|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
4-485 |
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: 805.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 4 VGNFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDEL 83
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 84 AALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEYSFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVA 163
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 164 LACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKR 243
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 244 VQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVAVGDEtADRLIERLKPLIAALRIGPGELRGKDene 323
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDE-ADEWIPKLVERAKKLKVGAGDDPGAD--- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 324 MGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATA 403
Cdd:cd07085 317 MGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 404 ISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAFHSFGGWKRSVFGALNVHGPDGVRFYTRMKTVTS 483
Cdd:cd07085 397 IAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTS 476
|
..
gi 446372874 484 RW 485
Cdd:cd07085 477 RW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
4-485 |
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: 601.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 4 VGNFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDEL 83
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 84 AALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEYSFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVA 163
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 164 LACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKR 243
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 244 VQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVAVGDetADRLIERLKPLIAALRIGPGELRGKDene 323
Cdd:TIGR01722 241 VQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGA--ADEWVPEIRERAEKIRIGPGDDPGAE--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 324 MGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATA 403
Cdd:TIGR01722 316 MGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 404 ISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAFHSFGGWKRSVFGALNVHGPDGVRFYTRMKTVTS 483
Cdd:TIGR01722 396 IALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTT 475
|
..
gi 446372874 484 RW 485
Cdd:TIGR01722 476 RW 477
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
2-485 |
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: 581.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 2 ETVGNFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRD 81
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 82 ELAALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEYSFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFP 161
Cdd:COG1012 84 ELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 162 VALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHC-GNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAH 240
Cdd:COG1012 164 PALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGdGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 241 GKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVAVgDETADRLIERLKPLIAALRIGPGElrgKD 320
Cdd:COG1012 244 LKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVH-ESIYDEFVERLVAAAKALKVGDPL---DP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 321 ENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRnysVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDY 400
Cdd:COG1012 320 GTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGR---RPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 401 ATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAFHSFGGWKRSVFGALnvHGPDGVRFYTRMKT 480
Cdd:COG1012 397 EEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGRE--GGREGLEEYTETKT 474
|
....*
gi 446372874 481 VTSRW 485
Cdd:COG1012 475 VTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
15-481 |
1.13e-176 |
|
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: 504.37 E-value: 1.13e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 15 SSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKV 94
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 95 WSDALGELTRGIEVVEFACGIPHLSKGEySFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKP 174
Cdd:pfam00171 83 LAEARGEVDRAIDVLRYYAGLARRLDGE-TLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 175 PALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNH 253
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTgSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 254 AIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGElrgKDENEMGPVVSRAHQ 333
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLL-VHESIYDEFVEKLVEAAKKLKVGDPL---DPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 334 QKVLGYIDKGVSEGATLVMDGRnysvAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFG 413
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGE----AGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446372874 414 NGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAFHSFGGWKRSVFGALNvhGPDGVRFYTRMKTV 481
Cdd:pfam00171 394 LAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
4-499 |
2.90e-168 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 488.49 E-value: 2.90e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 4 VGNFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDEL 83
Cdd:PLN02419 114 VPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 84 AALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEYSFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVA 163
Cdd:PLN02419 194 AMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 164 LACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKR 243
Cdd:PLN02419 274 VTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 244 VQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVAVGDETA--DRLIERLKpliaALRIGPGElrgKDE 321
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSweDKLVERAK----ALKVTCGS---EPD 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 322 NEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYA 401
Cdd:PLN02419 427 ADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFD 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 402 TAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAFHSFGGWKRSVFGALNVHGPDGVRFYTRMKTV 481
Cdd:PLN02419 507 EAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLV 586
|
490
....*....|....*...
gi 446372874 482 TSRWPNGQQIVSeFSMPT 499
Cdd:PLN02419 587 TQKQKDIHSPFS-LAIPI 603
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
45-482 |
3.28e-143 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 418.15 E-value: 3.28e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 45 AAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEYS 124
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 125 FNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHC 204
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 205 -GNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMA 283
Cdd:cd07078 162 dGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 284 lPVVVAVGDETADRLIERLKPLIAALRIGPGElrgKDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGrnySVAGYP 363
Cdd:cd07078 242 -ASRLLVHESIYDEFVERLVERVKALKVGNPL---DPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGG---KRLEGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 364 EGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIP 443
Cdd:cd07078 315 KGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*....
