|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
38-491 |
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: 894.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:cd07085 24 ATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLRGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLA 197
Cdd:cd07085 104 EVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 198 KLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTL 277
Cdd:cd07085 184 ELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 278 NQLVGAAFGAAGQRCMALSTAILVG-EAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASI 356
Cdd:cd07085 264 NALVGAAFGAAGQRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 357 LLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYA 436
Cdd:cd07085 344 VLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQ 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1907085552 437 HMVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 491
Cdd:cd07085 424 REVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
38-491 |
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: 849.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:TIGR01722 24 ATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVARGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLA 197
Cdd:TIGR01722 104 EVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 198 KLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTL 277
Cdd:TIGR01722 184 ELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 278 NQLVGAAFGAAGQRCMALSTAILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIL 357
Cdd:TIGR01722 264 DALVGAAYGAAGQRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 358 LDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAH 437
Cdd:TIGR01722 344 LDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQH 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1907085552 438 MVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 491
Cdd:TIGR01722 424 EIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
38-507 |
0e+00 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 645.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:PLN02419 137 ATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLA 197
Cdd:PLN02419 217 EVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 198 KLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTL 277
Cdd:PLN02419 297 ELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 278 NQLVGAAFGAAGQRCMALSTAILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIL 357
Cdd:PLN02419 377 NALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 358 LDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAH 437
Cdd:PLN02419 457 LDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQM 536
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 438 MVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSspaVVMPT 507
Cdd:PLN02419 537 DIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQKDIHSPFS---LAIPI 603
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
38-491 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 521.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:COG1012 29 ATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLA 197
Cdd:COG1012 109 DFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 198 KLLQDSGAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENT 276
Cdd:COG1012 189 ELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 277 LNQLVGAAFGAAGQRCMALSTAILVGE-AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGAS 355
Cdd:COG1012 269 VEAAVRGAFGNAGQRCTAASRLLVHESiYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 356 ILLDGRRIKVkgyENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKY 435
Cdd:COG1012 349 LLTGGRRPDG---EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRV 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907085552 436 AHMVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDtnFYGKQGIQFYTQLKTITSQW 491
Cdd:COG1012 426 ARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGR--EGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
38-487 |
5.36e-172 |
|
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: 492.82 E-value: 5.36e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:pfam00171 15 ATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLA 197
Cdd:pfam00171 95 DVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 198 KLLQDSGAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENT 276
Cdd:pfam00171 174 ELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 277 LNQLVGAAFGAAGQRCMALSTAILVGEAK-KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGAS 355
Cdd:pfam00171 254 VEAAVFGAFGNAGQVCTATSRLLVHESIYdEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 356 ILLDGRRikvkGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKY 435
Cdd:pfam00171 334 LLTGGEA----GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRV 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907085552 436 AHMVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 487
Cdd:pfam00171 410 ARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
55-488 |
2.28e-134 |
|
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: 395.81 E-value: 2.28e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 55 DAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGET 134
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 135 MPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIH 214
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 215 G-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCM 293
Cdd:cd07078 161 GdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 294 ALStAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIkvkGYENG 371
Cdd:cd07078 241 AAS-RLLVHEsiYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRL---EGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 372 NFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIP 451
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907085552 452 VPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 488
Cdd:cd07078 397 GAEPSAPFGGVKQS--GIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
39-488 |
1.76e-132 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 392.87 E-value: 1.76e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQ 118
Cdd:cd07131 24 LEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQEAID 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 119 VVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAK 198
Cdd:cd07131 104 MAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 199 LLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTL 277
Cdd:cd07131 184 LFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 278 NQLVGAAFGAAGQRCMALSTAIL-VGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASI 356
Cdd:cd07131 264 EGALWSAFGTTGQRCTATSRLIVhESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 357 LLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYA 436
Cdd:cd07131 344 LLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRAR 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 437 HMVDVGQVGVNVPI---PVPLPmF-----SFTGSRSSfrgdtnfyGKQGIQFYTQLKTIT 488
Cdd:cd07131 424 RDLEAGITYVNAPTigaEVHLP-FggvkkSGNGHREA--------GTTALDAFTEWKAVY 474
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
39-487 |
8.73e-123 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 367.73 E-value: 8.73e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQ 118
Cdd:cd07097 24 TSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 119 VVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAK 198
Cdd:cd07097 104 IFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 199 LLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTL 277
Cdd:cd07097 184 ILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 278 NQLVGAAFGAAGQRCMALSTAILV-GEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASI 356
Cdd:cd07097 264 ECAVQGAFFSTGQRCTASSRLIVTeGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 357 LLDGRRIkvKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYA 436
Cdd:cd07097 344 VYGGERL--KRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFK 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085552 437 HMVDVGQVGVNVP-----IPVPlpmfsFTGSRSSFRGdtnfYGKQG---IQFYTQLKTI 487
Cdd:cd07097 422 RRVEAGVVMVNLPtagvdYHVP-----FGGRKGSSYG----PREQGeaaLEFYTTIKTV 471
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
22-449 |
2.86e-115 |
|
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: 348.78 E-value: 2.86e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 22 VNATWYPASSFSSSSV--ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLIT 99
Cdd:cd07086 3 IGGEWVGSGGETFTSRnpANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 100 LEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGN 179
Cdd:cd07086 83 LEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 180 TFLMKPSERVP----GATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRV 255
Cdd:cd07086 163 TVVWKPSETTPltaiAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 256 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAIL-VGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLI 334
Cdd:cd07086 243 LLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVhESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 335 TPQAKERVCNLIDSGTKEGASILLDGRRIkvKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVN 414
Cdd:cd07086 323 NQAAVEKYLNAIEIAKSQGGTVLTGGKRI--DGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINN 400
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907085552 415 DNPYGNGTAIFTTNGATARKY--AHMVDVGQVGVNVP 449
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIP 437
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
38-488 |
1.23e-112 |
|
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: 341.08 E-value: 1.23e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAE-GDVFRG 116
Cdd:cd07093 5 ATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRDIPRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 117 LQVVEHACSVTSLMLGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLL 196
Cdd:cd07093 85 AANFRFFADYILQLDGESYPQDGGALN-YVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 197 AKLLQDSGAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKEN 275
Cdd:cd07093 164 AELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 276 TLNQLVGAAFGAAGQRCMAlSTAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEG 353
Cdd:cd07093 244 AVDAAVRSSFSNNGEVCLA-GSRILVQRsiYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 354 ASILLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATAR 433
Cdd:cd07093 323 ATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAH 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1907085552 434 KYAHMVDVGQVGVNVPIPVPLPMfSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 488
Cdd:cd07093 403 RVARRLEAGTVWVNCWLVRDLRT-PFGGVKAS--GIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
38-488 |
8.05e-111 |
|
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: 336.33 E-value: 8.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:cd07103 5 ATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVV----EHACSVTslmlGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGA 192
Cdd:cd07103 85 SFLewfaEEARRIY----GRTIPSPAPGKRILVIKQPVGVVAAITPWNFPaAMITRKIAP-ALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 193 TMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAknHG--VVMP 269
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG--NApfIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 270 DANKENTLNQLVGAAFGAAGQRCMAlSTAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLID 347
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVC-ANRIYVHEsiYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 348 SGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTT 427
Cdd:cd07103 317 DAVAKGAKVLTGGKRLGLGGY----FYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907085552 428 NGATARKYAHMVDVGQVGVNVPIPvPLPMFSFTGSRSSfrGdtnfYG----KQGIQFYTQLKTIT 488
Cdd:cd07103 393 DLARAWRVAEALEAGMVGINTGLI-SDAEAPFGGVKES--G----LGreggKEGLEEYLETKYVS 450
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
38-487 |
4.32e-103 |
|
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: 316.39 E-value: 4.32e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:cd07106 5 ATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHacsVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLA 197
Cdd:cd07106 85 AWLRY---TASLDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 198 KLLQDSgAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTL 277
Cdd:cd07106 162 ELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 278 NQLVGAAFGAAGQRCMALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGAS 355
Cdd:cd07106 241 PKLFWGAFINSGQVCAAIKR-LYVHESiyDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 356 ILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKY 435
Cdd:cd07106 320 VLAGGEPLDGPGY----FIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAV 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907085552 436 AHMVDVGQVGVNvPIPVPLPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 487
Cdd:cd07106 396 ARRLEAGTVWIN-THGALDPDAPFGGHKQSGIGVE--FGIEGLKEYTQTQVI 444
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
62-488 |
1.63e-98 |
|
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: 301.84 E-value: 1.63e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 62 KRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKD 141
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 142 MDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHDAV 220
Cdd:cd06534 84 GEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGgGDEVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 221 NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaIL 300
Cdd:cd06534 164 AALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR-LL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 301 VGEAKKwlPELVDRAKnlrvnagdqpgadlgplitpqakervcnlidsgtkegasilldgrrikvkgyengnfvgpTIIS 380
Cdd:cd06534 243 VHESIY--DEFVEKLV------------------------------------------------------------TVLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 381 NVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVPLPMFSFT 460
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFG 340
|
410 420
....*....|....*....|....*...
gi 1907085552 461 GSRSSFRGDTNfyGKQGIQFYTQLKTIT 488
Cdd:cd06534 341 GVKNSGIGREG--GPYGLEEYTRTKTVV 366
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
38-487 |
2.34e-98 |
|
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: 304.96 E-value: 2.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:cd07088 21 ATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLL 196
Cdd:cd07088 101 DYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPfFLIARKLAP-ALVTGNTIVIKPSEETPLNALEF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 197 AKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKEN 275
Cdd:cd07088 180 AELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 276 TLNQLVGAAFGAAGQRCMAlSTAILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTK 351
Cdd:cd07088 260 AVKAIVDSRIINCGQVCTC-AERVYVHEdiYDEFMEKLVEKMKAVKV--GDpfDAATDMGPLVNEAALDKVEEMVERAVE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 352 EGASILLDGRRIKVkgyENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAT 431
Cdd:cd07088 337 AGATLLTGGKRPEG---EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNT 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907085552 432 ARKYAHMVDVGQVGVNVPIPVPLPMFSfTGSRSSFRGDTNfyGKQGIQFYTQLKTI 487
Cdd:cd07088 414 AMRATNELEFGETYINRENFEAMQGFH-AGWKKSGLGGAD--GKHGLEEYLQTKVV 466
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
38-487 |
1.77e-97 |
|
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: 302.16 E-value: 1.77e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAF--PAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFR 115
Cdd:cd07114 5 ATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 116 GLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATML 195
Cdd:cd07114 85 LAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 196 LAKLLQDSGAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKE 274
Cdd:cd07114 165 LAKLAEEAGFPPGVVNVVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 275 NTLNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKE 352
Cdd:cd07114 245 AAVNGVVAGIFAAAGQTCVAGSR-LLVQRsiYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 353 GASILLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATA 432
Cdd:cd07114 324 GARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARA 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1907085552 433 RKYAHMVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 487
Cdd:cd07114 404 HRVARAIEAGTVWVNTYRALS-PSSPFGGFKDSGIGREN--GIEAIREYTQTKSV 455
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
38-447 |
2.43e-97 |
|
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: 302.69 E-value: 2.43e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAF--PAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFR 115
Cdd:cd07119 21 ANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 116 GLQVVEHACSVTSLMLGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATML 195
Cdd:cd07119 101 VANCFRYYAGLATKETGEVYDV-PPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 196 LAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKE 274
Cdd:cd07119 180 LFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 275 NTLNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKE 352
Cdd:cd07119 260 TAVDQALNGVFFNAGQVCSAGSR-LLVEEsiHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 353 GASILLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATA 432
Cdd:cd07119 339 GARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARA 418
|
410
....*....|....*
gi 1907085552 433 RKYAHMVDVGQVGVN 447
Cdd:cd07119 419 NRVARRLRAGTVWIN 433
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
38-487 |
1.09e-95 |
|
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: 297.68 E-value: 1.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:cd07090 5 ATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLA 197
Cdd:cd07090 85 DCLEYYAGLAPTLSGEHVP-LPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 198 KLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTL 277
Cdd:cd07090 164 EILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 278 NQLVGAAFGAAGQRCmALSTAILVGEA--KKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEG 353
Cdd:cd07090 244 NGAMMANFLSQGQVC-SNGTRVFVQRSikDEFTERLVERTKKIRI--GDplDEDTQMGALISEEHLEKVLGYIESAKQEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 354 ASILLDGRRIKVK-GYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATA 432
Cdd:cd07090 321 AKVLCGGERVVPEdGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085552 433 RKYAHMVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 487
