157 GAAGQRCmALSTAILVGEAKkwLPELVD----RAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGR 232
Cdd:cd07113 278 LHQGQVC-AAPERFYVHRSK--FDELVTklkqALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 233 RIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDV 312
Cdd:cd07113 355 ALAGEGY----FVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEA 430
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1039739590 313 GQVGVNVPIPVPlPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTIT 359
Cdd:cd07113 431 GTVWVNMHTFLD-PAVPFGGMKQSGIGRE--FGSAFIDDYTELKSVM 474
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
1-358 |
4.21e-65 |
|
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: 214.58 E-value: 4.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07144 125 IQGKTIPTSPNKL-AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHGqHDAV--NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07144 204 VNIIPG-YGAVagSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYN 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMALSTaILVGEA--KKWLPELVDRAK-NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRiK 235
Cdd:cd07144 283 SGQNCTATSR-IYVQESiyDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK-A 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 236 VKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQV 315
Cdd:cd07144 361 PEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMV 440
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1039739590 316 GVNVP----IPVPlpmfsFTGSRSSfrGDTNFYGKQGIQFYTQLKTI 358
Cdd:cd07144 441 WINSSndsdVGVP-----FGGFKMS--GIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
19-358 |
4.98e-65 |
|
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: 213.64 E-value: 4.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDH 97
Cdd:cd07089 121 REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVgEALTTD 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 98 PDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANkentLNQLVGAAFG----AAGQRCmALSTAILVG 173
Cdd:cd07089 201 PRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDAD----LAAAAPAAVGvcmhNAGQGC-ALTTRLLVP 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 EAKKwlPELVDRAKN----LRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikVKGYENGNFVGPTI 249
Cdd:cd07089 276 RSRY--DEVVEALAAafeaLPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGR--PAGLDKGFYVEPTL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 250 ISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN----VPIPVPl 325
Cdd:cd07089 352 FADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINggggYGPDAP- 430
|
330 340 350
....*....|....*....|....*....|...
gi 1039739590 326 pmfsFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 358
Cdd:cd07089 431 ----FGGYKQSGLGRE--NGIEGLEEFLETKSI 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
1-358 |
1.77e-64 |
|
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: 212.46 E-value: 1.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07112 105 VYGEVAPTGPDALALIT-REPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDA-NKENTLNQLVGAAFG 157
Cdd:cd07112 184 LNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFW 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 158 AAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRR 233
Cdd:cd07112 264 NQGEVCSAGSR-LLVHEsiKDEFLEKVVAAAREWKP--GDplDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKR 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 234 IKVKGyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVG 313
Cdd:cd07112 341 VLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAG 418
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039739590 314 QVGVN----VPIPVPlpmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07112 419 TVWVNcfdeGDITTP-----FGGFKQSGNGRDK--SLHALDKYTELKTT 460
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
2-362 |
2.03e-63 |
|
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: 209.07 E-value: 2.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 2 LGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKLLQDSGAPDGT 80
Cdd:cd07152 92 QGEILPSAPGRLS-LARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:cd07152 171 LHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMAlSTAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkg 238
Cdd:cd07152 251 QICMA-AGRHLVHEsvADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTY----- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 yeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07152 325 --DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHIN 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1039739590 319 VPIPVPLPMFSFTGSRSSFRGdTNFYGKQGIQFYTQlktitSQW 362
Cdd:cd07152 403 DQTVNDEPHNPFGGMGASGNG-SRFGGPANWEEFTQ-----WQW 440
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
3-356 |
1.00e-61 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 206.08 E-value: 1.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PLN02278 142 GDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITRKVGP-ALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 82 NIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:PLN02278 221 NVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG 238
Cdd:PLN02278 301 QTCVC-ANRILVQEGiyDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGG 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 yengNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PLN02278 380 ----TFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVN 455
|
330 340 350
....*....|....*....|....*....|....*...
gi 1039739590 319 VPIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 356
Cdd:PLN02278 456 EGL-ISTEVAPFGGVKQSGLGREG--SKYGIDEYLEIK 490
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
19-318 |
1.19e-61 |
|
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: 203.85 E-value: 1.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 19 RLPLGVCAGIAPFNFPamipLW-MF----PMAMVcGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNF 93
Cdd:cd07100 94 YEPLGVVLGIMPWNFP----FWqVFrfaaPNLMA-GNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 94 ICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVG 173
Cdd:cd07100 169 IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIA-AKRFIVH 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 E--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTI 249
Cdd:cd07100 248 EdvYDEFLEKFVEAMAALKV--GDpmDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGA----FYPPTV 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039739590 250 ISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07100 322 LTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
16-359 |
1.34e-61 |
|
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: 204.51 E-value: 1.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HDAVNFI 94
Cdd:cd07146 115 FTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDEL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 95 CDHPDIKAISFVGSNQAGEYIfeRGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGE 174
Cdd:cd07146 195 ITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKR-ILVHE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 175 --AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkgyeNGNFVGPTII 250
Cdd:cd07146 272 svADEFVDLLVEKSAALVV--GDpmDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGNQR-------QGALYAPTVL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 251 SNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNvpiPVP---LPM 327
Cdd:cd07146 343 DHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVN---EVPgfrSEL 419
|
330 340 350
....*....|....*....|....*....|....*.
gi 1039739590 328 FSFTGSRSSFRGdtnfyGKQGIQ----FYTQLKTIT 359
Cdd:cd07146 420 SPFGGVKDSGLG-----GKEGVReamkEMTNVKTYS 450
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
1-361 |
2.33e-61 |
|
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: 204.46 E-value: 2.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP--GATmLLAKLLQDSGAPD 78
Cdd:cd07151 110 MEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPitGGL-LLAKIFEEAGLPK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 79 GTLNIIHGqhdAVNFICD----HPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGA 154
Cdd:cd07151 189 GVLNVVVG---AGSEIGDafveHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 155 AFGAAGQRCMALSTaILVGEA--KKWLPELVDRAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDSGTKEGASILLD 230
Cdd:cd07151 266 KFLHQGQICMAINR-IIVHEDvyDEFVEKFVERVKALPY--GDPsdPDTVVGPLINESQVDGLLDKIEQAVEEGATLLVG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 231 GRRikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMV 310
Cdd:cd07151 343 GEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRI 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039739590 311 DVGQVGVNvPIPV-PLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTITSQ 361
Cdd:cd07151 416 DAGMTHIN-DQPVnDEPHVPFGGEKNS--GLGRFNGEWALEEFTTDKWISVQ 464
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
16-318 |
3.75e-61 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 204.78 E-value: 3.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 16 YSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFI 94
Cdd:PRK03137 167 YFYI-PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 95 CDHPDIKAISFVGSNQAGEYIFER------GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALST 168
Cdd:PRK03137 246 VDHPKTRFITFTGSREVGLRIYERaakvqpGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSR 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 169 AILVGEA-KKWLPELVDRAKNLRVNAGDQPgADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRRIKVKGYengnFVGP 247
Cdd:PRK03137 326 AIVHEDVyDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGY----FIQP 399
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039739590 248 TIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PRK03137 400 TIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN 470
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
1-318 |
4.43e-61 |
|
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: 203.38 E-value: 4.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGT 80
Cdd:cd07107 97 LKGETIPVGGRNL-HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREV-LPPGV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLV-GAAFGA 158
Cdd:cd07107 175 FNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVaGMNFTW 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMALSTAiLVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKV 236
Cdd:cd07107 255 CGQSCGSTSRL-FVHESiyDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLVTGGGRPEG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 237 KGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVG 316
Cdd:cd07107 334 PALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVW 413
|
..