gi 446372874 444 VPVPMAFHSFGGWKRSVFGAlnVHGPDGVRFYTRMKTVT 482
Cdd:cd07078 395 SVGAEPSAPFGGVKQSGIGR--EGGPYGLEEYTEPKTVT 431
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-481 |
1.55e-136 |
|
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: 402.40 E-value: 1.55e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 6 NFIHGKttLSSSGETLPVTNPA-TGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELA 84
Cdd:cd07097 3 NYIDGE--WVAGGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 85 ALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEYSFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVAL 164
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 165 ACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFN-VVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKR 243
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNlVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 244 VQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMA---LPVVVAVGDETADRLIERLKpliaALRIGPGElrgKD 320
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTAssrLIVTEGIHDRFVEALVERTK----ALKVGDAL---DE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 321 ENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRnySVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDY 400
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGE--RLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 401 ATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVpVPMAFHS-FGGWKRSVFGALNvHGPDGVRFYTRMK 479
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPT-AGVDYHVpFGGRKGSSYGPRE-QGEAALEFYTTIK 469
|
..
gi 446372874 480 TV 481
Cdd:cd07097 470 TV 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
6-482 |
4.65e-124 |
|
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: 370.91 E-value: 4.65e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 6 NFIHGKTTLSSSGETLPVTNPATGK-VIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELA 84
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 85 ALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEysfNVGSGV---DSFSLMQPLGVVAGITPFNFPAMVPMWMFP 161
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGE---TVPSELpnkDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 162 VALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAH 240
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHgRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 241 GKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMA---LPVVVAVGDETADRLIERLKpliaALRIGPGeLR 317
Cdd:cd07131 238 NKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTAtsrLIVHESVYDEFLKRFVERAK----RLRVGDG-LD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 318 gkDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRV 397
Cdd:cd07131 313 --EETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 398 PDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAFHSFGGWKRSVFGaLNVHGPDGVRFYTR 477
Cdd:cd07131 391 SSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNG-HREAGTTALDAFTE 469
|
....*
gi 446372874 478 MKTVT 482
Cdd:cd07131 470 WKAVY 474
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
6-482 |
5.02e-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: 347.63 E-value: 5.02e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 6 NFIHGKTTlSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAA 85
Cdd:cd07086 1 GVIGGEWV-GSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 86 LIVSEHGKVWSDALGELTRGIEVVEFACGiphLSKGEYSFNVGS---GVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPV 162
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVG---LSRMLYGLTIPSerpGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 163 ALACGNTFVLKPPALVPSASLRMAQLLQEA----GLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTAS 238
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 239 AHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGElr 317
Cdd:cd07086 237 RRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLI-VHESVYDEFLERLVKAYKQVRIGdPLD-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 318 gkDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRnySVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRV 397
Cdd:cd07086 314 --EGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGK--RIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 398 PDYATAISTVNSHEFGNGSVIFTTNGHYAREF--AQSVEAGMVGINIP---VPVPMAF----HSfGGWKRSvfgalnvhG 468
Cdd:cd07086 390 DSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPtsgAEIGGAFggekET-GGGRES--------G 460
|
490
....*....|....
gi 446372874 469 PDGVRFYTRMKTVT 482
Cdd:cd07086 461 SDAWKQYMRRSTCT 474
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
23-482 |
6.70e-115 |
|
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: 346.34 E-value: 6.70e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 23 VTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGEL 102
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 103 TRGIEVVE-FACGIPHLSkGEYSFNVGSGVDSFSLMQPLGVVAGITPFNFP-AMV-----PmwmfpvALACGNTFVLKPP 175
Cdd:cd07103 81 DYAASFLEwFAEEARRIY-GRTIPSPAPGKRILVIKQPVGVVAAITPWNFPaAMItrkiaP------ALAAGCTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 176 ALVPSASLRMAQLLQEAGLPDGVFNVVHC-GNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVqAF---Gaak 251
Cdd:cd07103 154 EETPLSALALAELAEEAGLPAGVLNVVTGsPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRV-SLelgG--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 252 nHA--IVMPDADLDATVNAIMGGAFGSAGERCMAlPVVVAVGDETADRLIERLKPLIAALRIGPgelrGKDEN-EMGPVV 328
Cdd:cd07103 230 -NApfIVFDDADLDKAVDGAIASKFRNAGQTCVC-ANRIYVHESIYDEFVEKLVERVKKLKVGN----GLDEGtDMGPLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 329 SRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYpegFYvGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVN 408
Cdd:cd07103 304 NERAVEKVEALVEDAVAKGAKVLTGGKRLGLGGY---FY-EPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARAN 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446372874 409 SHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVP-VPMAfhSFGGWKRSVFGALNvhGPDGVRFYTRMKTVT 482
Cdd:cd07103 380 DTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLIsDAEA--PFGGVKESGLGREG--GKEGLEEYLETKYVS 450
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
23-481 |
2.22e-113 |
|
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: 342.61 E-value: 2.22e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 23 VTNPATGKVIRQVTQSTREEMLAAIQSAHEAF--PAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALG 100
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 101 ELTRGIEVVEFACG---------IPhLSKGEYsfnvgsgvDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFV 171
Cdd:cd07114 81 QVRYLAEWYRYYAGladkiegavIP-VDKGDY--------LNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 172 LKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAA 250
Cdd:cd07114 152 LKPSEHTPASTLELAKLAEEAGFPPGVVNVVTgFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 251 KNHAIVMPDADLDATVNAIMGGAFGSAGERCMA---LPVVVAVGDETADRLIERLKpliaALRIGPGElrgKDENEMGPV 327