Cdd:cd07090 401 HRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
38-487 |
3.55e-94 |
|
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: 293.58 E-value: 3.55e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEG-DVFRG 116
Cdd:cd07115 5 ATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVPRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 117 LQVVEHACSVTSLMLGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLL 196
Cdd:cd07115 85 ADTFRYYAGWADKIEGEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 197 AKLLQDSGAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKEN 275
Cdd:cd07115 164 AELMAEAGFPAGVLNVVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 276 TLNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEG 353
Cdd:cd07115 244 AVRAAATGIFYNQGQMCTAGSR-LLVHEsiYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 354 ASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATAR 433
Cdd:cd07115 323 ARLLTGGKRPGARGF----FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085552 434 KYAHMVDVGQVGVNVpipvplpmFSFTGSRSSFRG--DTNF---YGKQGIQFYTQLKTI 487
Cdd:cd07115 399 RVAAALKAGTVWINT--------YNRFDPGSPFGGykQSGFgreMGREALDEYTEVKSV 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
53-488 |
3.97e-94 |
|
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: 292.51 E-value: 3.97e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 53 EMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLG 132
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 133 ETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKLLQDSGAPDGTLN 211
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 212 IIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 290
Cdd:cd07104 161 VVPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 291 RCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvk 366
Cdd:cd07104 241 ICMAAGR-ILVHEsvYDEFVEKLVAKAKALPV--GDPrdPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 367 gyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGV 446
Cdd:cd07104 314 ---EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHI 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1907085552 447 NVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 488
Cdd:cd07104 391 NDQTVNDEPHVPFGGVKAS--GGGRFGGPASLEEFTEWQWIT 430
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
39-488 |
5.73e-92 |
|
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: 289.51 E-value: 5.73e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQ 118
Cdd:cd07124 56 PSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAID 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 119 VVEHACSVTSLMLGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAK 198
Cdd:cd07124 136 FLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 199 LLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFER------GSRNGKRVQANMGAKNHGVVMPDA 271
Cdd:cd07124 215 ILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERaakvqpGQKWLKRVIAEMGGKNAIIVDEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 272 NKENTLNQLVGAAFGAAGQRCMALSTAILVGEA-KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGT 350
Cdd:cd07124 295 DLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVyDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 351 KEGaSILLDGRRIKVKgyENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGA 430
Cdd:cd07124 375 SEG-RLLLGGEVLELA--AEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPE 451
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907085552 431 TARKYAHMVDVGQVGVNVPIPVPLPMF-SFTGSRSSfrGDTnfyGKQG-----IQFyTQLKTIT 488
Cdd:cd07124 452 HLERARREFEVGNLYANRKITGALVGRqPFGGFKMS--GTG---SKAGgpdylLQF-MQPKTVT 509
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
38-488 |
1.59e-91 |
|
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: 286.54 E-value: 1.59e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPA--WADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFR 115
Cdd:cd07118 5 AHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 116 GLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATML 195
Cdd:cd07118 85 AADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 196 LAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKE 274
Cdd:cd07118 165 LAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 275 NTLNqlvGAAFGA---AGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLID 347
Cdd:cd07118 245 AAAD---AVVFGVyfnAGECCNSGSR-LLVHEsiADAFVAAVVARSRKVRV--GDplDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 348 SGTKEGASILLDGRRIkvkGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTT 427
Cdd:cd07118 319 AGRAEGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSK 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907085552 428 NGATARKYAHMVDVGQVGVNVPIP--VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 488
Cdd:cd07118 396 DIDTALTVARRIRAGTVWVNTFLDgsPELP---FGGFKQSGIGREL--GRYGVEEYTELKTVH 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
39-488 |
4.03e-90 |
|
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: 282.95 E-value: 4.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQ 118
Cdd:cd07149 8 DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 119 VVEHACSVTSLMLGETMPsitkdMDL---------YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERV 189
Cdd:cd07149 88 TLRLSAEEAKRLAGETIP-----FDAspggegrigFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 190 PGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGsrnG-KRVQANMGAKNHGVV 267
Cdd:cd07149 163 PLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKA---GlKKVTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 268 MPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEAKK--WLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVC 343
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQVCISVQR-IFVHEDIYdeFLERFVAATKKLVV--GDplDEDTDVGPMISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 344 NLIDSGTKEGASILLDGRRikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTA 423
Cdd:cd07149 317 EWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAG 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907085552 424 IFTTNGATARKYAHMVDVGQVGVNVPipvplpmfsftgsrSSFRGDTNFYG--------KQGIQF----YTQLKTIT 488
Cdd:cd07149 390 VFTNDLQKALKAARELEVGGVMINDS--------------STFRVDHMPYGgvkesgtgREGPRYaieeMTEIKLVC 452
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
38-485 |
1.74e-89 |
|
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: 281.70 E-value: 1.74e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAE-GDVFRG 116
Cdd:TIGR01804 21 ANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLETLDTGKTLQETIvADMDSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 117 LQVVEHACSVTSLMLGETMPSITKDmDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLL 196
Cdd:TIGR01804 101 ADVFEFFAGLAPALNGEIIPLGGPS-FAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 197 AKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKEN 275
Cdd:TIGR01804 180 AEIMEEAGLPKGVFNVVQGDGAEVgPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLES 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 276 TLNQLVGAAFGAAGQRCMALSTAILVGEAK-KWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGA 354
Cdd:TIGR01804 260 AVDGAMLGNFFSAGQVCSNGTRVFVHKKIKeRFLARLVERTERIKLGDPFDEATEMGPLISAAHRDKVLSYIEKGKAEGA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 355 SILLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARK 434
Cdd:TIGR01804 340 TLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHR 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1907085552 435 YAHMVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLK 485
Cdd:TIGR01804 420 VADQLEAGTVWINTynLYPAEAP---FGGYKQSGIGREN--GKAALAHYTEVK 467
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
38-488 |
5.32e-89 |
|
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: 279.98 E-value: 5.32e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:cd07150 7 ADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLA 197
Cdd:cd07150 87 ELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 198 KLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANkent 276
Cdd:cd07150 167 EIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD---- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 277 LNQLVG-AAFGA---AGQRCMAlSTAILVGEA--KKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDS 348
Cdd:cd07150 243 LDYAVRaAAFGAfmhQGQICMS-ASRIIVEEPvyDEFVKKFVARASKLKV--GDprDPDTVIGPLISPRQVERIKRQVED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 349 GTKEGASILldgrrikVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTN 428
Cdd:cd07150 320 AVAKGAKLL-------TGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 429 GATARKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 488
Cdd:cd07150 393 LQRAFKLAERLESGMVHINDPTILDEAHVPFGGVKAS--GFGREGGEWSMEEFTELKWIT 450
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
38-488 |
1.56e-88 |
|
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: 279.39 E-value: 1.56e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGktladAEGDVFRGL 117
Cdd:cd07138 22 ATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMG-----APITLARAA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVvehACSVTSLmlgETMPSITKDMDLYSY-------RLPLGVCAGIAPFNFPA-MIPLWMFPmAMVCGNTFLMKPSERV 189
Cdd:cd07138 97 QV---GLGIGHL---RAAADALKDFEFEERrgnslvvREPIGVCGLITPWNWPLnQIVLKVAP-ALAAGCTVVLKPSEVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 190 PGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVM 268
Cdd:cd07138 170 PLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIIL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 269 PDANKENTLNQLVGAAFGAAGQRCMALsTAILVGEAKkwLPELVDRAK----NLRVNAGDQPGADLGPLITPQAKERVCN 344
Cdd:cd07138 250 DDADLEKAVPRGVAACFANSGQSCNAP-TRMLVPRSR--YAEAEEIAAaaaeAYVVGDPRDPATTLGPLASAAQFDRVQG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 345 LIDSGTKEGASiLLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAI 424
Cdd:cd07138 327 YIQKGIEEGAR-LVAGGPGRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYV 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907085552 425 FTTNGATARKYAHMVDVGQVGVNVPIPVPL-PmfsFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 488
Cdd:cd07138 406 WSADPERARAVARRLRAGQVHINGAAFNPGaP---FGGYKQS--GNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
38-488 |
3.08e-88 |
|
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: 278.35 E-value: 3.08e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWA-DTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRG 116
Cdd:cd07109 5 STGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 117 LQVVE-HACSVTSLMlGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATML 195
Cdd:cd07109 85 ARYFEyYGGAADKLH-GETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 196 LAKLLQDSGAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKE 274
Cdd:cd07109 163 LAELAEEAGLPAGALNVVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 275 NTLNQLVGAAFGAAGQRCMALSTaILVGEA--KKWLPELVDRAKNLRVNAG-DQPgaDLGPLITPQAKERVCNLIDSGTK 351
Cdd:cd07109 243 AALPVVVNAIIQNAGQTCSAGSR-LLVHRSiyDEVLERLVERFRALRVGPGlEDP--DLGPLISAKQLDRVEGFVARARA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 352 EGASILLDGRRIKVKgYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAT 431
Cdd:cd07109 320 RGARIVAGGRIAEGA-PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 432 ARKYAHMVDVGQVGVNVPIP---VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 488
Cdd:cd07109 399 ALRVARRLRAGQVFVNNYGAgggIELP---FGGVKKSGHGREK--GLEALYNYTQTKTVA 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
38-447 |
8.24e-88 |
|
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: 277.31 E-value: 8.24e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:cd07145 7 ANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT 193
Cdd:cd07145 87 RLFKLAAEEAKVLRGETIPVdayeYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 194 MLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDAN 272
Cdd:cd07145 167 IELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 273 KENTLNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDS 348
Cdd:cd07145 247 LERAVSIAVRGRFENAGQVCNAVKR-ILVEEevYDKFLKLLVEKVKKLKV--GDplDESTDLGPLISPEAVERMENLVND 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 349 GTKEGASILLDGRRIKvkgyenGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTN 428
Cdd:cd07145 324 AVEKGGKILYGGKRDE------GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND 397
|
410
....*....|....*....
gi 1907085552 429 GATARKYAHMVDVGQVGVN 447
Cdd:cd07145 398 INRALKVARELEAGGVVIN 416
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
38-488 |
1.22e-87 |
|
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: 277.17 E-value: 1.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPA--WADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTL-ADAEGDVf 114
Cdd:cd07091 27 ATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLeESAKGDV- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 115 rglqvvehACSVTSL---------MLGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKP 185
Cdd:cd07091 106 --------ALSIKCLryyagwadkIQGKTIPIDGNFLA-YTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 186 SERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKN 263
Cdd:cd07091 177 AEQTPLSALYLAELIKEAGFPPGVVNIVPGFgPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 264 HGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKER 341
Cdd:cd07091 257 PNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSR-IFVQESiyDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 342 VCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNG 421
Cdd:cd07091 336 ILSYIESGKKEGATLLTGGERHGSKGY----FIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLA 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907085552 422 TAIFTTNGATARKYAHMVDVGQVGVNVpIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 488
Cdd:cd07091 412 AGVFTKDINKALRVSRALKAGTVWVNT-YNVFDAAVPFGGFKQSGFGREL--GEEGLEEYTQVKAVT 475
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
38-489 |
2.79e-86 |
|
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: 273.05 E-value: 2.79e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGl 117
Cdd:cd07092 5 ATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 qVVEH-------ACSVTSLMLGETMPSITKdmdlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP 190
Cdd:cd07092 84 -AVDNfrffagaARTLEGPAAGEYLPGHTS----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 191 GATMLLAKLLQDsGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMP 269
Cdd:cd07092 159 LTTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 270 DANKENTLNQLVGAAFGAAGQRCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLID 347
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTA-ACRVYVHESvyDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 348 sGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTT 427
Cdd:cd07092 317 -RAPAHARVLTGGRRAEGPGY----FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907085552 428 NGATARKYAHMVDVGQVGVNVPIPVPLPMfSFTGSRSSfrGdtnfYGKQ----GIQFYTQLKTITS 489
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEM-PHGGFKQS--G----YGKDlsiyALEDYTRIKHVMV 450
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
38-485 |
2.89e-86 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 274.65 E-value: 2.89e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:PLN02278 48 ATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVPGATMLL 196
Cdd:PLN02278 128 SFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITRKVGP-ALAAGCTVVVKPSELTPLTALAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 197 AKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKEN 275
Cdd:PLN02278 207 AELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 276 TLNQLVGAAFGAAGQRCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEG 353
Cdd:PLN02278 287 AVKGALASKFRNSGQTCVC-ANRILVQEGiyDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 354 ASILLDGRRIKVKgyenGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATAR 433
Cdd:PLN02278 366 AKVLLGGKRHSLG----GTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAW 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907085552 434 KYAHMVDVGQVGVNVPIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 485
Cdd:PLN02278 442 RVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLGREG--SKYGIDEYLEIK 490
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
38-488 |
4.39e-86 |
|
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: 273.55 E-value: 4.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAF-PAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLAdaegdVFRG 116
Cdd:cd07113 23 ATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIH-----LSRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 117 LQVvehACSVTSL---------MLGETM-PSIT----KDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFL 182
Cdd:cd07113 98 FEV---GQSANFLryfagwatkINGETLaPSIPsmqgERYTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 183 MKPSERVPgATML-LAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGA 261
Cdd:cd07113 175 IKPSEFTP-LTLLrVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 262 KNHGVVMPDANKENTLNQLVGAAFGAAGQRCmALSTAILVGEAKkwLPELVD----RAKNLRVNAGDQPGADLGPLITPQ 337
Cdd:cd07113 254 KNAAAFLKDADIDWVVEGLLTAGFLHQGQVC-AAPERFYVHRSK--FDELVTklkqALSSFQVGSPMDESVMFGPLANQP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 338 AKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP 417
Cdd:cd07113 331 HFDKVCSYLDDARAEGDEIVRGGEALAGEGY----FVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTP 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907085552 418 YGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTIT 488
Cdd:cd07113 407 FGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLD-PAVPFGGMKQSGIGRE--FGSAFIDDYTELKSVM 474
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
38-447 |
4.56e-85 |
|
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: 270.60 E-value: 4.56e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADT-SILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRG 116
Cdd:cd07082 24 IDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 117 LQVVEHACSVTSLMLGETMPSITKDMDLYSY----RLPLGVCAGIAPFNFP------AMIPlwmfpmAMVCGNTFLMKPS 186
Cdd:cd07082 104 IDYIRDTIEELKRLDGDSLPGDWFPGTKGKIaqvrREPLGVVLAIGPFNYPlnltvsKLIP------ALIMGNTVVFKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 187 ERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRngKRVQANMGAKNHG 265
Cdd:cd07082 178 TQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 266 VVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVC 343
Cdd:cd07082 256 IVLPDADLELAAKEIVKGALSYSGQRCTAIKR-VLVHEsvADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 344 NLIDSGTKEGASILLDGRRikvkgyENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTA 423
Cdd:cd07082 335 GLIDDAVAKGATVLNGGGR------EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQAS 408
|
410 420
....*....|....*....|....