gi 1039739590 317 VN 318
Cdd:cd07107 414 IN 415
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
3-359 |
5.46e-61 |
|
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: 203.05 E-value: 5.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPD 78
Cdd:cd07094 101 GEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 79 GTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSrnGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFG 157
Cdd:cd07094 181 GVLQVVTGErEVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVDRDADLDAAIEALAKGGFY 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 158 AAGQRCMALSTAILVGE-AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikv 236
Cdd:cd07094 259 HAGQVCISVQRIYVHEElYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEAGARLLCGGER--- 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 237 kgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVG 316
Cdd:cd07094 336 ----DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVM 411
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1039739590 317 VNVPIPVPLPMFSFTGSRSSfrgdtnFYGKQGIQF----YTQLKTIT 359
Cdd:cd07094 412 VNDSSAFRTDWMPFGGVKES------GVGREGVPYameeMTEEKTVV 452
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
3-359 |
6.57e-61 |
|
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: 202.98 E-value: 6.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLN 82
Cdd:cd07108 100 GETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQV-LPAGVLN 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHGQHDAVNF-ICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLV-GAAFGAAG 160
Cdd:cd07108 178 VITGYGEECGAaLVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIaGMRFTRQG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMAlSTAILVGEA--KKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKE-GASILLDGRRIK 235
Cdd:cd07108 258 QSCTA-GSRLFVHEDiyDAFLEKLVAKLSKLKI--GDplDEATDIGAIISEKQFAKVCGYIDLGLSTsGATVLRGGPLPG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 236 VKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQV 315
Cdd:cd07108 335 EGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWV 414
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1039739590 316 GVNVPIpVPLPMFSFTGSRSSFRGDTnfYGKQG-IQFYTQLKTIT 359
Cdd:cd07108 415 QVNQGG-GQQPGQSYGGFKQSGLGRE--ASLEGmLEHFTQKKTVN 456
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
18-359 |
1.25e-58 |
|
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: 196.67 E-value: 1.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 18 YRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDH 97
Cdd:cd07099 116 EYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 98 PdIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA-- 175
Cdd:cd07099 196 G-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVER-VYVHESvy 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGyengNFVGPTIISNVKP 255
Cdd:cd07099 274 DEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGARSNGGG----PFYEPTVLTDVPH 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 256 SMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN-VPIPVPLPMFSFTGSR 334
Cdd:cd07099 350 DMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINdVLLTAGIPALPFGGVK 429
|
330 340
....*....|....*....|....*
gi 1039739590 335 SSfrGDTNFYGKQGIQFYTQLKTIT 359
Cdd:cd07099 430 DS--GGGRRHGAEGLREFCRPKAIA 452
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
3-363 |
1.23e-57 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 193.03 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPA-MIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PRK10090 53 GEIIQSDRPGENILLFKRALGVTTGILPWNFPFfLIARKMAP-ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 82 NIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:PRK10090 132 NLVLGRGETVgQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRC-MALSTAILVGEAKKWLPELVDRAKNLRV-NAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG 238
Cdd:PRK10090 212 QVCnCAERVYVQKGIYDQFVNRLGEAMQAVQFgNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 YengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PRK10090 292 Y----YYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039739590 319 vpipvplpmfsftgsRSSFRGDTNFY------------GKQGIQFYTQLKTITSQWK 363
Cdd:PRK10090 368 ---------------RENFEAMQGFHagwrksgiggadGKHGLHEYLQTQVVYLQSD 409
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
16-358 |
1.54e-57 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 194.71 E-value: 1.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFIC 95
Cdd:PRK13252 137 YTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 96 DHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVGEA 175
Cdd:PRK13252 217 EHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTN-GTRVFVQKS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 KK--WLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYENGNFVGPTIIS 251
Cdd:PRK13252 296 IKaaFEARLLERVERIRI--GDpmDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 252 NVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV--PIPVPLPmfs 329
Cdd:PRK13252 374 DCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPAEMP--- 450
|
330 340
....*....|....*....|....*....
gi 1039739590 330 FTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:PRK13252 451 VGGYKQSGIGREN--GIATLEHYTQIKSV 477
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
3-358 |
1.63e-56 |
|
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: 191.94 E-value: 1.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSitkDMDLYSYRL--PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07142 124 GMTLPA---DGPHHVYTLhePIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGV 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHGQHDAVNF-ICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 158
Cdd:cd07142 201 LNIVTGFGPTAGAaIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 159 AGQRCMAlSTAILVGEakKWLPELVDRAKN--LRVNAGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRI 234
Cdd:cd07142 281 QGQCCCA-GSRTFVHE--SIYDEFVEKAKAraLKRVVGDpfRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRI 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 235 KVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQ 314
Cdd:cd07142 358 GSKGY----YIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGT 433
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1039739590 315 VGVNVpIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 358
Cdd:cd07142 434 VWVNC-YDVFDASIPFGGYKMSGIGREK--GIYALNNYLQVKAV 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
12-358 |
1.75e-56 |
|
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: 191.79 E-value: 1.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 12 DMDLYSYRL--PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQ-H 88
Cdd:cd07559 125 DEDTLSYHFhePLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFgS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 89 DAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKE--NTLNQLVGAAFGAA---GQRC 163
Cdd:cd07559 204 EAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAMDAddDFDDKAEEGQLGFAfnqGEVC 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 164 MALSTAiLVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYEN 241
Cdd:cd07559 284 TCPSRA-LVQESiyDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDK 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 242 GNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV-- 319
Cdd:cd07559 363 GYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCyh 442
|
330 340 350
....*....|....*....|....*....|....*....