Cdd:cd07114 232 KSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAgsrLLVQRSIYDEFVERLVARAR----AIRVGDPL---DPETQMGPL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 328 VSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTV 407
Cdd:cd07114 305 ATERQLEKVERYVARAREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALA 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446372874 408 NSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINI-PVPVPMAfhSFGGWKRSVFGALNvhGPDGVRFYTRMKTV 481
Cdd:cd07114 385 NDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNTyRALSPSS--PFGGFKDSGIGREN--GIEAIREYTQTKSV 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
23-482 |
6.41e-113 |
|
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: 341.47 E-value: 6.41e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 23 VTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGK-VWSDALGE 101
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKpITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 102 LTRGIEVVE-FACGIPHLskGEYSFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPS 180
Cdd:cd07093 81 IPRAAANFRfFADYILQL--DGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 181 ASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPD 259
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHgFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 260 ADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGElrgkDENEMGPVVSRAHQQKVLG 338
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRIL-VQRSIYDEFLERFVERAKALKVGdPLD----PDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 339 YIDKGVSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVI 418
Cdd:cd07093 314 YVELARAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446372874 419 FTTNGHYAREFAQSVEAGMVGINIP----VPVPmafhsFGGWKRSVFGALNvhGPDGVRFYTRMKTVT 482
Cdd:cd07093 394 WTRDLGRAHRVARRLEAGTVWVNCWlvrdLRTP-----FGGVKASGIGREG--GDYSLEFYTELKNVC 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
48-482 |
1.10e-110 |
|
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: 332.66 E-value: 1.10e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 48 QSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEYSFNV 127
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 128 GSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHC-GN 206
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGgGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 207 EAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPV 286
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 287 VVAVGDEtADRLIERLKpliaalrigpgelrgkdenemgpvvsrahqqkvlgyidkgvsegatlvmdgrnysvagypegf 366
Cdd:cd06534 241 LLVHESI-YDEFVEKLV--------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 367 yvggTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPV 446
Cdd:cd06534 257 ----TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIG 332
|
410 420 430
....*....|....*....|....*....|....*.
gi 446372874 447 PMAFHSFGGWKRSVFGALnvHGPDGVRFYTRMKTVT 482
Cdd:cd06534 333 VGPEAPFGGVKNSGIGRE--GGPYGLEEYTRTKTVV 366
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
7-481 |
8.80e-109 |
|
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: 331.15 E-value: 8.80e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAAL 86
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 87 IVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEYSFNVGSGVDSFSLMQPLGVVAGITPFNFP-AMVPMWMFPvALA 165
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPfFLIARKLAP-ALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 166 CGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHC-GNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRV 244
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 245 QAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMAlPVVVAVGDETADRLIERLKPLIAALRIG-PGElrgkDENE 323
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTC-AERVYVHEDIYDEFMEKLVEKMKAVKVGdPFD----AATD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 324 MGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGypeGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATA 403
Cdd:cd07088 315 MGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEK---GYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446372874 404 ISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPM-AFHSfgGWKRSVFGALNvhGPDGVRFYTRMKTV 481
Cdd:cd07088 392 IELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMqGFHA--GWKKSGLGGAD--GKHGLEEYLQTKVV 466
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
21-462 |
6.38e-108 |
|
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: 328.52 E-value: 6.38e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 21 LPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALG 100
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 101 ELTRGIEVVEFACGIPHLSKGEYSFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPS 180
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 181 ASLRMAQLLQEAGLPDGVFNVV-HCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPD 259
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVtGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 260 ADLDATVNAIMGGAFGSAGERCMA---LPVVVAVGDETADRLIERlkplIAALRIgpGELRGKDeNEMGPVVSRAHQQKV 336
Cdd:cd07150 241 ADLDYAVRAAAFGAFMHQGQICMSasrIIVEEPVYDEFVKKFVAR----ASKLKV--GDPRDPD-TVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 337 LGYIDKGVSEGATLVmdgrnysVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGS 416
Cdd:cd07150 314 KRQVEDAVAKGAKLL-------TGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSA 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446372874 417 VIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAFHSFGGWKRSVFG 462
Cdd:cd07150 387 AILTNDLQRAFKLAERLESGMVHINDPTILDEAHVPFGGVKASGFG 432
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-481 |
1.43e-104 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 321.06 E-value: 1.43e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 1 METVGNFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHR 80
Cdd:PRK13252 4 QPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 81 DELAALIVSEHGKVWSDAL-GELTRGIEVVEFACGIPHLSKGEY-SFNVGSGVdsFSLMQPLGVVAGITPFNFPAMVPMW 158
Cdd:PRK13252 84 DELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQiPLRGGSFV--YTRREPLGVCAGIGAWNYPIQIACW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 159 MFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTAS 238
Cdd:PRK13252 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 239 AHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMAlPVVVAVGDETADRLIERLKPLIAALRIG-Pgelr 317
Cdd:PRK13252 242 ASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTN-GTRVFVQKSIKAAFEARLLERVERIRIGdP---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 318 gKDEN-EMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVR 396
Cdd:PRK13252 317 -MDPAtNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 397 VPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINI----PVPVPmafhsFGGWKRSVFGALNvhGPDGV 472
Cdd:PRK13252 396 FDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgesPAEMP-----VGGYKQSGIGREN--GIATL 468
|
....*....