gi 1907085552 424 IFTTNGATARKYAHMVDVGQVGVN 447
Cdd:cd07082 409 IFTKDINKARKLADALEVGTVNIN 432
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
55-488 |
8.90e-85 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 268.68 E-value: 8.90e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 55 DAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGET 134
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 135 MPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIH 214
Cdd:cd07105 83 IPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 215 GQ----HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 290
Cdd:cd07105 163 HSpedaPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 291 RCMalSTA-ILVGE--AKKWLPELVDRAKNLRvnagdQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRikvKG 367
Cdd:cd07105 243 ICM--STErIIVHEsiADEFVEKLKAAAEKLF-----AGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLA---DE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 368 YENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 447
Cdd:cd07105 313 SPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1907085552 448 VPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 488
Cdd:cd07105 393 GMTVHDEPTLPHGGVKSS--GYGRFNGKWGIDEFTETKWIT 431
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
38-488 |
2.04e-83 |
|
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: 265.76 E-value: 2.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTL-ADAEGDVFRG 116
Cdd:cd07108 5 ATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 117 LQVVEHACSVTSLMLGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLL 196
Cdd:cd07108 85 ADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 197 AKLLQDSgAPDGTLNIIHGQHDAVNF-ICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKEN 275
Cdd:cd07108 164 AEILAQV-LPAGVLNVITGYGEECGAaLVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 276 TLNQLV-GAAFGAAGQRCMAlSTAILVGEA--KKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGT 350
Cdd:cd07108 243 AVDGAIaGMRFTRQGQSCTA-GSRLFVHEDiyDAFLEKLVAKLSKLKI--GDplDEATDIGAIISEKQFAKVCGYIDLGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 351 KE-GASILLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNG 429
Cdd:cd07108 320 STsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDL 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 430 ATARKYAHMVDVGQVGVNVPIpVPLPMFSFTGSRSSFRGDTnfYGKQG-IQFYTQLKTIT 488
Cdd:cd07108 400 GRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLGRE--ASLEGmLEHFTQKKTVN 456
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
38-488 |
2.35e-83 |
|
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: 265.98 E-value: 2.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAF--PAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLA-------- 107
Cdd:cd07139 22 ATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISwsrraqgp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 108 ------DAEGDVFRGLQVVEHacsVTSLMLGETMPSitkdmdlysyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTF 181
Cdd:cd07139 102 gpaallRYYAALARDFPFEER---RPGSGGGHVLVR----------REPVGVVAAIVPWNAPLFLAALKIAPALAAGCTV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 182 LMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGA 261
Cdd:cd07139 169 VLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 262 KNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAILVGEAKK--WLPELVDRAKNLRVNAGDQPGADLGPLITPQAK 339
Cdd:cd07139 249 KSAAIVLDDADLDAAVPGLVPASLMNNGQVCVAL-TRILVPRSRYdeVVEALAAAVAALKVGDPLDPATQIGPLASARQR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 340 ERVCNLIDSGTKEGASILLDGRRikVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYG 419
Cdd:cd07139 328 ERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYG 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 420 NGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVP-LPmfsFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 488
Cdd:cd07139 406 LSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFgAP---FGGFKQS--GIGREGGPEGLDAYLETKSIY 470
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
38-447 |
3.50e-82 |
|
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: 262.70 E-value: 3.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:cd07107 5 ATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLA 197
Cdd:cd07107 85 ALLDYFAGLVTELKGETIPVGGRNL-HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 198 KLLQDSgAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENT 276
Cdd:cd07107 164 ELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 277 LNQLV-GAAFGAAGQRCMALSTAiLVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEG 353
Cdd:cd07107 243 ADAAVaGMNFTWCGQSCGSTSRL-FVHESiyDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 354 ASILLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATAR 433
Cdd:cd07107 322 ARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAH 401
|
410
....*....|....
gi 1907085552 434 KYAHMVDVGQVGVN 447
Cdd:cd07107 402 RTARRVEAGYVWIN 415
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
39-488 |
6.18e-81 |
|
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: 259.29 E-value: 6.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQ 118
Cdd:cd07094 8 DGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 119 VVEHACSVTSLMLGETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATM 194
Cdd:cd07094 88 TLRLAAEEAERIRGEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 195 LLAKLLQDSGAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSrnGKRVQANMGAKNHGVVMPDANK 273
Cdd:cd07094 168 ELAKILVEAGVPEGVLQVVTGErEVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVDRDADL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 274 ENTLNQLVGAAFGAAGQRCMALSTAILVGE-AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKE 352
Cdd:cd07094 246 DAAIEALAKGGFYHAGQVCISVQRIYVHEElYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAVEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 353 GASILLDGRRikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATA 432
Cdd:cd07094 326 GARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 433 RKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSfrgdtnFYGKQGIQF----YTQLKTIT 488
Cdd:cd07094 399 FKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKES------GVGREGVPYameeMTEEKTVV 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
18-488 |
1.95e-80 |
|
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: 258.82 E-value: 1.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 18 VSSKVNATWYPAssfssssvaTNEVVGRVPQSTKAEMDAAVESCKRAF---PAWADTSILSRQQVLLRYQQLIKENLKEI 94
Cdd:cd07141 19 VSGKTFPTINPA---------TGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 95 ARLITLEQGKTLADA-EGDVFRGLQVVEHACSVTSLMLGETMPSitkDMDLYSY-RL-PLGVCAGIAPFNFPAMIPLWMF 171
Cdd:cd07141 90 ASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPM---DGDFFTYtRHePVGVCGQIIPWNFPLLMAAWKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 172 PMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSR 250
Cdd:cd07141 167 APALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 251 -NGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPG 327
Cdd:cd07141 247 sNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCA-GSRTFVQESiyDEFVKRSVERAKKRVVGNPFDPK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 328 ADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLD 407
Cdd:cd07141 326 TEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 408 EAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 487
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGREL--GEYGLQEYTEVKTV 478
|
.
gi 1907085552 488 T 488
Cdd:cd07141 479 T 479
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
39-447 |
5.77e-80 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 258.33 E-value: 5.77e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQ 118
Cdd:PRK03137 60 KSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAID 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 119 VVE-HACSVTSLMLGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLA 197
Cdd:PRK03137 140 FLEyYARQMLKLADGKPVESRPGEHNRYFYI-PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 198 KLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFER------GSRNGKRVQANMGAKNHGVVMPD 270
Cdd:PRK03137 219 EVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFITFTGSREVGLRIYERaakvqpGQIWLKRVIAEMGGKDAIVVDED 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 271 ANKENTLNQLVGAAFGAAGQRCMALSTAILVGEA-KKWLPELVDRAKNLRVNAGDQPgADLGPLITPQAKERVCNLIDSG 349
Cdd:PRK03137 299 ADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVyDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 350 TKEGaSILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNG 429
Cdd:PRK03137 378 KEEG-RLVLGGEGDDSKGY----FIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNR 452
|
410
....*....|....*...
gi 1907085552 430 ATARKYAHMVDVGQVGVN 447
Cdd:PRK03137 453 EHLEKARREFHVGNLYFN 470
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
41-491 |
1.11e-79 |
|
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: 255.68 E-value: 1.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 41 EVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVV 120
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 121 EHACSVTSLMLGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKL 199
Cdd:cd07152 82 HEAAGLPTQPQGEILPSAPGRLS-LARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 200 LQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQ 279
Cdd:cd07152 161 FEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 280 LVGAAFGAAGQRCMAlSTAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIL 357
Cdd:cd07152 241 GAWGAFLHQGQICMA-AGRHLVHEsvADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 358 LDGRRikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAH 437
Cdd:cd07152 320 AGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1907085552 438 MVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGdTNFYGKQGIQFYTQlktitSQW 491
Cdd:cd07152 393 RLRTGMLHINDQTVNDEPHNPFGGMGASGNG-SRFGGPANWEEFTQ-----WQW 440
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
38-487 |
4.28e-79 |
|
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: 255.41 E-value: 4.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPA-WADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTL-ADAEGDVFR 115
Cdd:cd07144 31 STGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYhSNALGDLDE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 116 GLQVVEHACSVTSLMLGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATML 195
Cdd:cd07144 111 IIAVIRYYAGWADKIQGKTIPTSPNKL-AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 196 LAKLLQDSGAPDGTLNIIHGqHDAV--NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANK 273
Cdd:cd07144 190 FANLVKEAGFPPGVVNIIPG-YGAVagSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 274 ENTLNQLVGAAFGAAGQRCMALSTaILVGEA--KKWLPELVDRAK-NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGT 350
Cdd:cd07144 269 DQAVKWAAAGIMYNSGQNCTATSR-IYVQESiyDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 351 KEGASILLDGRRiKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGA 430
Cdd:cd07144 348 KEGAKLVYGGEK-APEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIR 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907085552 431 TARKYAHMVDVGQVGVNVP----IPVPlpmfsFTGSRSSfrGDTNFYGKQGIQFYTQLKTI 487
Cdd:cd07144 427 RAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMS--GIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
38-487 |
4.85e-79 |
|
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: 254.47 E-value: 4.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWA-DTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEG----- 111
Cdd:cd07089 5 ATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAmqvdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 112 --DVFRGlqVVEHACS--------VTSLMLGETMPSITKDmdlysyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTF 181
Cdd:cd07089 85 piGHLRY--FADLADSfpwefdlpVPALRGGPGRRVVRRE--------PVGVVAAITPWNFPFFLNLAKLAPALAAGNTV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 182 LMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMG 260
Cdd:cd07089 155 VLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVgEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 261 AKNHGVVMPDANkentLNQLVGAAFG----AAGQRCmALSTAILVGEAKKwlPELVDRAKN----LRVNAGDQPGADLGP 332
Cdd:cd07089 235 GKSANIVLDDAD----LAAAAPAAVGvcmhNAGQGC-ALTTRLLVPRSRY--DEVVEALAAafeaLPVGDPADPGTVMGP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 333 LITPQAKERVCNLIDSGTKEGASILLDGRRikVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKI 412
Cdd:cd07089 308 LISAAQRDRVEGYIARGRDEGARLVTGGGR--PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRI 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085552 413 VNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 487
Cdd:cd07089 386 ANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINggggYGPDAP-----FGGYKQSGLGRE--NGIEGLEEFLETKSI 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
38-487 |
7.53e-79 |
|
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: 254.06 E-value: 7.53e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPA--WADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADA-EGDVF 114
Cdd:cd07112 10 ATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAlAVDVP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 115 RGLQVVEHACSVTSLMLGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATM 194
Cdd:cd07112 90 SAANTFRWYAEAIDKVYGEVAPTGPDALALIT-REPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 195 LLAKLLQDSGAPDGTLNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDA- 271
Cdd:cd07112 169 RLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADAp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 272 NKENTLNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLID 347
Cdd:cd07112 249 DLDAAAEAAAAGIFWNQGEVCSAGSR-LLVHEsiKDEFLEKVVAAAREWKP--GDplDPATRMGALVSEAHFDKVLGYIE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 348 SGTKEGASILLDGRRIKVKGyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTT 427
Cdd:cd07112 326 SGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTS 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907085552 428 NGATARKYAHMVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 487
Cdd:cd07112 404 DLSRAHRVARRLRAGTVWVNcfdeGDITTP-----FGGFKQSGNGRDK--SLHALDKYTELKTT 460
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
38-488 |
2.23e-78 |
|
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: 252.66 E-value: 2.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDV---- 113
Cdd:cd07110 5 ATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVddva 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 114 -----FRGL--QVVEHAcsvtslmlGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPS 186
Cdd:cd07110 85 gcfeyYADLaeQLDAKA--------ERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 187 ERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNF-ICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHG 265
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGApLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 266 VVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVC 343
Cdd:cd07110 237 IVFDDADLEKAVEWAMFGCFWNNGQICSATSR-LLVHEsiADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 344 NLIDSGTKEGASILLDGRRikVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTA 423
Cdd:cd07110 316 SFIARGKEEGARLLCGGRR--PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907085552 424 IFTTNGATARKYAHMVDVGQVGVNVPIPVpLPMFSFTG-SRSSFRGDtnfYGKQGIQFYTQLKTIT 488
Cdd:cd07110 394 VISRDAERCDRVAEALEAGIVWINCSQPC-FPQAPWGGyKRSGIGRE---LGEWGLDNYLEVKQIT 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
39-490 |
2.30e-78 |
|
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: 253.00 E-value: 2.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQ 118
Cdd:cd07151 19 TGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 119 VVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP--GATmLL 196
Cdd:cd07151 99 ITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPitGGL-LL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 197 AKLLQDSGAPDGTLNIIHGqhdAVNFICD----HPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDAN 272
Cdd:cd07151 178 AKIFEEAGLPKGVLNVVVG---AGSEIGDafveHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDAD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 273 KENTLNQLVGAAFGAAGQRCMALSTaILVGEA--KKWLPELVDRAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDS 348
Cdd:cd07151 255 IDAAVNAAVFGKFLHQGQICMAINR-IIVHEDvyDEFVEKFVERVKALPY--GDPsdPDTVVGPLINESQVDGLLDKIEQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 349 GTKEGASILLDGRRikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTN 428
Cdd:cd07151 332 AVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSD 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907085552 429 GATARKYAHMVDVGQVGVNvPIPV-PLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTITSQ 490
Cdd:cd07151 405 LERGVQFARRIDAGMTHIN-DQPVnDEPHVPFGGEKNS--GLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
38-488 |
4.26e-78 |
|
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: 251.76 E-value: 4.26e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:cd07099 4 ATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGE---TMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATM 194
Cdd:cd07099 84 EAIDWAARNAPRVLAPrkvPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 195 LLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPdIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKE 274
Cdd:cd07099 164 LLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 275 NTLNQLVGAAFGAAGQRCMALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKE 352
Cdd:cd07099 243 RAAAAAVWGAMVNAGQTCISVER-VYVHESvyDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 353 GASILLDGRRIKVKGyengNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATA 432
Cdd:cd07099 322 GAKALTGGARSNGGG----PFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907085552 433 RKYAHMVDVGQVGVN-VPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 488
Cdd:cd07099 398 EAIARRLEAGAVSINdVLLTAGIPALPFGGVKDS--GGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
38-487 |
1.51e-77 |
|
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: 251.29 E-value: 1.51e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAF--PAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKT-LADAEGDVF 114
Cdd:cd07143 30 STGKLITKIAEATEADVDIAVEVAHAAFetDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTfGTAKRVDVQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 115 RGLQVVEHACSVTSLMLGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATM 194
Cdd:cd07143 110 ASADTFRYYGGWADKIHGQVIETDIKKLT-YTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSAL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 195 LLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDAN 272
Cdd:cd07143 189 YMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDAD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 273 KENTLNQLVGAAFGAAGQRCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGT 350
Cdd:cd07143 269 LESAVVWTAYGIFFNHGQVCCA-GSRIYVQEGiyDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 351 KEGASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGA 430
Cdd:cd07143 348 AEGATVETGGKRHGNEGY----FIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNIN 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907085552 431 TARKYAHMVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 487
Cdd:cd07143 424 NAIRVANALKAGTVWVNcynlLHHQVP-----FGGYKQSGIGRE--LGEYALENYTQIKAV 477
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
54-447 |
3.38e-77 |
|
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: 248.53 E-value: 3.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 54 MDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQV----VEHACSvtsl 129
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWIcryyAENAEA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 130 MLgETMPSITKDMDLYSYRLPLGVCAGIAPFNFPamipLW-MF----PMAMVcGNTFLMKPSERVPGATMLLAKLLQDSG 204
Cdd:cd07100 77 FL-ADEPIETDAGKAYVRYEPLGVVLGIMPWNFP----FWqVFrfaaPNLMA-GNTVLLKHASNVPGCALAIEELFREAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 205 APDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAA 284
Cdd:cd07100 151 FPEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 285 FGAAGQRCMAlSTAILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDG 360
Cdd:cd07100 231 LQNAGQSCIA-AKRFIVHEdvYDEFLEKFVEAMAALKV--GDpmDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 361 RRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVD 440
Cdd:cd07100 308 KRPDGPGA----FYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLE 383
|
....*..