gi 1039739590 320 PIPVPLPmfsFTGSRSSFRGDTNFygKQGIQFYTQLKTI 358
Cdd:cd07559 443 QYPAHAP---FGGYKKSGIGRETH--KMMLDHYQQTKNI 476
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
19-345 |
1.79e-55 |
|
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: 188.61 E-value: 1.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHP 98
Cdd:cd07147 121 RFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 99 DIKAISFVGSNQAGEYIFERGSRngKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA--K 176
Cdd:cd07147 201 RIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQR-VLVHRSvyD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 177 KWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkgyeNGNFVGPTIISNVK 254
Cdd:cd07147 278 EFKSRLVARVKALKT--GDpkDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVP 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 255 PSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN-VPipvplpmfsftgs 333
Cdd:cd07147 349 PDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdVP------------- 415
|
330
....*....|..
gi 1039739590 334 rsSFRGDTNFYG 345
Cdd:cd07147 416 --TFRVDHMPYG 425
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
19-322 |
1.83e-55 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 188.96 E-value: 1.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHDAV-NFICDH 97
Cdd:PRK13473 136 RDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGH 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 98 PDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVGEA-- 175
Cdd:PRK13473 215 PKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTA-ACRIYAQRGiy 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEG-ASILLDGRRIKVKGYengnFVGPTIISNVK 254
Cdd:PRK13473 294 DDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGY----YYEPTLLAGAR 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039739590 255 PSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIP 322
Cdd:PRK13473 370 QDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM 437
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
21-318 |
3.86e-55 |
|
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: 188.37 E-value: 3.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDI 100
Cdd:cd07111 147 PVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 101 KAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGE--AKKW 178
Cdd:cd07111 227 DKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSR-LLVQEsvAEEL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 179 LPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPSMT 258
Cdd:cd07111 306 IRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGP----FYPPTLFTNVPPASR 381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 259 CYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07111 382 IAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWIN 441
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
19-358 |
5.84e-54 |
|
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: 184.97 E-value: 5.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQ-HDAVNFICDH 97
Cdd:cd07117 134 REPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKgSKSGEYLLNH 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 98 PDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA-- 175
Cdd:cd07117 213 PGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSR-IFVQEGiy 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYENGNFVGPTIISNVKP 255
Cdd:cd07117 292 DEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTN 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 256 SMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV--PIPVPLPmfsFTGS 333
Cdd:cd07117 372 DMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTynQIPAGAP---FGGY 448
|
330 340
....*....|....*....|....*
gi 1039739590 334 RSSFRGDTNFygKQGIQFYTQLKTI 358
Cdd:cd07117 449 KKSGIGRETH--KSMLDAYTQMKNI 471
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
3-358 |
1.59e-53 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 184.33 E-value: 1.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:PRK09847 140 GEVATTSSHELAMIV-REPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLN 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIF-ERGSRNGKRVQANMGAKNHGVVMPDANKentLNQLVGAA----F 156
Cdd:PRK09847 219 VVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLkDAGDSNMKRVWLEAGGKSANIVFADCPD---LQQAASATaagiF 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 157 GAAGQRCMAlSTAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRRI 234
Cdd:PRK09847 296 YNQGQVCIA-GTRLLLEEsiADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 235 KVKGYengnfVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQ 314
Cdd:PRK09847 374 GLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGS 448
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039739590 315 VGVNV----PIPVPlpmfsFTGSRSSFRG-DTNFYgkqGIQFYTQLKTI 358
Cdd:PRK09847 449 VFVNNyndgDMTVP-----FGGYKQSGNGrDKSLH---ALEKFTELKTI 489
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
19-322 |
1.07e-52 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 182.24 E-value: 1.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HDAVNFICDH 97
Cdd:PLN02467 149 KEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASH 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 98 PDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGE--A 175
Cdd:PLN02467 229 PGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSR-LLVHEriA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikVKGYENGNFVGPTIISNVKP 255
Cdd:PLN02467 308 SEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKR--PEHLKKGFFIEPTIITDVTT 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039739590 256 SMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIP 322
Cdd:PLN02467 386 SMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQP 452
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
21-363 |
6.34e-52 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 181.16 E-value: 6.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHDAVNFICDHPD 99
Cdd:PLN02466 195 PIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 100 IKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAiLVGEakKW 178
Cdd:PLN02466 275 VDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT-FVHE--RV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 179 LPELVDRAKN--LRVNAGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIISNVK 254
Cdd:PLN02466 352 YDEFVEKAKAraLKRVVGDpfKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 255 PSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN------VPIPvplpmf 328
Cdd:PLN02466 428 DDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfdAAIP------ 501
|
330 340 350
....*....|....*....|....*....|....*
gi 1039739590 329 sFTGSRSSFRGDTNfyGKQGIQFYTQLKTITSQWK 363
Cdd:PLN02466 502 -FGGYKMSGIGREK--GIYSLNNYLQVKAVVTPLK 533
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
19-359 |
1.34e-51 |
|
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: 178.31 E-value: 1.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQD-SGAPDGTLNIIHGQ-HDAVNFICD 96
Cdd:cd07120 115 REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEiPSLPAGVVNLFTESgSEGAAHLVA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 97 HPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGE-- 174
Cdd:cd07120 195 SPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSR-VLVQRsi 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 175 AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIkVKGYENGNFVGPTIISNVK 254
Cdd:cd07120 274 ADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGPV-TEGLAKGAFLRPTLLEVDD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 255 PSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVpLPMFSFTGSR 334
Cdd:cd07120 353 PDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKL-FAEAEEGGYR 431
|
330 340
....*....|....*....|....*
gi 1039739590 335 SSFRGDTNfyGKQGIQFYTQLKTIT 359
Cdd:cd07120 432 QSGLGRLH--GVAALEDFIEYKHIY 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
19-358 |
9.02e-51 |
|
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: 175.90 E-value: 9.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHP 98
Cdd:cd07102 114 REPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 99 DIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA--K 176
Cdd:cd07102 194 RIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIER-IYVHESiyD 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 177 KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVkGYENGNFVGPTIISNVKPS 256
Cdd:cd07102 273 AFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALFPE-DKAGGAYLAPTVLTNVDHS 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 257 MTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNvPIPVPLPMFSFTGSRSS 336
Cdd:cd07102 352 MRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMN-RCDYLDPALAWTGVKDS 430
|
330 340
....*....|....*....|..