gi 1907085552 441 VGQVGVN 447
Cdd:cd07100 384 AGMVFIN 390
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
38-487 |
1.46e-75 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 246.33 E-value: 1.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAE-GDVFRG 116
Cdd:PRK13252 30 ATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSvVDIVTG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 117 LQVVEHACSVTSLMLGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLL 196
Cdd:PRK13252 110 ADVLEYYAGLAPALEGEQIPLRGGSF-VYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 197 AKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENT 276
Cdd:PRK13252 189 AEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 277 LNQLVGAAFGAAGQRCMAlSTAILVGEAKK--WLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKE 352
Cdd:PRK13252 269 ADIAMLANFYSSGQVCTN-GTRVFVQKSIKaaFEARLLERVERIRI--GDpmDPATNFGPLVSFAHRDKVLGYIEKGKAE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 353 GASILLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATA 432
Cdd:PRK13252 346 GARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRA 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907085552 433 RKYAHMVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 487
Cdd:PRK13252 426 HRVIHQLEAGICWINTwgESPAEMP---VGGYKQSGIGREN--GIATLEHYTQIKSV 477
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
39-488 |
4.25e-75 |
|
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: 243.81 E-value: 4.25e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESckrafpAWADTSILSRQQ---VLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFR 115
Cdd:cd07146 8 TGEVVGTVPAGTEEALREALAL------AASYRSTLTRYQrsaILNKAAALLEARREEFARLITLESGLCLKDTRYEVGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 116 GLQVVEHACSVTSLMLGETMPS-IT---KDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPG 191
Cdd:cd07146 82 AADVLRFAAAEALRDDGESFSCdLTangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 192 ATMLLAKLLQDSGAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIfeRGSRNGKRVQANMGAKNHGVVMPD 270
Cdd:cd07146 162 SAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 271 ANKENTLNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLI 346
Cdd:cd07146 240 ADLERAATLAVAGSYANSGQRCTAVKR-ILVHEsvADEFVDLLVEKSAALVV--GDpmDPATDMGTVIDEEAAIQIENRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 347 DSGTKEGASILLDGRRikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFT 426
Cdd:cd07146 317 EEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085552 427 TNGATARKYAHMVDVGQVGVNvpiPVP---LPMFSFTGSRSSFRGdtnfyGKQGIQ----FYTQLKTIT 488
Cdd:cd07146 390 NDLDTIKRLVERLDVGTVNVN---EVPgfrSELSPFGGVKDSGLG-----GKEGVReamkEMTNVKTYS 450
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
39-474 |
1.33e-73 |
|
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: 240.23 E-value: 1.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQ 118
Cdd:cd07147 8 TGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 119 VVEHACSVTSLMLGETMPsitkdMDLYS---------YRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERV 189
Cdd:cd07147 88 TFRIAAEEATRIYGEVLP-----LDISArgegrqglvRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 190 PGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRngKRVQANMGAKNHGVVMP 269
Cdd:cd07147 163 PLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIVDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 270 DANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA--KKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNL 345
Cdd:cd07147 241 DADLDFAAQRIIFGAFYQAGQSCISVQR-VLVHRSvyDEFKSRLVARVKALKT--GDpkDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 346 IDSGTKEGASILLDGRRikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIF 425
Cdd:cd07147 318 VNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1907085552 426 TTNGATARKYAHMVDVGQVGVN-VPipvplpmfsftgsrsSFRGDTNFYG 474
Cdd:cd07147 391 TRDLEKALRAWDELEVGGVVINdVP---------------TFRVDHMPYG 425
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
38-487 |
1.84e-73 |
|
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: 240.71 E-value: 1.84e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGK-----TLAD--AE 110
Cdd:cd07559 24 VNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKpiretLAADipLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 111 GDVFRGLQVVEHACSVTSLMLGETMPSitkdmdlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP 190
Cdd:cd07559 104 IDHFRYFAGVIRAQEGSLSEIDEDTLS-------YHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 191 GATMLLAKLLQDSgAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMP 269
Cdd:cd07559 177 LSILVLMELIGDL-LPKGVVNVVTGFgSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 270 DANKE--NTLNQLVGAAFGAA---GQRCMALSTAiLVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERV 342
Cdd:cd07559 256 DAMDAddDFDDKAEEGQLGFAfnqGEVCTCPSRA-LVQESiyDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 343 CNLIDSGTKEGASILLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGT 422
Cdd:cd07559 335 LSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGG 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907085552 423 AIFTTNGATARKYAHMVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNFygKQGIQFYTQLKTI 487
Cdd:cd07559 415 GVWTRDINRALRVARGIQTGRVWVNCyhQYPAHAP---FGGYKKSGIGRETH--KMMLDHYQQTKNI 476
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
38-451 |
5.21e-72 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 236.73 E-value: 5.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGK----TLAD---AE 110
Cdd:PRK13473 25 ATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKplhlALNDeipAI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 111 GDVFR---GLqvvehACSVTSLMLGETMPSITkdmdlySY--RLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKP 185
Cdd:PRK13473 105 VDVFRffaGA-----ARCLEGKAAGEYLEGHT------SMirRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 186 SERVPGATMLLAKLLQDSgAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNH 264
Cdd:PRK13473 174 SEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 265 GVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERV 342
Cdd:PRK13473 253 VIVFDDADLDAVVEGIRTFGYYNAGQDCTA-ACRIYAQRGiyDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 343 CNLIDSGTKEG-ASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNG 421
Cdd:PRK13473 332 AGFVERAKALGhIRVVTGGEAPDGKGY----YYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLA 407
|
410 420 430
....*....|....*....|....*....|
gi 1907085552 422 TAIFTTNGATARKYAHMVDVGQVGVNVPIP 451
Cdd:PRK13473 408 SSVWTRDVGRAHRVSARLQYGCTWVNTHFM 437
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
38-488 |
6.53e-71 |
|
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: 233.00 E-value: 6.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAF--PAWADTSILsRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFR 115
Cdd:cd07120 5 ATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFEISG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 116 GLQVVEHACSVTSLMLGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATML 195
Cdd:cd07120 84 AISELRYYAGLARTEAGRMIEPEPGSFSLVL-REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 196 LAKLLQD-SGAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANK 273
Cdd:cd07120 163 IIRILAEiPSLPAGVVNLFTESgSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 274 ENTLNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTK 351
Cdd:cd07120 243 DAALPKLERALTIFAGQFCMAGSR-VLVQRsiADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 352 EGASILLDGRRIkVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAT 431
Cdd:cd07120 322 AGAEVVLRGGPV-TEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLAR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907085552 432 ARKYAHMVDVGQVGVNVPIPVpLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 488
Cdd:cd07120 401 AMRVARAIRAGTVWINDWNKL-FAEAEEGGYRQSGLGRLH--GVAALEDFIEYKHIY 454
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
38-487 |
1.23e-69 |
|
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: 230.42 E-value: 1.23e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGK-----TLAD--AE 110
Cdd:cd07117 24 ANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKpiretRAVDipLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 111 GDVFRGLQVVEHACSVTSLMLGETMPSITKdmdlysyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP 190
Cdd:cd07117 104 ADHFRYFAGVIRAEEGSANMIDEDTLSIVL-------REPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 191 GATMLLAKLLQDSgAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMP 269
Cdd:cd07117 177 LSLLELAKIIQDV-LPKGVVNIVTGKgSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 270 DANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLID 347
Cdd:cd07117 256 DANWDKALEGAQLGILFNQGQVCCAGSR-IFVQEGiyDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 348 SGTKEGASILLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTT 427
Cdd:cd07117 335 IAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTK 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907085552 428 NGATARKYAHMVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNFygKQGIQFYTQLKTI 487
Cdd:cd07117 415 DINRALRVARAVETGRVWVNTynQIPAGAP---FGGYKKSGIGRETH--KSMLDAYTQMKNI 471
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
39-487 |
3.57e-68 |
|
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: 226.61 E-value: 3.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFP--AWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAE-GDVFR 115
Cdd:cd07142 28 NGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARyAEVPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 116 GLQVVEHACSVTSLMLGETMPSitkDMDLYSYRL--PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT 193
Cdd:cd07142 108 AARLFRYYAGWADKIHGMTLPA---DGPHHVYTLhePIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 194 MLLAKLLQDSGAPDGTLNIIHGQHDAVNF-ICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDA 271
Cdd:cd07142 185 LLAAKLAAEAGLPDGVLNIVTGFGPTAGAaIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 272 NKENTLNQLVGAAFGAAGQRCMAlSTAILVGEakKWLPELVDRAKN--LRVNAGD--QPGADLGPLITPQAKERVCNLID 347
Cdd:cd07142 265 DVDKAVELAHFALFFNQGQCCCA-GSRTFVHE--SIYDEFVEKAKAraLKRVVGDpfRKGVEQGPQVDKEQFEKILSYIE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 348 SGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTT 427
Cdd:cd07142 342 HGKEEGATLITGGDRIGSKGY----YIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSK 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 428 NGATARKYAHMVDVGQVGVNVpIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 487
Cdd:cd07142 418 NIDTANTLSRALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREK--GIYALNNYLQVKAV 474
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
53-451 |
4.58e-67 |
|
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: 222.15 E-value: 4.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 53 EMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVfrGLQVVEHACSVTSLMlg 132
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEV--AAMAGKIDISIKAYH-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 133 ETMPSITKDMD----LYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDG 208
Cdd:cd07095 77 ERTGERATPMAqgraVLRHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 209 TLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFER-GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 287
Cdd:cd07095 156 VLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 288 AGQRCMALSTAILVG--EAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKv 365
Cdd:cd07095 236 AGQRCTCARRLIVPDgaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 366 kgyENGNFVGPTIIsNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVG 445
Cdd:cd07095 315 ---AGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVN 390
|
....*.
gi 1907085552 446 VNVPIP 451
Cdd:cd07095 391 WNRPTT 396
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
38-449 |
6.89e-67 |
|
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: 223.24 E-value: 6.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:cd07130 20 ANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----GAT 193
Cdd:cd07130 100 DICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPltaiAVT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 194 MLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIfergsrnGKRVQANMGAK-------NHGV 266
Cdd:cd07130 180 KIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQV-------GQAVAARFGRSllelggnNAII 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 267 VMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKERV 342
Cdd:cd07130 253 VMEDADLDLAVRAVLFAAVGTAGQRCTTTRR-LIVHEsiYDEVLERLKKAYKQVRI--GDplDDGTLVGPLHTKAAVDNY 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 343 CNLIDSGTKEGASILLDGRRIKvkgyENGNFVGPTIISnVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGT 422
Cdd:cd07130 330 LAAIEEAKSQGGTVLFGGKVID----GPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSS 404
|
410 420
....*....|....*....|....*....
gi 1907085552 423 AIFTTNGATARKY--AHMVDVGQVGVNVP 449
Cdd:cd07130 405 SIFTTDLRNAFRWlgPKGSDCGIVNVNIG 433
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
37-489 |
2.32e-66 |
|
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: 221.03 E-value: 2.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 37 VATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRG 116
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 117 LQVVEH-ACSVTSLMLGE----TMPSITKDMDLYSyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPG 191
Cdd:cd07101 83 AIVARYyARRAERLLKPRrrrgAIPVLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 192 ATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPD 270
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGPGSEVgGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 271 ANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDS 348
Cdd:cd07101 238 ADLDKAAAGAVRACFSNAGQLCVSIER-IYVHESvyDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 349 GTKEGASILLDGR-RIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTT 427
Cdd:cd07101 317 AVAKGATVLAGGRaRPDLGPY----FYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907085552 428 NGATARKYAHMVDVGQVGVNVPI-----PVPLPMFSFTGSRSSFRgdtnfYGKQGIQFYTQLKTITS 489
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNEGYaaawaSIDAPMGGMKDSGLGRR-----HGAEGLLKYTETQTVAV 454
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
38-447 |
7.13e-66 |
|
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: 220.73 E-value: 7.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADA-EGDVFRG 116
Cdd:cd07111 45 ATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESrDCDIPLV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 117 LQVVEHACSVTSLMlgetmpsitkDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLL 196
Cdd:cd07111 125 ARHFYHHAGWAQLL----------DTELAGWK-PVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 197 AKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENT 276
Cdd:cd07111 194 AEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 277 LNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGA 354
Cdd:cd07111 274 VEGIVDAIWFNQGQVCCAGSR-LLVQEsvAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 355 SILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARK 434
Cdd:cd07111 353 DVFQPGADLPSKGP----FYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALE 428
|
410
....*....|...
gi 1907085552 435 YAHMVDVGQVGVN 447
Cdd:cd07111 429 VALSLKAGVVWIN 441
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
38-487 |
3.79e-65 |
|
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: 217.88 E-value: 3.79e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:cd07102 4 IDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGML 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLA 197
Cdd:cd07102 84 ERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 198 KLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTL 277
Cdd:cd07102 164 AAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 278 NQLVGAAFGAAGQRCMALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGAS 355
Cdd:cd07102 244 ESLVDGAFFNSGQSCCSIER-IYVHESiyDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGAR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 356 ILLDGRRIKVkGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKY 435
Cdd:cd07102 323 ALIDGALFPE-DKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907085552 436 AHMVDVGQVGVNvPIPVPLPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 487
Cdd:cd07102 402 GEQLETGTVFMN-RCDYLDPALAWTGVKDSGRGVT--LSRLGYDQLTRPKSY 450
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
38-451 |
1.87e-64 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 217.29 E-value: 1.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPA-----WADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGD 112
Cdd:PLN02467 31 ATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 113 VFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRL---PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERV 189
Cdd:PLN02467 111 MDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKGYVlkePLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 190 PGATMLLAKLLQDSGAPDGTLNIIHGQ-HDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVM 268
Cdd:PLN02467 191 SVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 269 PDANKENTLNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLI 346
Cdd:PLN02467 271 DDVDLDKAVEWAMFGCFWTNGQICSATSR-LLVHEriASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 347 DSGTKEGASILLDGRRikVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFT 426
Cdd:PLN02467 350 STAKSEGATILCGGKR--PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVIS 427
|
410 420
....*....|....*....|....*
gi 1907085552 427 TNGATARKYAHMVDVGQVGVNVPIP 451
Cdd:PLN02467 428 NDLERCERVSEAFQAGIVWINCSQP 452
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
38-447 |
1.66e-63 |
|
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: 214.09 E-value: 1.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAegdvfrgl 117
Cdd:cd07098 4 ATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDA-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 qvvehacsvtslMLGETMPSITKdMD-------------------LYSYRL------PLGVCAGIAPFNFP------AMI 166
Cdd:cd07098 76 ------------SLGEILVTCEK-IRwtlkhgekalrpesrpgglLMFYKRarveyePLGVVGAIVSWNYPfhnllgPII 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 167 PlwmfpmAMVCGNTFLMKPSERVPGATM----LLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGE 242
Cdd:cd07098 143 A------ALFAGNAIVVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 243 YIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEA--KKWLPELVDRAKNLRV 320
Cdd:cd07098 217 KVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIER-VIVHEKiyDKLLEILTDRVQALRQ 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 321 NAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVV 400
Cdd:cd07098 296 GPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVV 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907085552 401 LETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 447
Cdd:cd07098 376 MKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIN 422
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
85-492 |
7.13e-63 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 210.75 E-value: 7.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 85 QLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPA 164
Cdd:PRK10090 6 AGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 165 -MIPLWMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGE 242
Cdd:PRK10090 86 fLIARKMAP-ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGSVSAGE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 243 YIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRC-MALSTAILVGEAKKWLPELVDRAKNLRV- 320
Cdd:PRK10090 165 KIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCnCAERVYVQKGIYDQFVNRLGEAMQAVQFg 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 321 NAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVV 400
Cdd:PRK10090 245 NPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGY----YYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 401 LETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNvpipvplpmfsftgsRSSFRGDTNFY------- 473
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN---------------RENFEAMQGFHagwrksg 385
|
410 420
....*....|....*....|....
gi 1907085552 474 -----GKQGIQFYTQLKTITSQWK 492
Cdd:PRK10090 386 iggadGKHGLHEYLQTQVVYLQSD 409
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
39-447 |
7.70e-63 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 213.14 E-value: 7.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFP--AWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEG-DVFR 115
Cdd:PLN02766 45 TGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAvDIPA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 116 GLQVVEHACSVTSLMLGETMpSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATML 195
Cdd:PLN02766 125 AAGLLRYYAGAADKIHGETL-KMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 196 LAKLLQDSGAPDGTLNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDANK 273
Cdd:PLN02766 204 YAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 274 ENTLNQLVGAAFGAAGQRCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTK 351
Cdd:PLN02766 284 DMAVDLALLGIFYNKGEICVA-SSRVYVQEGiyDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 352 EGASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAT 431
Cdd:PLN02766 363 EGATLLTGGKPCGDKGY----YIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDV 438
|
410
....*....|....*.
gi 1907085552 432 ARKYAHMVDVGQVGVN 447
Cdd:PLN02766 439 ANTVSRSIRAGTIWVN 454
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
38-487 |
2.07e-62 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 211.68 E-value: 2.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPA--WADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADA-EGDVF 114
Cdd:PRK09847 43 VTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 115 RGLQVVEHACSVTSLMLGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATM 194
Cdd:PRK09847 123 GAARAIRWYAEAIDKVYGEVATTSSHELAMIV-REPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 195 LLAKLLQDSGAPDGTLNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIF-ERGSRNGKRVQANMGAKNHGVVMPDAN 272
Cdd:PRK09847 202 RLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLkDAGDSNMKRVWLEAGGKSANIVFADCP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 273 KentLNQLVGAA----FGAAGQRCMAlSTAILVGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLI 346
Cdd:PRK09847 282 D---LQQAASATaagiFYNQGQVCIA-GTRLLLEEsiADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 347 DSGTKEGaSILLDGRRIKVKGYengnfVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFT 426
Cdd:PRK09847 358 REGESKG-QLLLDGRNAGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWT 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907085552 427 TNGATARKYAHMVDVGQVGVNV----PIPVPlpmfsFTGSRSSFRG-DTNFYgkqGIQFYTQLKTI 487
Cdd:PRK09847 432 RDLSRAHRMSRRLKAGSVFVNNyndgDMTVP-----FGGYKQSGNGrDKSLH---ALEKFTELKTI 489
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
13-485 |
1.18e-61 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 209.38 E-value: 1.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 13 SRILQVSSKVNATWYPASSFSSSSV---ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKE 89
Cdd:PRK11241 6 STLFRQQALINGEWLDANNGEVIDVtnpANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMME 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 90 NLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPL 168
Cdd:PRK11241 86 HQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPaAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 169 WMFPmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFER 247
Cdd:PRK11241 166 KAGP-ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 248 GSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCM-ALSTAILVGEAKKWLPELVDRAKNLRVNAGDQP 326
Cdd:PRK11241 245 CAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVcANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 327 GADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETL 406
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHEL----GGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085552 407 DEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 485
Cdd:PRK11241 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLGREG--SKYGIEDYLEIK 476
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
39-450 |
1.23e-61 |
|
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: 210.13 E-value: 1.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDV----- 113
Cdd:cd07125 56 HERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVreaid 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 114 ---FRGLQVVEhacsvtsLMLGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP 190
Cdd:cd07125 136 fcrYYAAQARE-------LFSDPELPGPTGELNGLELH-GRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 191 GATMLLAKLLQDSGAPDGTLNII------HGQHdavnfICDHPDIKAISFVGSNQAGEYIFE-RGSRNGKRVQ--ANMGA 261
Cdd:cd07125 208 LIAARAVELLHEAGVPRDVLQLVpgdgeeIGEA-----LVAHPRIDGVIFTGSTETAKLINRaLAERDGPILPliAETGG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 262 KNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAILVGE-AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKE 340
Cdd:cd07125 283 KNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEiAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 341 RVCNLIDSGTKEGASI----LLDgrrikvkgyENGNFVGPTIISNVKPSmtCYKEEIFGPVLVVL--ETETLDEAIKIVN 414
Cdd:cd07125 363 LLRAHTELMRGEAWLIapapLDD---------GNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIrfKAEDLDEAIEDIN 431
|
410 420 430
....*....|....*....|....*....|....*.
gi 1907085552 415 DNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPI 450
Cdd:cd07125 432 ATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNI 467
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
37-490 |
2.26e-61 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 209.73 E-value: 2.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 37 VATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVfrg 116
Cdd:PRK09407 39 PFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEV--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 117 LQVVehacsVTSLMLGETMPSITKD----------MDLYSYRLPLGVCAGIAPFNFPA------MIPlwmfpmAMVCGNT 180
Cdd:PRK09407 116 LDVA-----LTARYYARRAPKLLAPrrragalpvlTKTTELRQPKGVVGVISPWNYPLtlavsdAIP------ALLAGNA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 181 FLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIkaISFVGSNQAGEYIFERGSRNGKRVQANM 259
Cdd:PRK09407 185 VVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVgTALVDNADY--LMFTGSTATGRVLAEQAGRRLIGFSLEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 260 GAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEAKK--WLPELVDRAKNLRVNAGDQPGADLGPLITPQ 337
Cdd:PRK09407 263 GGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIER-IYVHESIYdeFVRAFVAAVRAMRLGAGYDYSADMGSLISEA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 338 AKERVCNLIDSGTKEGASILLDGRRIKVKG---YEngnfvgPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVN 414
Cdd:PRK09407 342 QLETVSAHVDDAVAKGATVLAGGKARPDLGplfYE------PTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAN 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085552 415 DNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIpvpLPMFSFTGSRSSFRGDTNF---YGKQGIQFYTQLKTITSQ 490
Cdd:PRK09407 416 DTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGY---AAAWGSVDAPMGGMKDSGLgrrHGAEGLLKYTESQTIATQ 491
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
39-492 |
9.58e-60 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 205.81 E-value: 9.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFP--AWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEG-DVFR 115
Cdd:PLN02466 82 TGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKaELPM 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 116 GLQVVEHACSVTSLMLGETMPSitkDMDLYSYRL--PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT 193
Cdd:PLN02466 162 FARLFRYYAGWADKIHGLTVPA---DGPHHVQTLhePIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 194 MLLAKLLQDSGAPDGTLNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSR-NGKRVQANMGAKNHGVVMPDA 271
Cdd:PLN02466 239 LYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 272 NKENTLNQLVGAAFGAAGQRCMALSTAiLVGEakKWLPELVDRAKN--LRVNAGD--QPGADLGPLITPQAKERVCNLID 347
Cdd:PLN02466 319 DVDKAVELAHFALFFNQGQCCCAGSRT-FVHE--RVYDEFVEKAKAraLKRVVGDpfKKGVEQGPQIDSEQFEKILRYIK 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 348 SGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTT 427
Cdd:PLN02466 396 SGVESGATLECGGDRFGSKGY----YIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQ 471
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907085552 428 NGATARKYAHMVDVGQVGVN------VPIPvplpmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTITSQWK 492
Cdd:PLN02466 472 NLDTANTLSRALRVGTVWVNcfdvfdAAIP-------FGGYKMSGIGREK--GIYSLNNYLQVKAVVTPLK 533
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
38-447 |
1.50e-57 |
|
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: 198.96 E-value: 1.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:cd07083 41 APSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVE-HACSVTSLML-GETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATML 195
Cdd:cd07083 121 DFIRyYARAALRLRYpAVEVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 196 LAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFERGSRNG------KRVQANMGAKNHGVVM 268
Cdd:cd07083 200 VFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLApgqtwfKRLYVETGGKNAIIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 269 PDANKENTLNQLVGAAFGAAGQRCMALSTAILV-GEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLID 347
Cdd:cd07083 280 ETADFELVVEGVVVSAFGFQGQKCSAASRLILTqGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 348 SGTKEGaSILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYGNGTAIF 425
Cdd:cd07083 360 HGKNEG-QLVLGGKRLEGEGY----FVAPTVVEEVPPKARIAQEEIFGPVLSVIryKDDDFAEALEVANSTPYGLTGGVY 434
|
410 420
....*....|....*....|..