gi 1039739590 337 FRGDTnfYGKQGIQFYTQLKTI 358
Cdd:cd07102 431 GRGVT--LSRLGYDQLTRPKSY 450
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
17-322 |
1.40e-50 |
|
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: 175.15 E-value: 1.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 17 SYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICD 96
Cdd:cd07095 94 RHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRETGEALAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 97 HPDIKAISFVGSNQAGEYIFER-GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAILVG-- 173
Cdd:cd07095 173 HEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDga 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 EAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKvkgyENGNFVGPTIIsNV 253
Cdd:cd07095 253 VGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV----AGTAFLSPGII-DV 327
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039739590 254 KPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIP 322
Cdd:cd07095 328 TDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTT 396
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
3-318 |
1.79e-50 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 176.55 E-value: 1.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMpSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLN 82
Cdd:PLN02766 141 GETL-KMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVIN 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 83 IIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:PLN02766 220 VVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG 238
Cdd:PLN02766 300 EICVA-SSRVYVQEGiyDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 239 YengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PLN02766 379 Y----YIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN 454
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
3-320 |
1.87e-50 |
|
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: 175.86 E-value: 1.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----GATMLLAKLLQDSGAPD 78
Cdd:cd07130 114 GLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPltaiAVTKIVARVLEKNGLPG 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 79 GTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIfergsrnGKRVQANMGAK-------NHGVVMPDANKENTLNQL 151
Cdd:cd07130 194 AIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQV-------GQAVAARFGRSllelggnNAIIVMEDADLDLAVRAV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 152 VGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASI 227
Cdd:cd07130 267 LFAAVGTAGQRCTTTRR-LIVHEsiYDEVLERLKKAYKQVRI--GDplDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTV 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 228 LLDGRRIKvkgyENGNFVGPTIISnVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKY- 306
Cdd:cd07130 344 LFGGKVID----GPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWl 418
|
330
....*....|....*
gi 1039739590 307 -AHMVDVGQVGVNVP 320
Cdd:cd07130 419 gPKGSDCGIVNVNIG 433
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
21-318 |
2.35e-49 |
|
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: 172.48 E-value: 2.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFP------AMIPlwmfpmAMVCGNTFLMKPSERVPGATM----LLAKLLQDSGAPDGTLNIIHGQHDA 90
Cdd:cd07098 120 PLGVVGAIVSWNYPfhnllgPIIA------ALFAGNAIVVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLPET 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 91 VNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaI 170
Cdd:cd07098 194 AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIER-V 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 171 LVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYENGNFVGPT 248
Cdd:cd07098 273 IVHEKiyDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPT 352
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 249 IISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07098 353 LLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIN 422
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
5-360 |
2.54e-49 |
|
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: 172.11 E-value: 2.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 5 TMPSITKDMDLYSyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNII 84
Cdd:cd07101 105 AIPVLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 85 HGQHDAV-NFICDHPDIkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRC 163
Cdd:cd07101 182 TGPGSEVgGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLC 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 164 MALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGR-RIKVKGYe 240
Cdd:cd07101 260 VSIER-IYVHESvyDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRaRPDLGPY- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 241 ngnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVP 320
Cdd:cd07101 338 ---FYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEG 414
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1039739590 321 I-----PVPLPMFSFTGSRSSFRgdtnfYGKQGIQFYTQLKTITS 360
Cdd:cd07101 415 YaaawaSIDAPMGGMKDSGLGRR-----HGAEGLLKYTETQTVAV 454
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
18-361 |
2.69e-46 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 165.44 E-value: 2.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 18 YRLPLGVCAGIAPFNFPA------MIPlwmfpmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV 91
Cdd:PRK09407 151 LRQPKGVVGVISPWNYPLtlavsdAIP------ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 92 -NFICDHPDIkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaI 170
Cdd:PRK09407 225 gTALVDNADY--LMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIER-I 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 171 LVGEAKK--WLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG---YEngnfv 245
Cdd:PRK09407 302 YVHESIYdeFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGplfYE----- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 246 gPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIpvpL 325
Cdd:PRK09407 377 -PTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGY---A 452
|
330 340 350
....*....|....*....|....*....|....*....
gi 1039739590 326 PMFSFTGSRSSFRGDTNF---YGKQGIQFYTQLKTITSQ 361
Cdd:PRK09407 453 AAWGSVDAPMGGMKDSGLgrrHGAEGLLKYTESQTIATQ 491
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
1-321 |
5.55e-44 |
|
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: 159.28 E-value: 5.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 1 MLGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGT 80
Cdd:cd07125 148 FSDPELPGPTGELNGLELH-GRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNII------HGQHdavnfICDHPDIKAISFVGSNQAGEYIFE-RGSRNGKRVQ--ANMGAKNHGVVMPDANKENTLNQL 151
Cdd:cd07125 227 LQLVpgdgeeIGEA-----LVAHPRIDGVIFTGSTETAKLINRaLAERDGPILPliAETGGKNAMIVDSTALPEQAVKDV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 152 VGAAFGAAGQRCMALSTAILVGE-AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASI--- 227
Cdd:cd07125 302 VQSAFGSAGQRCSALRLLYLQEEiAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIapa 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 228 -LLDgrrikvkgyENGNFVGPTIISNVKPSmtCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYGNGTAIFTTNGATAR 304
Cdd:cd07125 382 pLDD---------GNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIE 450
|
330
....*....|....*..
gi 1039739590 305 KYAHMVDVGQVGVNVPI 321
Cdd:cd07125 451 YWRERVEAGNLYINRNI 467
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
21-358 |
9.34e-43 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 154.90 E-value: 9.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPamipLWMF-----PmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFIC 95
Cdd:PRK09406 123 PLGVVLAVMPWNFP----LWQVvrfaaP-ALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAIL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 96 DHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAIL---V 172
Cdd:PRK09406 198 RDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVhadV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 173 GEAkkWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIISN 252
Cdd:PRK09406 278 YDA--FAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGW----FYPPTVITD 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 253 VKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNvPIPVPLPMFSFTG 332
Cdd:PRK09406 352 ITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPELPFGG 430
|
330 340 350
....*....|....*....|....*....|
gi 1039739590 333 SRSSfrGdtnfYGKQ----GIQFYTQLKTI 358
Cdd:PRK09406 431 VKRS--G----YGRElsahGIREFCNIKTV 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
4-318 |
1.23e-42 |
|
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: 155.43 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 4 ETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNI 83
Cdd:cd07083 138 VEVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQF 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 84 IHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNG------KRVQANMGAKNHGVVMPDANKENTLNQLVGAAF 156
Cdd:cd07083 217 LPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLApgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAF 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 157 GAAGQRCMALSTAILV-GEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRRIK 235
Cdd:cd07083 297 GFQGQKCSAASRLILTqGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 236 VKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVG 313
Cdd:cd07083 376 GEGY----FVAPTVVEEVPPKARIAQEEIFGPVLSVIryKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVG 451
|
....*
gi 1039739590 314 QVGVN 318
Cdd:cd07083 452 NLYIN 456
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
19-318 |
1.38e-42 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 154.92 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLL-QDSGAPDGTLNII-HGQHDAVNFICD 96
Cdd:TIGR04284 139 REAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIaEHTDFPPGVVNIVtSSDHRLGALLAK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 97 HPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQlvgAAFGA---AGQRCmALSTAILVG 173
Cdd:TIGR04284 219 DPRVDMVSFTGSTATGRAVMADAAATLKKVFLELGGKSAFIVLDDADLAAACSM---AAFTVcmhAGQGC-AITTRLVVP 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 EAKkwLPELVDRAK----NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikVKGYENGNFVGPTI 249
Cdd:TIGR04284 295 RAR--YDEAVAAAAatmgSIKPGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGR--PADRDRGFFVEPTV 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039739590 250 ISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:TIGR04284 371 IAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVN 439
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
16-362 |
5.40e-41 |
|
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 Cd Length: 486 Bit Score: 150.72 E-value: 5.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFI 94
Cdd:cd07140 142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 95 CDHPDIKAISFVGSNQAGEYIFER-GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVG 173
Cdd:cd07140 222 SDHPDVRKLGFTGSTPIGKHIMKScAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA-AGRLFVE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 EA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIIS 251
Cdd:cd07140 301 ESihDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 252 NVKPSMTCYKEEIFGPVLVV--LETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV--PIPVPLPM 327
Cdd:cd07140 377 DVEDHMFIAKEESFGPIMIIskFDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTynKTDVAAPF 456
|
330 340 350
....*....|....*....|....*....|....*
gi 1039739590 328 FSFtgSRSSFRGDtnfYGKQGIQFYTQLKTITSQW 362
Cdd:cd07140 457 GGF--KQSGFGKD---LGEEALNEYLKTKTVTIEY 486
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
18-318 |
1.77e-40 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 148.86 E-value: 1.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 18 YRlPLGVCAGIAPFNFPamipLWMF-----PMaMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVN 92
Cdd:PRK13968 124 YR-PLGTILAIMPWNFP----LWQVmrgavPI-LLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVS 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 93 FICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAIL- 171
Cdd:PRK13968 198 QMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIe 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 172 VGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGyengNFVGPTIIS 251
Cdd:PRK13968 278 EGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLLGGEKIAGAG----NYYAPTVLA 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039739590 252 NVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PRK13968 354 NVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN 420
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
16-318 |
3.49e-39 |
|
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: 145.67 E-value: 3.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 16 YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHG-QHDAVNFI 94
Cdd:cd07116 131 YHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 95 CDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPD-ANKENTL--NQLVGAAFGA--AGQRCMALSTA 169
Cdd:cd07116 210 ASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFADvMDADDAFfdKALEGFVMFAlnQGEVCTCPSRA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 170 iLVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYENGNFVGP 247
Cdd:cd07116 290 -LIQESiyDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVP 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039739590 248 TIISNVKpSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07116 369 TTFKGGN-KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN 438
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
3-356 |
6.25e-39 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 145.05 E-value: 6.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTL 81
Cdd:PRK11241 128 GDTIPGHQADKRLIVIKQPIGVTAAITPWNFPaAMITRKAGP-ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVF 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 82 NIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAG 160
Cdd:PRK11241 207 NVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAG 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 161 QRCM-ALSTAILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVkgy 239
Cdd:PRK11241 287 QTCVcANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHEL--- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 eNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNV 319
Cdd:PRK11241 364 -GGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINT 442
|
330 340 350
....*....|....*....|....*....|....*..
gi 1039739590 320 PIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 356
Cdd:PRK11241 443 GI-ISNEVAPFGGIKASGLGREG--SKYGIEDYLEIK 476
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
21-320 |
6.39e-37 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 139.97 E-value: 6.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----GATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICD 96
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 97 HPDIKAISFVGSNQAGEYIFER-GSRNGKRVqANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA 175
Cdd:PLN02315 234 DTRIPLVSFTGSSKVGLMVQQTvNARFGKCL-LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRR-LLLHES 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 --KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKvkgyENGNFVGPTIISnV 253
Cdd:PLN02315 312 iyDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE----SEGNFVQPTIVE-I 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039739590 254 KPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKY--AHMVDVGQVGVNVP 320
Cdd:PLN02315 387 SPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWigPLGSDCGIVNVNIP 455
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
21-318 |
3.69e-36 |
|
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: 136.12 E-value: 3.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGtLNIIHGQHDAVNFICDHP 98
Cdd:cd07087 100 PLGVVLIIGPWNYPLQ--LALAPLigAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEA-VAVVEGGVEVATALLAEP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 99 -DIkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEAKK 177
Cdd:cd07087 177 fDH--IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY-VLVHESIK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 178 wlPELVDRAKNlRVNA--GDQPG--ADLGPLITPQAKERVCNLIDSGTkegasILLDGRRIKVKGYengnfVGPTIISNV 253
Cdd:cd07087 254 --DELIEELKK-AIKEfyGEDPKesPDYGRIINERHFDRLASLLDDGK-----VVIGGQVDKEERY-----IAPTILDDV 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 254 KPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP-----YgngtaIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPkplalY-----LFSEDKAVQERVLAETSSGGVCVN 385
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
21-290 |
2.51e-35 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 135.09 E-value: 2.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDI 100
Cdd:PRK09457 134 PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 101 KAISFVGSNQAGeYIFER--GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVGEAKK- 177
Cdd:PRK09457 214 DGLLFTGSANTG-YLLHRqfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTC-ARRLLVPQGAQg 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 178 --WLPELVDRAKNLRVNAGD-QPGADLGPLITPQAKERVC----NLIDSgtkeGASILLDGRRIKvkgyENGNFVGPTII 250
Cdd:PRK09457 292 daFLARLVAVAKRLTVGRWDaEPQPFMGAVISEQAAQGLVaaqaQLLAL----GGKSLLEMTQLQ----AGTGLLTPGII 363
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039739590 251 --SNVK--PSmtcykEEIFGPVLVVLETETLDEAIKIVNDNPYG 290
Cdd:PRK09457 364 dvTGVAelPD-----EEYFGPLLQVVRYDDFDEAIRLANNTRFG 402
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
21-318 |
2.12e-33 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 129.76 E-value: 2.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLqDSGAPDGTLNIIHGQHDAVNFICDHP-D 99
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-TKYLDPSYVRVIEGGVEVTTELLKEPfD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 100 IkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAILVGEAKKwl 179
Cdd:PTZ00381 188 H--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKD-- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 180 pELVDRAKNLRVNA-GDQP--GADLGPLITPQAKERVCNLIDSgtkegasillDGRRIKVKGY--ENGNFVGPTIISNVK 254
Cdd:PTZ00381 264 -KFIEALKEAIKEFfGEDPkkSEDYSRIVNEFHTKRLAELIKD----------HGGKVVYGGEvdIENKYVAPTIIVNPD 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039739590 255 PSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN 396
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
3-351 |
5.13e-32 |
|
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: 125.61 E-value: 5.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 3 GETMPsitkdMDL---------YSYRLPLGVCAGIAPFNFPA-MIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQ 72