gi 1907085552 426 TTNGATARKYAHMVDVGQVGVN 447
Cdd:cd07083 435 SRKREHLEEARREFHVGNLYIN 456
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
38-487 |
2.80e-54 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 189.18 E-value: 2.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVF--- 114
Cdd:PRK09406 9 ATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALkca 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 115 RGLQ-VVEHAcsvtSLMLGETmPSITKDMD----LYSYRlPLGVCAGIAPFNFPamipLWM---FPM-AMVCGNTFLMKP 185
Cdd:PRK09406 89 KGFRyYAEHA----EALLADE-PADAAAVGasraYVRYQ-PLGVVLAVMPWNFP----LWQvvrFAApALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 186 SERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHG 265
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 266 VVMPDANKENTLNQLVGAAFGAAGQRCMALSTAIL---VGEAkkWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERV 342
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVhadVYDA--FAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 343 CNLIDSGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGT 422
Cdd:PRK09406 317 EKQVDDAVAAGATILCGGKRPDGPGW----FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085552 423 AIFTTNGATARKYAHMVDVGQVGVNvPIPVPLPMFSFTGSRSSfrGdtnfYGKQ----GIQFYTQLKTI 487
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPELPFGGVKRS--G----YGRElsahGIREFCNIKTV 454
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
38-447 |
5.80e-53 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 185.84 E-value: 5.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:PRK13968 15 ATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLgETMPSITKDMD-LYSYRlPLGVCAGIAPFNFPamipLWMF-----PMaMVCGNTFLMKPSERVPG 191
Cdd:PRK13968 95 NLCDWYAEHGPAML-KAEPTLVENQQaVIEYR-PLGTILAIMPWNFP----LWQVmrgavPI-LLAGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 192 ATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDA 271
Cdd:PRK13968 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 272 NKENTLNQLVGAAFGAAGQRCMALSTAIL-VGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGT 350
Cdd:PRK13968 248 DLELAVKAAVAGRYQNTGQVCAAAKRFIIeEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 351 KEGASILLDGRRIKVKGyengNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGA 430
Cdd:PRK13968 328 AEGARLLLGGEKIAGAG----NYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
410
....*....|....*..
gi 1907085552 431 TARKYAHMVDVGQVGVN 447
Cdd:PRK13968 404 QARQMAARLECGGVFIN 420
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
39-447 |
7.33e-52 |
|
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: 183.42 E-value: 7.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEG------- 111
Cdd:cd07116 25 TGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAadiplai 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 112 DVFRGLQVVEHACSvtslmlgETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPG 191
Cdd:cd07116 105 DHFRYFAGCIRAQE-------GSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 192 ATMLLAKLLQDSgAPDGTLNIIHG-QHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPD 270
Cdd:cd07116 178 SILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFAD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 271 -ANKENTL--NQLVGAAFGA--AGQRCMALSTAiLVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVC 343
Cdd:cd07116 257 vMDADDAFfdKALEGFVMFAlnQGEVCTCPSRA-LIQESiyDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKIL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 344 NLIDSGTKEGASILLDGRRIKVKGYENGNFVGPTIISNVKpSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTA 423
Cdd:cd07116 336 SYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAG 414
|
410 420
....*....|....*....|....
gi 1907085552 424 IFTTNGATARKYAHMVDVGQVGVN 447
Cdd:cd07116 415 VWTRDGNTAYRMGRGIQAGRVWTN 438
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
38-419 |
1.29e-51 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 182.85 E-value: 1.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVfrGL 117
Cdd:PRK09457 23 VSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEV--TA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLM--LGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATML 195
Cdd:PRK09457 101 MINKIAISIQAYHerTGEKRSEMADGAAVLRHR-PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 196 LAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGeYIFER--GSRNGKRVQANMGAKNHGVVMPDANK 273
Cdd:PRK09457 180 TVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTG-YLLHRqfAGQPEKILALEMGGNNPLVIDEVADI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 274 ENTLNQLVGAAFGAAGQRCMAlSTAILVGEAKK---WLPELVDRAKNLRVNAGD-QPGADLGPLITPQAKERVC----NL 345
Cdd:PRK09457 259 DAAVHLIIQSAFISAGQRCTC-ARRLLVPQGAQgdaFLARLVAVAKRLTVGRWDaEPQPFMGAVISEQAAQGLVaaqaQL 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907085552 346 IDSgtkeGASILLDGRRIKvkgyENGNFVGPTII--SNVK--PSmtcykEEIFGPVLVVLETETLDEAIKIVNDNPYG 419
Cdd:PRK09457 338 LAL----GGKSLLEMTQLQ----AGTGLLTPGIIdvTGVAelPD-----EEYFGPLLQVVRYDDFDEAIRLANNTRFG 402
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
38-447 |
1.75e-49 |
|
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: 176.88 E-value: 1.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAF--PAWA-DTSIlsRQQVLLRYQQLIKENLKEIARLITLEQG--KTL---ADA 109
Cdd:TIGR04284 23 ATEEVLGVAADATAADMDAAIAAARRAFdeTDWSrDTAL--RVRCLRQLRDALRAHVEELRELTIAEVGapRMLtagAQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 110 EGDVFRGLQVVEHACSVT-SLMLGETMPsitkdMDLYSYRL----PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMK 184
Cdd:TIGR04284 101 EGPVDDLGFAADLAESYAwTTDLGVASP-----MGIPTRRTlrreAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 185 PSERVPGATMLLAKLL-QDSGAPDGTLNII-HGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAK 262
Cdd:TIGR04284 176 PAPDTPWCAAVLGELIaEHTDFPPGVVNIVtSSDHRLGALLAKDPRVDMVSFTGSTATGRAVMADAAATLKKVFLELGGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 263 NHGVVMPDANKENTLNQlvgAAFGA---AGQRCmALSTAILVGEAKkwLPELVDRAK----NLRVNAGDQPGADLGPLIT 335
Cdd:TIGR04284 256 SAFIVLDDADLAAACSM---AAFTVcmhAGQGC-AITTRLVVPRAR--YDEAVAAAAatmgSIKPGDPADPGTVCGPVIS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 336 PQAKERVCNLIDSGTKEGASILLDGRRikVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVND 415
Cdd:TIGR04284 330 ARQRDRVQSYLDLAVAEGGRFACGGGR--PADRDRGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIAND 407
|
410 420 430
....*....|....*....|....*....|..
gi 1907085552 416 NPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 447
Cdd:TIGR04284 408 SPYGLSGTVFGADPERAAAVAARVRTGTVNVN 439
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
38-491 |
2.78e-48 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 173.84 E-value: 2.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPA--WADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGK--TLAdAEGDV 113
Cdd:cd07140 29 TDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAvyTLA-LKTHV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 114 FRGLQVVEHACSVTSLMLGETMP--SITKDMDL-YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP 190
Cdd:cd07140 108 GMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 191 GATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIFER-GSRNGKRVQANMGAKNHGVVM 268
Cdd:cd07140 188 LTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGKHIMKScAVSNLKKVSLELGGKSPLIIF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 269 PDANKENTLNQLVGAAFGAAGQRCMAlSTAILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLI 346
Cdd:cd07140 268 ADCDMDKAVRMGMSSVFFNKGENCIA-AGRLFVEESihDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYC 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 347 DSGTKEGASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVV--LETETLDEAIKIVNDNPYGNGTAI 424
Cdd:cd07140 347 ERGVKEGATLVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFGPIMIIskFDDGDVDGVLQRANDTEYGLASGV 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085552 425 FTTNGATARKYAHMVDVGQVGVNV--PIPVPLPMFSFtgSRSSFRGDtnfYGKQGIQFYTQLKTITSQW 491
Cdd:cd07140 423 FTKDINKALYVSDKLEAGTVFVNTynKTDVAAPFGGF--KQSGFGKD---LGEEALNEYLKTKTVTIEY 486
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
38-449 |
1.05e-46 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 170.01 E-value: 1.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 38 ATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGL 117
Cdd:PLN02315 42 ANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEII 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 118 QVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----GAT 193
Cdd:PLN02315 122 DMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPlitiAMT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 194 MLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFER-GSRNGKRVqANMGAKNHGVVMPDAN 272
Cdd:PLN02315 202 KLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTvNARFGKCL-LELSGNNAIIVMDDAD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 273 KENTLNQLVGAAFGAAGQRCMALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGT 350
Cdd:PLN02315 281 IQLAVRSVLFAAVGTAGQRCTTCRR-LLLHESiyDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIK 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 351 KEGASILLDGRRIKvkgyENGNFVGPTIISnVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGA 430
Cdd:PLN02315 360 SQGGKILTGGSAIE----SEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPE 434
|
410 420
....*....|....*....|.
gi 1907085552 431 TARKY--AHMVDVGQVGVNVP 449
Cdd:PLN02315 435 TIFKWigPLGSDCGIVNVNIP 455
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
41-480 |
8.77e-43 |
|
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: 157.97 E-value: 8.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 41 EVVGRVPQSTKAEMDAAVESCKRAF-------PAWADTSILSRQQVLLRyqqlikENLKEIARLITLEQGKTLADAEGDV 113
Cdd:cd07148 10 KPIGEVPTVDWAAIDKALDTAHALFldrnnwlPAHERIAILERLADLME------ERADELALLIAREGGKPLVDAKVEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 114 FRGLQVVEHACSVTSLMLGETMPsitkdMDL---------YSYRLPLGVCAGIAPFNFPA-MIPLWMFPmAMVCGNTFLM 183
Cdd:cd07148 84 TRAIDGVELAADELGQLGGREIP-----MGLtpasagriaFTTREPIGVVVAISAFNHPLnLIVHQVAP-AIAAGCPVIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 184 KPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSrNGKRVqanmgAKN 263
Cdd:cd07148 158 KPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLA-PGTRC-----ALE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 264 HG-----VVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGE--AKKWLPELVDRAKNLRVnaGDQ--PGADLGPLI 334
Cdd:cd07148 232 HGgaapvIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQR-VFVPAeiADDFAQRLAAAAEKLVV--GDPtdPDTEVGPLI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 335 TPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYEngnfvgPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVN 414
Cdd:cd07148 309 RPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTYA------PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQAN 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907085552 415 DNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSfrGdtnfYGKQGIQF 480
Cdd:cd07148 383 SLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQS--G----YGTGGIPY 442
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
45-478 |
1.66e-42 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 158.00 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 45 RVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHAC 124
Cdd:PLN00412 46 KVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 125 SVTSLMLGE-------TMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLA 197
Cdd:PLN00412 126 EEGVRILGEgkflvsdSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 198 KLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNqAGEYIfergSRNGKRV--QANMGAKNHGVVMPDANKE 274
Cdd:PLN00412 206 HCFHLAGFPKGLISCVTGKGSEIgDFLTMHPGVNCISFTGGD-TGIAI----SKKAGMVplQMELGGKDACIVLEDADLD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 275 NTLNQLVGAAFGAAGQRCMALStAILVGE--AKKWLPELVDRAKNLRVNAGDQpGADLGPLITPQAKERVCNLIDSGTKE 352
Cdd:PLN00412 281 LAAANIIKGGFSYSGQRCTAVK-VVLVMEsvADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEK 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 353 GASILLDGRRikvkgyeNGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATA 432
Cdd:PLN00412 359 GATFCQEWKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKA 431
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907085552 433 RKYAHMVDVGQVGVNVPiPVPLP-MFSFTGSRSSfrgdtnFYGKQGI 478
Cdd:PLN00412 432 ILISDAMETGTVQINSA-PARGPdHFPFQGLKDS------GIGSQGI 471
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
40-425 |
8.35e-39 |
|
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: 148.12 E-value: 8.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 40 NEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLK-EIARLITLEQGKTLADAEGDV----- 113
Cdd:cd07123 57 AHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRyELNAATMLGQGKNVWQAEIDAaceli 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 114 --FR----------GLQVVEHACSVTSLMlgetmpsitkdmdlySYRlPL-GVCAGIAPFNFPAM------IPLWMfpma 174
Cdd:cd07123 137 dfLRfnvkyaeelyAQQPLSSPAGVWNRL---------------EYR-PLeGFVYAVSPFNFTAIggnlagAPALM---- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 175 mvcGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGS--------NQAGEYIf 245
Cdd:cd07123 197 ---GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVgDTVLASPHLAGLHFTGStptfkslwKQIGENL- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 246 eRGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTA-ILVGEAKKWLPELVDRAKNLRVNAGD 324
Cdd:cd07123 273 -DRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAyVPESLWPEVKERLLEELKEIKMGDPD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 325 QPGADLGPLITPQAKERVCNLIDSGTKE-GASILLDGRRIKVKGYengnFVGPTIISNVKPSMTCYKEEIFGPVLVVL-- 401
Cdd:cd07123 352 DFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGY----FVEPTVIETTDPKHKLMTEEIFGPVLTVYvy 427
|
410 420
....*....|....*....|....*
gi 1907085552 402 ETETLDEAIKIVND-NPYGNGTAIF 425
Cdd:cd07123 428 PDSDFEETLELVDTtSPYALTGAIF 452
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
39-447 |
1.37e-38 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 150.73 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVfRglq 118
Cdd:PRK11904 572 RRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEV-R--- 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 119 vvE-------HACSVTSLML-GETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP 190
Cdd:PRK11904 648 --EavdfcryYAAQARRLFGaPEKLPGPTGESNELRLH-GRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTP 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 191 GATMLLAKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIfERG--SRNGKRVQ--ANMGAKNHG 265
Cdd:PRK11904 725 LIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIAGVAFTGSTETARII-NRTlaARDGPIVPliAETGGQNAM 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 266 VVMPDANKENTLNQLVGAAFGAAGQRCMALStAILVGE--AKKWLPELVDRAKNLRVnaGD--QPGADLGPLITPQAKER 341
Cdd:PRK11904 804 IVDSTALPEQVVDDVVTSAFRSAGQRCSALR-VLFVQEdiADRVIEMLKGAMAELKV--GDprLLSTDVGPVIDAEAKAN 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 342 VCNLIDSGTKEG---ASILLDGrrikvkGYENGNFVGPTIISnvKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDN 416
Cdd:PRK11904 881 LDAHIERMKREArllAQLPLPA------GTENGHFVAPTAFE--IDSISQLEREVFGPILHVIryKASDLDKVIDAINAT 952
|
410 420 430
....*....|....*....|....*....|.