Cdd:cd07148 102 GREIP-----MGLtpasagriaFTTREPIGVVVAISAFNHPLnLIVHQVAP-AIAAGCPVIVKPALATPLSCLAFVDLLH 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 73 DSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSrNGKRVqanmgAKNHG-----VVMPDANKENT 147
Cdd:cd07148 176 EAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLA-PGTRC-----ALEHGgaapvIVDRSADLDAM 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 148 LNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDSGTKE 223
Cdd:cd07148 250 IPPLVKGGFYHAGQVCVSVQR-VFVPAeiADDFAQRLAAAAEKLVV--GDPtdPDTEVGPLIRPREVDRVEEWVNEAVAA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 224 GASILLDGRRIKVKGYEngnfvgPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATA 303
Cdd:cd07148 327 GARLLCGGKRLSDTTYA------PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVA 400
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1039739590 304 RKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSfrGdtnfYGKQGIQF 351
Cdd:cd07148 401 LKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQS--G----YGTGGIPY 442
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
21-318 |
5.84e-32 |
|
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: 125.03 E-value: 5.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHDAVNFICDHP 98
Cdd:cd07134 100 PKGVCLIISPWNYPFN--LAFGPLvsAIAAGNTAILKPSELTPHTSAVIAKIIREAFDED-EVAVFEGDAEVAQALLELP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 99 dIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEAKKw 178
Cdd:cd07134 177 -FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY-VFVHESVK- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 179 lPELVDR-----AKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIkvkgyENGNFVGPTIISNV 253
Cdd:cd07134 254 -DAFVEHlkaeiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD-----AAQRYIAPTVLTNV 327
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039739590 254 KPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:cd07134 328 TPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN 392
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
18-296 |
9.37e-32 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 125.39 E-value: 9.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 18 YRlPL-GVCAGIAPFNFPAM------IPLWMfpmamvcGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDA 90
Cdd:cd07123 167 YR-PLeGFVYAVSPFNFTAIggnlagAPALM-------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 91 V-NFICDHPDIKAISFVGS--------NQAGEYIfeRGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 161
Cdd:cd07123 239 VgDTVLASPHLAGLHFTGStptfkslwKQIGENL--DRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQ 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 162 RCMALSTA-ILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKE-GASILLDGRRIKVKGY 239
Cdd:cd07123 317 KCSAASRAyVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGY 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 240 engnFVGPTIISNVKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVND-NPYGNGTAIF 296
Cdd:cd07123 397 ----FVEPTVIETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDTtSPYALTGAIF 452
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
19-349 |
2.53e-31 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 124.10 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 19 RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDH 97
Cdd:PLN00412 156 KIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIgDFLTMH 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 98 PDIKAISFVGSNqAGEYIfergSRNGKRV--QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALStAILVGE- 174
Cdd:PLN00412 236 PGVNCISFTGGD-TGIAI----SKKAGMVplQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVK-VVLVMEs 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 175 -AKKWLPELVDRAKNLRVNAGDQpGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvkgyeNGNFVGPTIISNV 253
Cdd:PLN00412 310 vADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNV 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 254 KPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPiPVPLP-MFSFTG 332
Cdd:PLN00412 382 RPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA-PARGPdHFPFQG 460
|
330
....*....|....*..
gi 1039739590 333 SRSSfrgdtnFYGKQGI 349
Cdd:PLN00412 461 LKDS------GIGSQGI 471
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
21-297 |
2.38e-29 |
|
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: 117.71 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQdSGAPDGTLNIIHGQHDAVNFICDHPDI 100
Cdd:cd07135 108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVP-KYLDPDAFQVVQGGVPETTALLEQKFD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 101 KaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEAKkwLP 180
Cdd:cd07135 187 K-IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDY-VLVDPSV--YD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 181 ELVDRAK---NLRVNAGDQPGADLGPLITPQAKERVCNLIDSgTKegASILLDGRRIKVKgyengNFVGPTIISNVKPSM 257
Cdd:cd07135 263 EFVEELKkvlDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT-TK--GKVVIGGEMDEAT-----RFIPPTIVSDVSWDD 334
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1039739590 258 TCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFT 297
Cdd:cd07135 335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFT 374
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
21-318 |
3.26e-28 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 226683 [Multi-domain] Cd Length: 769 Bit Score: 116.34 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPgatmLLA----KLLQDSGAPDGTLNIIHGQHDAVN-FIC 95
Cdd:COG4230 236 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP----LIAaqavRLLHEAGVPPGVLQLLPGRGETVGaALT 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 96 DHPDIKAISFVGSNQAGEYIfER--GSRNGKRVQ--ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAIL 171
Cdd:COG4230 312 ADARVAGVMFTGSTEVARLI-QRqlAKRQGRPIPliAETGGQNAMIVDSSALAEQVVADVLASAFDSAGQRCSALRVLCL 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 172 VGE-AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDsgtkegaSILLDGRRI----KVKGYENGNFVG 246
Cdd:COG4230 391 QEDvADRILTMLKGAMAELRVGNPDRLTTDVGPVIDAEAKANIEKHIQ-------TMRSKGRLVhqaaAPNSLQKGTFVA 463
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039739590 247 PTIISnvKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:COG4230 464 PTLIE--LENLDELQREVFGPVLHVVryKRDELDEVIDQINATGYGLTLGVHTRIDETIAHVTERAHAGNLYVN 535
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
21-318 |
1.18e-27 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 113.85 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVN-FICDHPD 99
Cdd:TIGR01238 160 SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGaALTSDPR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 100 IKAISFVGSNQAGEYI----FERGSRNGKRVqANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAILVGE- 174
Cdd:TIGR01238 240 IAGVAFTGSTEVAQLInqtlAQREDAPVPLI-AETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDv 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 175 AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIlLDGRRIKVKGYENGNFVGPTIISnvK 254
Cdd:TIGR01238 319 ADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKI-AQLTLDDSRACQHGTFVAPTLFE--L 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039739590 255 PSMTCYKEEIFGPVL--VVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:TIGR01238 396 DDIAELSEEVFGPVLhvVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN 461
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
16-305 |
2.15e-26 |
|
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: 109.52 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 16 YSYRLPLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHDAVNF 93
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQ--LALAPLigAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 94 IC----DHpdikaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTA 169
Cdd:cd07136 172 LLdqkfDY-----IFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVA-PDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 170 ILVGEAKK--WLPELVDRAKNLRvnaGDQP--GADLGPLITPQAKERVCNLIDSGTkegasILLDGrrikvKGYENGNFV 245
Cdd:cd07136 246 VLVHESVKekFIKELKEEIKKFY---GEDPleSPDYGRIINEKHFDRLAGLLDNGK-----IVFGG-----NTDRETLYI 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039739590 246 GPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP-----YgngtaIFTTNGATARK 305
Cdd:cd07136 313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPkplalY-----LFSEDKKVEKK 372
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
21-358 |
4.69e-26 |
|
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: 108.27 E-value: 4.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQ---DSGApdgtLNIIHGQHDAVNFICDH 97
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPeylDTKA----IKVIEGGVPETTALLEQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 98 PDIKaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA-AGQRCMALSTaILVGEak 176
Cdd:cd07137 177 KWDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDY-VLVEE-- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 177 KWLPELVDRAKN-LRVNAGDQP--GADLGPLITPQAKERVCNLIDSgTKEGASILLDGRRIkvkgyENGNFVGPTIISNV 253
Cdd:cd07137 253 SFAPTLIDALKNtLEKFFGENPkeSKDLSRIVNSHHFQRLSRLLDD-PSVADKIVHGGERD-----EKNLYIEPTILLDP 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 254 KPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN-VPIPVPLPMFSFTG 332
Cdd:cd07137 327 PLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdTVVQYAIDTLPFGG 406
|
330 340
....*....|....*....|....*.
gi 1039739590 333 SRSSfrGDTNFYGKQGIQFYTQLKTI 358
Cdd:cd07137 407 VGES--GFGAYHGKFSFDAFSHKKAV 430
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
23-318 |
1.52e-25 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 108.75 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 23 GVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIK 101
Cdd:PRK11904 686 GVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 102 AISFVGSNQAGEYIfERG--SRNGKRVQ--ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALStAILVGE--A 175
Cdd:PRK11904 766 GVAFTGSTETARII-NRTlaARDGPIVPliAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALR-VLFVQEdiA 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 176 KKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEG---ASILLDGrrikvkGYENGNFVGPTII 250
Cdd:PRK11904 844 DRVIEMLKGAMAELKV--GDprLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLPA------GTENGHFVAPTAF 915
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 251 SnvKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PRK11904 916 E--IDSISQLEREVFGPILHVIryKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
7-280 |
1.61e-24 |
|
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: 104.24 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 7 PSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIH 85
Cdd:cd07084 86 LGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLIN 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 86 GQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRngKRVQANMGAKNHGVVMPDAN-KENTLNQLVGAAFGAAGQRCM 164
Cdd:cd07084 166 GDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 165 ALStAILVGEAKKWLPeLVDRAKNLRVNAGDQpGADLGPLITPQAKERVCNLIDsgtkegasilLDGRRIKVKGYENGNF 244
Cdd:cd07084 244 AQS-MLFVPENWSKTP-LVEKLKALLARRKLE-DLLLGPVQTFTTLAMIAHMEN----------LLGSVLLFSGKELKNH 310
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1039739590 245 VGPTIISNVKPS---MTC---------YKEEIFGPVLVVLETETLDEA 280
Cdd:cd07084 311 SIPSIYGACVASalfVPIdeilktyelVTEEIFGPFAIVVEYKKDQLA 358
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
21-318 |
3.48e-23 |
|
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: 100.25 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFP---AMIPLwmfPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHD------AV 91
Cdd:cd07133 101 PLGVVGIIVPWNYPlylALGPL---IAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTGGADvaaafsSL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 92 NFicDHpdikaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMA----L- 166
Cdd:cd07133 177 PF--DH-----LLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVApdyvLv 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 167 ---STAILVGEAKKWL----PELVDraknlrvnagdqpGADLGPLITPQAKERVCNLIDSGTKEGASI---------LLD 230
Cdd:cd07133 250 pedKLEEFVAAAKAAVakmyPTLAD-------------NPDYTSIINERHYARLQGLLEDARAKGARVielnpagedFAA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 231 GRRIkvkgyengnfvGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP-----YgngtaIFTTNGATARK 305
Cdd:cd07133 317 TRKL-----------PPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPrplalY-----YFGEDKAEQDR 380
|
330
....*....|...
gi 1039739590 306 YAHMVDVGQVGVN 318
Cdd:cd07133 381 VLRRTHSGGVTIN 393
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
14-299 |
7.32e-21 |
|
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: 93.44 E-value: 7.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 14 DLYSYRLPLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDA- 90
Cdd:cd07132 93 DVYIYKEPLGVVLIIGAWNYP--LQLTLVPLvgAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVLGGVEETt 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 91 --VNFICDHpdikaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMA--- 165
Cdd:cd07132 171 elLKQRFDY-----IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdy 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 166 -LSTA----ILVGEAKKWLPELVdraknlrvnaGDQP--GADLGPLITPQAKERVCNLIDSGTkegasILLDGRrikvkG 238
Cdd:cd07132 246 vLCTPevqeKFVEALKKTLKEFY----------GEDPkeSPDYGRIINDRHFQRLKKLLSGGK-----VAIGGQ-----T 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039739590 239 YENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVN--DNP---YgngtaIFTTN 299
Cdd:cd07132 306 DEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINsrEKPlalY-----VFSNN 366
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
21-290 |
7.62e-21 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 94.66 E-value: 7.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPD 99
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVgAALVADAR 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 100 IKAISFVGSNQAGEY----IFERGSRNGKRVQ--ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAILVG 173
Cdd:PRK11809 848 VRGVMFTGSTEVARLlqrnLAGRLDPQGRPIPliAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQD 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 174 E-AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRiKVKGYENGNFVGPTIISn 252
Cdd:PRK11809 928 DvADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARE-NSEDWQSGTFVPPTLIE- 1005
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1039739590 253 vKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYG 290
Cdd:PRK11809 1006 -LDSFDELKREVFGPVLHVVryNRNQLDELIEQINASGYG 1044
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
21-358 |
3.83e-19 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 88.56 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHDAVNFICDHPDI 100
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVVEGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 101 KaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA-AGQRCMALSTAIlvgEAKKWL 179
Cdd:PLN02174 191 K-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYIL---TTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 180 PELVDRAK-NLRVNAGDQP--GADLGPLITPQAKERVCNLIDSgtKEGASILLDGRRikvKGYENGNfVGPTIISNVKPS 256
Cdd:PLN02174 267 PKVIDAMKkELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDE--KEVSDKIVYGGE---KDRENLK-IAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 257 MTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN-VPIPVPLPMFSFTGSRS 335
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVGE 420
|
330 340
....*....|....*....|...