gi 1907085552 417 PYGNGTAIFTTNGATARKYAHMVDVGQVGVN 447
Cdd:PRK11904 953 GYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
76-447 |
4.71e-37 |
|
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: 141.51 E-value: 4.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 76 RQQVLLRYQQLIKENLKEIARLITLEQGKTLADAE-GDVFRGLQVVEHAC----------SV-TSLMLGETMPSITKDmd 143
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAVVLGEIDHALkhlkkwmkprRVsVPLLLQPAKAYVIPE-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 144 lysyrlPLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGtLNIIHGQHDAVN 221
Cdd:cd07087 100 ------PLGVVLIIGPWNYPLQ--LALAPLigAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEA-VAVVEGGVEVAT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 222 FICDHP-DIkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaIL 300
Cdd:cd07087 171 ALLAEPfDH--IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY-VL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 301 VGEAKKwlPELVDRAKNlRVNA--GDQPG--ADLGPLITPQAKERVCNLIDSGTkegasILLDGRRIKVKGYengnfVGP 376
Cdd:cd07087 248 VHESIK--DELIEELKK-AIKEfyGEDPKesPDYGRIINERHFDRLASLLDDGK-----VVIGGQVDKEERY-----IAP 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907085552 377 TIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP-----YgngtaIFTTNGATARKYAHMVDVGQVGVN 447
Cdd:cd07087 315 TILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPkplalY-----LFSEDKAVQERVLAETSSGGVCVN 385
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
13-447 |
1.35e-35 |
|
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: 138.89 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 13 SRILQVSSKVNA----TWYPASSFSSSSVATNE------------VVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSR 76
Cdd:TIGR01238 19 SELKPLEAQIHAwadkTWQAAPIIGHSYKADGEaqpvtnpadrrdIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 77 QQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSvtslmlgetmpSITKDMDLYSYRlPLGVCAG 156
Cdd:TIGR01238 99 AAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAK-----------QVRDVLGEFSVE-SRGVFVC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 157 IAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVN-FICDHPDIKAISFV 235
Cdd:TIGR01238 167 ISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGaALTSDPRIAGVAFT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 236 GSNQAGEYI----FERGSRNGKRVqANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAILVGE-AKKWLPE 310
Cdd:TIGR01238 247 GSTEVAQLInqtlAQREDAPVPLI-AETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDvADRVLTM 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 311 LVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIlLDGRRIKVKGYENGNFVGPTIISnvKPSMTCYK 390
Cdd:TIGR01238 326 IQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKI-AQLTLDDSRACQHGTFVAPTLFE--LDDIAELS 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907085552 391 EEIFGPVL--VVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 447
Cdd:TIGR01238 403 EEVFGPVLhvVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN 461
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
58-447 |
4.18e-34 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 134.39 E-value: 4.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 58 VESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLadaegdvfRGLQVVEHACSVTSL--MLGE-- 133
Cdd:PTZ00381 13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHP--------FETKMTEVLLTVAEIehLLKHld 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 134 --------TMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLqDSGA 205
Cdd:PTZ00381 85 eylkpekvDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-TKYL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 206 PDGTLNIIHGQHDAVNFICDHP-DIkaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAA 284
Cdd:PTZ00381 164 DPSYVRVIEGGVEVTTELLKEPfDH--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 285 FGAAGQRCMALSTAILVGEAKKwlpELVDRAKNLRVNA-GDQP--GADLGPLITPQAKERVCNLIDSgtkegasillDGR 361
Cdd:PTZ00381 242 FLNAGQTCVAPDYVLVHRSIKD---KFIEALKEAIKEFfGEDPkkSEDYSRIVNEFHTKRLAELIKD----------HGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 362 RIKVKGY--ENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMV 439
Cdd:PTZ00381 309 KVVYGGEvdIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENT 388
|
....*...
gi 1907085552 440 DVGQVGVN 447
Cdd:PTZ00381 389 SSGAVVIN 396
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
55-447 |
1.26e-31 |
|
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: 126.57 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 55 DAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKtlADAEGDVFRGLQVVE---HAC------- 124
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRK--PAAEVDLTEILPVLSeinHAIkhlkkwm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 125 -----SVTSLMLGetmpsiTKDMDLYSyrlPLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLA 197
Cdd:cd07134 79 kpkrvRTPLLLFG------TKSKIRYE---PKGVCLIISPWNYPFN--LAFGPLvsAIAAGNTAILKPSELTPHTSAVIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 198 KLLQDSGAPDgTLNIIHGQHDAVNFICDHPdIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTL 277
Cdd:cd07134 148 KIIREAFDED-EVAVFEGDAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 278 NQLVGAAFGAAGQRCMALSTaILVGEAKKwlPELVDR-----AKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKE 352
Cdd:cd07134 226 KKIAWGKFLNAGQTCIAPDY-VFVHESVK--DAFVEHlkaeiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 353 GASILLDGRRIkvkgyENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATA 432
Cdd:cd07134 303 GAKVEFGGQFD-----AAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANV 377
|
410
....*....|....*
gi 1907085552 433 RKYAHMVDVGQVGVN 447
Cdd:cd07134 378 NKVLARTSSGGVVVN 392
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
39-447 |
6.98e-31 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 127.36 E-value: 6.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVfRglq 118
Cdd:COG4230 580 HSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEV-R--- 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 119 vvE-------HACSVTSLMLGETmpsitkdmdlySYRlPLGVCAGIAPFNFP---------AmiplwmfpmAMVCGNTFL 182
Cdd:COG4230 656 --EavdfcryYAAQARRLFAAPT-----------VLR-GRGVFVCISPWNFPlaiftgqvaA---------ALAAGNTVL 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 183 MKPSERVPgatmLLA----KLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAgeyifergsrnGKRVQA 257
Cdd:COG4230 713 AKPAEQTP----LIAaravRLLHEAGVPADVLQLLPGDGETVgAALVADPRIAGVAFTGSTET-----------ARLINR 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 258 NMGAKNHGVVMPDAnkEnT--LN-----------QLVG----AAFGAAGQRCMALStaIL-VGE--AKKWLPELVDRAKN 317
Cdd:COG4230 778 TLAARDGPIVPLIA--E-TggQNamivdssalpeQVVDdvlaSAFDSAGQRCSALR--VLcVQEdiADRVLEMLKGAMAE 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 318 LRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIlldgRRIKV-KGYENGNFVGPTIISnvKPSMTCYKEEIFGP 396
Cdd:COG4230 853 LRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLV----HQLPLpEECANGTFVAPTLIE--IDSISDLEREVFGP 926
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1907085552 397 VLVVL--ETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN 447
Cdd:COG4230 927 VLHVVryKADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
41-419 |
5.42e-30 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 124.70 E-value: 5.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 41 EVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVfRglQVV 120
Cdd:PRK11809 671 DIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEV-R--EAV 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 121 E----HACSVTSlmlgetmpsitkDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLL 196
Cdd:PRK11809 748 DflryYAGQVRD------------DFDNDTHR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQA 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 197 AKLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEY----IFERGSRNGKRVQ--ANMGAKNHGVVMP 269
Cdd:PRK11809 815 VRILLEAGVPAGVVQLLPGRGETVgAALVADARVRGVMFTGSTEVARLlqrnLAGRLDPQGRPIPliAETGGQNAMIVDS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 270 DANKENTLNQLVGAAFGAAGQRCMALSTAILVGE-AKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDS 348
Cdd:PRK11809 895 SALTEQVVADVLASAFDSAGQRCSALRVLCLQDDvADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQA 974
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907085552 349 GTKEGASILLDGRRiKVKGYENGNFVGPTIISnvKPSMTCYKEEIFGPVLVVL--ETETLDEAIKIVNDNPYG 419
Cdd:PRK11809 975 MRAKGRPVFQAARE-NSEDWQSGTFVPPTLIE--LDSFDELKREVFGPVLHVVryNRNQLDELIEQINASGYG 1044
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
39-419 |
9.19e-30 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 124.21 E-value: 9.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 39 TNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDV----- 113
Cdd:PRK11905 577 HDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVreavd 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 114 ---FRGLQVvehacsvtslmlgetmpsitKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP 190
Cdd:PRK11905 657 flrYYAAQA--------------------RRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTP 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 191 gatmLLA----KLLQDSGAPDGTLNIIHGQHDAV-NFICDHPDIKAISFVGSNQAGEYIfER--GSRNGKRVQ--ANMGA 261
Cdd:PRK11905 717 ----LIAaravRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLI-QRtlAKRSGPPVPliAETGG 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 262 KNHGVVMPDANKEntlnQLVGA----AFGAAGQRCMALStaIL-VGE--AKKWLPELVDRAKNLRVNAGDQPGADLGPLI 334
Cdd:PRK11905 792 QNAMIVDSSALPE----QVVADviasAFDSAGQRCSALR--VLcLQEdvADRVLTMLKGAMDELRIGDPWRLSTDVGPVI 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 335 TPQAKERVCNLIDSGTKEGASIlldgRRIKV-KGYENGNFVGPTIISnvKPSMTCYKEEIFGPVLVVL--ETETLDEAIK 411
Cdd:PRK11905 866 DAEAQANIEAHIEAMRAAGRLV----HQLPLpAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVrfKADELDRVID 939
|
....*...
gi 1907085552 412 IVNDNPYG 419
Cdd:PRK11905 940 DINATGYG 947
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
150-426 |
1.47e-28 |
|
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: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 150 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQdSGAPDGTLNIIHGQHDAVNFICDHPDI 229
Cdd:cd07135 108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVP-KYLDPDAFQVVQGGVPETTALLEQKFD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 230 KaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaILVGEAKkwLP 309
Cdd:cd07135 187 K-IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDY-VLVDPSV--YD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 310 ELVDRAK---NLRVNAGDQPGADLGPLITPQAKERVCNLIDSgTKegASILLDGRRIKVKgyengNFVGPTIISNVKPSM 386
Cdd:cd07135 263 EFVEELKkvlDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT-TK--GKVVIGGEMDEAT-----RFIPPTIVSDVSWDD 334
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907085552 387 TCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFT 426
Cdd:cd07135 335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFT 374
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
52-487 |
6.88e-27 |
|
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: 112.89 E-value: 6.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 52 AEMDAAVESCKRAFPAWadtsilsRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAegdvFRG-LQVVEHACSVTSLM 130
Cdd:cd07137 6 RELRETFRSGRTRSAEW-------RKSQLKGLLRLVDENEDDIFAALRQDLGKPSAES----FRDeVSVLVSSCKLAIKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 131 LGETMPSITKDMDLYSYRL-------PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQ-- 201
Cdd:cd07137 75 LKKWMAPEKVKTPLTTFPAkaeivsePLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPey 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 202 -DSGApdgtLNIIHGQHDAVNFICDHPDIKaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQL 280
Cdd:cd07137 155 lDTKA----IKVIEGGVPETTALLEQKWDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 281 VGAAFGA-AGQRCMALSTaILVGEakKWLPELVDRAKN-LRVNAGDQP--GADLGPLITPQAKERVCNLIDSgTKEGASI 356
Cdd:cd07137 230 AGGKWGCnNGQACIAPDY-VLVEE--SFAPTLIDALKNtLEKFFGENPkeSKDLSRIVNSHHFQRLSRLLDD-PSVADKI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 357 LLDGRRIkvkgyENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYA 436
Cdd:cd07137 306 VHGGERD-----EKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIV 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907085552 437 HMVDVGQVGVN-VPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTI 487
Cdd:cd07137 381 AETSSGGVTFNdTVVQYAIDTLPFGGVGES--GFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
56-409 |
2.19e-26 |
|
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: 111.56 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 56 AAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKT---LADAEGDV--FRGLQVVEHACSVTSLM 130
Cdd:cd07084 3 RALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGwmfAENICGDQvqLRARAFVIYSYRIPHEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 131 LGEtmPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGT 209
Cdd:cd07084 83 GNH--LGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 210 LNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRngKRVQANMGAKNHGVVMPDAN-KENTLNQLVGAAFGAA 288
Cdd:cd07084 161 VTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 289 GQRCMALStAILVGEAKKWLPeLVDRAKNLRVNAGDQpGADLGPLITPQAKERVCNLIDsgtkegasilLDGRRIKVKGY 368
Cdd:cd07084 239 GQKCTAQS-MLFVPENWSKTP-LVEKLKALLARRKLE-DLLLGPVQTFTTLAMIAHMEN----------LLGSVLLFSGK 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1907085552 369 ENGNFVGPTIISNVKPS---MTC---------YKEEIFGPVLVVLETETLDEA 409
Cdd:cd07084 306 ELKNHSIPSIYGACVASalfVPIdeilktyelVTEEIFGPFAIVVEYKKDQLA 358
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
145-434 |
1.07e-25 |
|
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: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 145 YSYRLPLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHDAVNF 222
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQ--LALAPLigAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 223 IC----DHpdikaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTA 298
Cdd:cd07136 172 LLdqkfDY-----IFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVA-PDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 299 ILVGEAKK--WLPELVDRAKNLRvnaGDQP--GADLGPLITPQAKERVCNLIDSGTkegasILLDGrrikvKGYENGNFV 374
Cdd:cd07136 246 VLVHESVKekFIKELKEEIKKFY---GEDPleSPDYGRIINEKHFDRLAGLLDNGK-----IVFGG-----NTDRETLYI 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907085552 375 GPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP-----YgngtaIFTTNGATARK 434
Cdd:cd07136 313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPkplalY-----LFSEDKKVEKK 372
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
150-447 |
1.23e-22 |
|
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: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 150 PLGVCAGIAPFNFP---AMIPLwmfPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHD------AV 220
Cdd:cd07133 101 PLGVVGIIVPWNYPlylALGPL---IAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTGGADvaaafsSL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 221 NFicDHpdikaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMA----L- 295
Cdd:cd07133 177 PF--DH-----LLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVApdyvLv 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 296 ---STAILVGEAKKWL----PELVDraknlrvnagdqpGADLGPLITPQAKERVCNLIDSGTKEGASI---------LLD 359
Cdd:cd07133 250 pedKLEEFVAAAKAAVakmyPTLAD-------------NPDYTSIINERHYARLQGLLEDARAKGARVielnpagedFAA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 360 GRRIkvkgyengnfvGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNP-----YgngtaIFTTNGATARK 434
Cdd:cd07133 317 TRKL-----------PPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPrplalY-----YFGEDKAEQDR 380
|
330
....*....|...