gi 1039739590 336 SFRGdtNFYGKQGIQFYTQLKTI 358
Cdd:PLN02174 421 SGMG--AYHGKFSFDAFSHKKAV 441
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
17-290 |
1.17e-18 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 88.00 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 17 SYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPgatmLLA----KLLQDSGAPDGTLNIIHGQHDAV- 91
Cdd:PRK11905 672 PGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTP----LIAaravRLLHEAGVPKDALQLLPGDGRTVg 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 92 NFICDHPDIKAISFVGSNQAGEYIfER--GSRNGKRVQ--ANMGAKNHGVVMPDANKEntlnQLVGA----AFGAAGQRC 163
Cdd:PRK11905 748 AALVADPRIAGVMFTGSTEVARLI-QRtlAKRSGPPVPliAETGGQNAMIVDSSALPE----QVVADviasAFDSAGQRC 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 164 MALStaIL-VGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIlldgRRIKV-KGY 239
Cdd:PRK11905 823 SALR--VLcLQEdvADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLpAET 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1039739590 240 ENGNFVGPTIISnvKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYG 290
Cdd:PRK11905 897 EKGTFVAPTLIE--IDSISDLEREVFGPVLHVVrfKADELDRVIDDINATGYG 947
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
21-318 |
2.33e-14 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 73.99 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQ---DSGApdgtLNIIHGQHDAVNFIC 95
Cdd:PLN02203 108 PLGVVLIFSSWNFP--IGLSLEPLigAIAAGNAVVLKPSELAPATSAFLAANIPkylDSKA----VKVIEGGPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 96 DHPDIKaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENT---LNQLVGAAFGA-AGQRCMALSTaIL 171
Cdd:PLN02203 182 QHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSLSSSRDTkvaVNRIVGGKWGScAGQACIAIDY-VL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 172 VGEakKWLPELVDRAKN-LRVNAGDQPG--ADLGPLITPQAKERVCNLIDSgTKEGASILLDGRRikvkgYENGNFVGPT 248
Cdd:PLN02203 260 VEE--RFAPILIELLKStIKKFFGENPResKSMARILNKKHFQRLSNLLKD-PRVAASIVHGGSI-----DEKKLFIEPT 331
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 249 IISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 318
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFN 401
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
18-284 |
2.54e-12 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 67.91 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 18 YRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDH 97
Cdd:cd07126 139 YRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 98 PDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKnhgVVMPDANKENTLN-QLVGAAFGAAGQRCMALStaILVGEaK 176
Cdd:cd07126 219 ANPRMTLFTGSSKVAERLALELHGKVKLEDAGFDWK---ILGPDVSDVDYVAwQCDQDAYACSGQKCSAQS--ILFAH-E 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 177 KWLPE-LVDRAKNLrvnAGDQPGADL--GPLITpQAKERVCNLIDSGTK-EGASILLDGRRIKvkgyeNGNFvgPTIISN 252
Cdd:cd07126 293 NWVQAgILDKLKAL---AEQRKLEDLtiGPVLT-WTTERILDHVDKLLAiPGAKVLFGGKPLT-----NHSI--PSIYGA 361
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1039739590 253 VKPS------MTCYKE--------EIFGPVLVVleTETLDEAIKIV 284
Cdd:cd07126 362 YEPTavfvplEEIAIEenfelvttEVFGPFQVV--TEYKDEQLPLV 405
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
13-285 |
1.36e-11 |
|
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: 65.64 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 13 MDLYSYRLPLGVCAGIAPFNFP-AmiplwmFPM-------AMVCGNTFLMKPSERVPGATMLLAKL----LQDSGAPDGT 80
Cdd:cd07129 97 PDLRRMLVPLGPVAVFGASNFPlA------FSVaggdtasALAAGCPVVVKAHPAHPGTSELVARAiraaLRATGLPAGV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 81 LNIIHGQHDAVNF-ICDHPDIKAISFVGSNQAGEYIFERGSR--NGKRVQANMGAKNHGVVMPDANKEN--TLNQ-LVGA 154
Cdd:cd07129 171 FSLLQGGGREVGVaLVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGALAERgeAIAQgFVGS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 155 AFGAAGQRCmaLSTAILVGEAKKWLPELVDRAKNLrvnAGDQPGadlGPLITPqakeRVCNLIDSGTKEGASilLDGRRI 234
Cdd:cd07129 251 LTLGAGQFC--TNPGLVLVPAGPAGDAFIAALAEA---LAAAPA---QTMLTP----GIAEAYRQGVEALAA--APGVRV 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039739590 235 KVKGY--ENGNFVGPTIisnVKPSMTCY------KEEIFGPVLVVLETETLDEAIKIVN 285
Cdd:cd07129 317 LAGGAaaEGGNQAAPTL---FKVDAAAFladpalQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
23-307 |
3.46e-10 |
|
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: 61.13 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 23 GVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQhdaVNFICDHPDIK 101
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHLGEQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 102 -AISFVGSNQAGEYIfeRGS----RNGKRVQANMGAKNHGVVMPDANKENT-----LNQLVGAAFGAAGQRCMALSTAIL 171
Cdd:cd07128 223 dVVAFTGSAATAAKL--RAHpnivARSIRFNAEADSLNAAILGPDATPGTPefdlfVKEVAREMTVKAGQKCTAIRRAFV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 172 -------VGEAkkwlpeLVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG--YE 240
Cdd:cd07128 301 pearvdaVIEA------LKARLAKVVV--GDprLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVGadAE 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039739590 241 NGNFVGPTII--SNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNdnpYGNG---TAIFTTNGATARKYA 307
Cdd:cd07128 373 KGAFFPPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAA---RGRGslvASVVTNDPAFARELV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
23-284 |
2.49e-07 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 52.40 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 23 GVCAGIAPFNFPAMiPLW-MFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQH----DAVNfICD 96
Cdd:PRK11903 150 GVALFINAFNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSagllDHLQ-PFD 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 97 hpdikAISFVGSNQAGEYIFERGS--RNGKRVQANMGAKNHGVVMPDANKEntlnqlvGAAFGA------------AGQR 162
Cdd:PRK11903 228 -----VVSFTGSAETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAAPG-------SEAFDLfvkevvremtvkSGQK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 163 CMALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDsGTKEGASILLDGRRIKVKGYE 240
Cdd:PRK11903 296 CTAIRR-IFVPEAlyDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDAD 373
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1039739590 241 N--GNFVGPTIISNVKP--SMTCYKEEIFGPVLVVLETETLDEAIKIV 284
Cdd:PRK11903 374 PavAACVGPTLLGASDPdaATAVHDVEVFGPVATLLPYRDAAHALALA 421
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
21-174 |
1.87e-04 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 42.98 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 21 PLGVCAGIAPFNFPAMIPLWMFpMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNII----HGQHDAVNFICD 96
Cdd:cd07077 100 PIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVlyvpHPSDELAEELLS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739590 97 HPDIKAISFVGSNQAGEYIfeRGSRNGKRVQAnMGAKNHGVVMPDANKENTLNQLV--GAAF-GAAgqrCMALSTAILVG 173
Cdd:cd07077 179 HPKIDLIVATGGRDAVDAA--VKHSPHIPVIG-FGAGNSPVVVDETADEERASGSVhdSKFFdQNA---CASEQNLYVVD 252
|
.
gi 1039739590 174 E 174
Cdd:cd07077 253 D 253
|
|
|