gi 1907085552 435 YAHMVDVGQVGVN 447
Cdd:cd07133 381 VLRRTHSGGVTIN 393
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
56-428 |
1.62e-20 |
|
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: 93.83 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 56 AAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIarLITLEQgktladaegDVFRGLQvvEHACSVTSLMLGETM 135
Cdd:cd07132 2 EAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEI--VEALAK---------DLRKPKF--EAVLSEILLVKNEIK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 136 PSI------------TKDM-----DLYSYRLPLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLL 196
Cdd:cd07132 69 YAIsnlpewmkpepvKKNLatlldDVYIYKEPLGVVLIIGAWNYP--LQLTLVPLvgAIAAGNCVVIKPSEVSPATAKLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 197 AKLLQDSGAPDGTLNIIHGQHDA---VNFICDHpdikaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANK 273
Cdd:cd07132 147 AELIPKYLDKECYPVVLGGVEETtelLKQRFDY-----IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 274 ENTLNQLVGAAFGAAGQRCMA----LSTA----ILVGEAKKWLPELVdraknlrvnaGDQP--GADLGPLITPQAKERVC 343
Cdd:cd07132 222 DVAARRIAWGKFINAGQTCIApdyvLCTPevqeKFVEALKKTLKEFY----------GEDPkeSPDYGRIINDRHFQRLK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 344 NLIDSGTkegasILLDGRrikvkGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVN--DNP---Y 418
Cdd:cd07132 292 KLLSGGK-----VAIGGQ-----TDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINsrEKPlalY 361
|
410
....*....|
gi 1907085552 419 gngtaIFTTN 428
Cdd:cd07132 362 -----VFSNN 366
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
150-487 |
1.57e-18 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 88.18 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 150 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHDAVNFICDHPDI 229
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVVEGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 230 KaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA-AGQRCMALSTAIlvgEAKKWL 308
Cdd:PLN02174 191 K-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYIL---TTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 309 PELVDRAK-NLRVNAGDQP--GADLGPLITPQAKERVCNLIDSgtKEGASILLDGRRikvKGYENGNfVGPTIISNVKPS 385
Cdd:PLN02174 267 PKVIDAMKkELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDE--KEVSDKIVYGGE---KDRENLK-IAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 386 MTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVN-VPIPVPLPMFSFTGSRS 464
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVGE 420
|
330 340
....*....|....*....|...
gi 1907085552 465 SFRGdtNFYGKQGIQFYTQLKTI 487
Cdd:PLN02174 421 SGMG--AYHGKFSFDAFSHKKAV 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
52-447 |
2.71e-15 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 78.23 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 52 AEMDAAVESCKRAFPAWadtsilsRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAegdvFRG-LQVVEHACSVTSLM 130
Cdd:PLN02203 13 AELRETYESGRTRSLEW-------RKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEA----YRDeVGVLTKSANLALSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 131 LGETMPSITKDMDLYSYRL-------PLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQ 201
Cdd:PLN02203 82 LKKWMAPKKAKLPLVAFPAtaevvpePLGVVLIFSSWNFP--IGLSLEPLigAIAAGNAVVLKPSELAPATSAFLAANIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 202 ---DSGApdgtLNIIHGQHDAVNFICDHPDIKaISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENT-- 276
Cdd:PLN02203 160 kylDSKA----VKVIEGGPAVGEQLLQHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSLSSSRDTkv 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 277 -LNQLVGAAFGA-AGQRCMALSTaILVGEakKWLPELVDRAKN-LRVNAGDQPG--ADLGPLITPQAKERVCNLIDSgTK 351
Cdd:PLN02203 235 aVNRIVGGKWGScAGQACIAIDY-VLVEE--RFAPILIELLKStIKKFFGENPResKSMARILNKKHFQRLSNLLKD-PR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 352 EGASILLDGRRikvkgYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGAT 431
Cdd:PLN02203 311 VAASIVHGGSI-----DEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKL 385
|
410
....*....|....*.
gi 1907085552 432 ARKYAHMVDVGQVGVN 447
Cdd:PLN02203 386 KRRILSETSSGSVTFN 401
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
55-414 |
7.66e-13 |
|
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: 70.26 E-value: 7.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 55 DAAVESCKRAFPAWADTSILSRQQVLLRYQQLI---KENLKEIA--------RLITLEQGKT------LADA--EGDVFR 115
Cdd:cd07129 2 DAAAAAAAAAFESYRALSPARRAAFLEAIADEIealGDELVARAhaetglpeARLQGELGRTtgqlrlFADLvrEGSWLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 116 GlqVVEHAcSVTSLMLGEtmpsitkdMDLYSYRLPLGVCAGIAPFNFP-AmiplwmFPM-------AMVCGNTFLMKPSE 187
Cdd:cd07129 82 A--RIDPA-DPDRQPLPR--------PDLRRMLVPLGPVAVFGASNFPlA------FSVaggdtasALAAGCPVVVKAHP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 188 RVPGATMLLAKL----LQDSGAPDGTLNIIHGQHDAVNF-ICDHPDIKAISFVGSNQAGEYIFERGSR--NGKRVQANMG 260
Cdd:cd07129 145 AHPGTSELVARAiraaLRATGLPAGVFSLLQGGGREVGVaLVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 261 AKNHGVVMPDANKEN--TLNQ-LVGAAFGAAGQRCmaLSTAILVGEAKKWLPELVDRAKNLrvnAGDQPGadlGPLITPq 337
Cdd:cd07129 225 SVNPVFILPGALAERgeAIAQgFVGSLTLGAGQFC--TNPGLVLVPAGPAGDAFIAALAEA---LAAAPA---QTMLTP- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 338 akeRVCNLIDSGTKEGASilLDGRRIKVKGY--ENGNFVGPTIisnVKPSMTCY------KEEIFGPVLVVLETETLDEA 409
Cdd:cd07129 296 ---GIAEAYRQGVEALAA--APGVRVLAGGAaaEGGNQAAPTL---FKVDAAAFladpalQEEVFGPASLVVRYDDAAEL 367
|
....*
gi 1907085552 410 IKIVN 414
Cdd:cd07129 368 LAVAE 372
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
95-413 |
8.20e-13 |
|
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: 70.60 E-value: 8.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 95 ARLITLEQGKTLADAEGDVFRGLQVVEHAC--SVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFP 172
Cdd:cd07126 85 ARLIQRVAPKSDAQALGEVVVTRKFLENFAgdQVRFLARSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPALQLM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 173 MAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNG 252
Cdd:cd07126 165 GALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAERLALELHGKV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 253 KRVQANMGAKnhgVVMPDANKENTLN-QLVGAAFGAAGQRCMALStaILVGEaKKWLPE-LVDRAKNLrvnAGDQPGADL 330
Cdd:cd07126 245 KLEDAGFDWK---ILGPDVSDVDYVAwQCDQDAYACSGQKCSAQS--ILFAH-ENWVQAgILDKLKAL---AEQRKLEDL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 331 --GPLITpQAKERVCNLIDSGTK-EGASILLDGRRIKvkgyeNGNFvgPTIISNVKPS------MTCYKE--------EI 393
Cdd:cd07126 316 tiGPVLT-WTTERILDHVDKLLAiPGAKVLFGGKPLT-----NHSI--PSIYGAYEPTavfvplEEIAIEenfelvttEV 387
|
330 340
....*....|....*....|
gi 1907085552 394 FGPVLVVleTETLDEAIKIV 413
Cdd:cd07126 388 FGPFQVV--TEYKDEQLPLV 405
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
152-436 |
7.23e-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: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 152 GVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQhdaVNFICDHPDIK 230
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHLGEQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 231 -AISFVGSNQAGEYIfeRGS----RNGKRVQANMGAKNHGVVMPDANKENT-----LNQLVGAAFGAAGQRCMALSTAIL 300
Cdd:cd07128 223 dVVAFTGSAATAAKL--RAHpnivARSIRFNAEADSLNAAILGPDATPGTPefdlfVKEVAREMTVKAGQKCTAIRRAFV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 301 -------VGEAkkwlpeLVDRAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKG--YE 369
Cdd:cd07128 301 pearvdaVIEA------LKARLAKVVV--GDprLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVGadAE 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907085552 370 NGNFVGPTII--SNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNdnpYGNG---TAIFTTNGATARKYA 436
Cdd:cd07128 373 KGAFFPPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAA---RGRGslvASVVTNDPAFARELV 441
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
51-468 |
2.78e-08 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 56.33 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 51 KAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLI--TLEQGKTLADAEGDVF---RGLQVVEHACS 125
Cdd:cd07127 83 QCDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVmhTTGQAFMMAFQAGGPHaqdRGLEAVAYAWR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 126 VTSLMLGETM---PSITKD---MDLYSYRLPLGVCAGIAPFNFPAmiplW-----MFPmAMVCGNTFLMKPServPGATM 194
Cdd:cd07127 163 EMSRIPPTAEwekPQGKHDplaMEKTFTVVPRGVALVIGCSTFPT----WngypgLFA-SLATGNPVIVKPH---PAAIL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 195 LLA-------KLLQDSG-APD-GTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIfERGSRnGKRVQANMGAKNHG 265
Cdd:cd07127 235 PLAitvqvarEVLAEAGfDPNlVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWL-EANAR-QAQVYTEKAGVNTV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 266 VVmpdankENTlNQLVGA----AFGAA---GQRCMAlSTAILV-------GEAKKWLPELV-DRAKNLRVNAGDQPGAD- 329
Cdd:cd07127 313 VV------DST-DDLKAMlrnlAFSLSlysGQMCTT-PQNIYVprdgiqtDDGRKSFDEVAaDLAAAIDGLLADPARAAa 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 330 -LGPLITPQAKERVcnlidSGTKEGASILLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDE 408
Cdd:cd07127 385 lLGAIQSPDTLARI-----AEARQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDH 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907085552 409 AIKIVNDNPYGNGT---AIFTTNGATARKYAHMVDvgQVGVNVPIPVPLPMF-SFTGSRSSFRG 468
Cdd:cd07127 460 SIELARESVREHGAmtvGVYSTDPEVVERVQEAAL--DAGVALSINLTGGVFvNQSAAFSDFHG 521
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
129-413 |
4.70e-07 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 52.40 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 129 LMLGETMPSITKDmDLYSYR---LPL-GVCAGIAPFNFPAMiPLW-MFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDS 203
Cdd:PRK11903 124 LLRDGEAVQLGKD-PAFQGQhvlVPTrGVALFINAFNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 204 GA-PDGTLNIIHGQH----DAVNfICDhpdikAISFVGSNQAGEYIFERGS--RNGKRVQANMGAKNHGVVMPDANKEnt 276
Cdd:PRK11903 202 GIlPAGALSVVCGSSagllDHLQ-PFD-----VVSFTGSAETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAAPG-- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 277 lnqlvGAAFGA------------AGQRCMALSTaILVGEA--KKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERV 342
Cdd:PRK11903 274 -----SEAFDLfvkevvremtvkSGQKCTAIRR-IFVPEAlyDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAV 347
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907085552 343 CNLIDsGTKEGASILLDGRRIKVKGYEN--GNFVGPTIISNVKP--SMTCYKEEIFGPVLVVLETETLDEAIKIV 413
Cdd:PRK11903 348 RAGLA-ALRAQAEVLFDGGGFALVDADPavAACVGPTLLGASDPdaATAVHDVEVFGPVATLLPYRDAAHALALA 421
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
119-303 |
2.28e-05 |
|
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: 46.83 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 119 VVEHACSVTSLMLGETmpsitkdmdlYSYRLPLGVCAGIAPFNFPAMIPLWMFpMAMVCGNTFLMKPSERVPGATMLLAK 198
Cdd:cd07077 79 SVGHIQDVLLPDNGET----------YVRAFPIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPFTNRALAL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 199 LLQDSGAPDGTLNII----HGQHDAVNFICDHPDIKAISFVGSNQAGEYIfeRGSRNGKRVQAnMGAKNHGVVMPDANKE 274
Cdd:cd07077 148 LFQAADAAHGPKILVlyvpHPSDELAEELLSHPKIDLIVATGGRDAVDAA--VKHSPHIPVIG-FGAGNSPVVVDETADE 224
|
170 180 190
....*....|....*....|....*....|..
gi 1907085552 275 NTLNQLV--GAAF-GAAgqrCMALSTAILVGE 303
Cdd:cd07077 225 ERASGSVhdSKFFdQNA---CASEQNLYVVDD 253
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
54-268 |
2.06e-03 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 40.71 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 54 MDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLAD-------AEGDVFRGLQVVEHACSV 126
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEdkviknhFAAEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907085552 127 TSlmlGETMPSITKDMDlysyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQD---- 202
Cdd:cd07081 81 LT---GDENGGTLIIAE------PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQaava 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907085552 203 SGAPDGTLNIIHGQH-DAVNFICDHPDIKAISFVGsnqaGEYIFERGSRNGKRVQAnMGAKNHGVVM 268
Cdd:cd07081 152 AGAPENLIGWIDNPSiELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIG-VGAGNTPVVI 213
|
|
| |