gi 446372874 473 RFYTRMKTV 481
Cdd:PRK13252 469 EHYTQIKSV 477
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
23-481 |
2.16e-104 |
|
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: 319.63 E-value: 2.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 23 VTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGEL 102
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 103 TRGIEVVEFACGIPHLSKGEySFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSAS 182
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGE-HVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 183 LRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADL 262
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 263 DATVNAIMGGAFGSAGERCM-ALPVVVAVG--DETADRLIERLKpliaALRIGPGELrgkDENEMGPVVSRAHQQKVLGY 339
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSnGTRVFVQRSikDEFTERLVERTK----KIRIGDPLD---EDTQMGALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 340 IDKGVSEGATLVMDGRNYSV-AGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVI 418
Cdd:cd07090 313 IESAKQEGAKVLCGGERVVPeDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446372874 419 FTTNGHYAREFAQSVEAGMVGIN----IPVPVPmafhsFGGWKRSVFGALNvhGPDGVRFYTRMKTV 481
Cdd:cd07090 393 FTRDLQRAHRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
4-482 |
1.06e-103 |
|
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: 318.38 E-value: 1.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 4 VGNFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWS--KMTPLRRARILFEFKVLLEKHRD 81
Cdd:cd07091 4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWwrKMDPRERGRLLNKLADLIERDRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 82 ELAALIVSEHGK-VWSDALGELTRGIEVVEFACGIPHLSKGEySFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMF 160
Cdd:cd07091 84 ELAALESLDNGKpLEESAKGDVALSIKCLRYYAGWADKIQGK-TIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 161 PVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASA 239
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPgFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 240 HG-KRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGELRG 318
Cdd:cd07091 243 SNlKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIF-VQESIYDEFVEKFKARAEKRVVGDPFDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 319 kdeNEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYpegfYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVP 398
Cdd:cd07091 322 ---TFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGY----FIQPTVFTDVKDDMKIAKEEIFGPVVTILKFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 399 DYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGIN----IPVPVPmafhsFGGWKRSVFGALNvhGPDGVRF 474
Cdd:cd07091 395 TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNtynvFDAAVP-----FGGFKQSGFGREL--GEEGLEE 467
|
....*...
gi 446372874 475 YTRMKTVT 482
Cdd:cd07091 468 YTQVKAVT 475
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
17-485 |
2.55e-103 |
|
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: 318.78 E-value: 2.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 17 SGETLPVTNPA-TGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVW 95
Cdd:cd07124 44 TEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNW 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 96 SDALGELTRGIEVVEFACGIPHLSKGeYSFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPP 175
Cdd:cd07124 124 AEADADVAEAIDFLEYYAREMLRLRG-FPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 176 ALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTAS------AHGKRVQAFG 248
Cdd:cd07124 203 EDTPVIAAKLVEILEEAGLPPGVVNFLPgPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkvqpgqKWLKRVIAEM 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 249 AAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVAVgDETADRLIERLKPLIAALRIGPGELRgkdENEMGPVV 328
Cdd:cd07124 283 GGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVH-ESVYDEFLERLVERTKALKVGDPEDP---EVYMGPVI 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 329 SRAHQQKVLGYIDKGVSEGaTLVMDGRnySVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVN 408
Cdd:cd07124 359 DKGARDRIRRYIEIGKSEG-RLLLGGE--VLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIAN 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446372874 409 SHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPM-AFHSFGGWKRSVFGALNvHGPDGVRFYTRMKTVTSRW 485
Cdd:cd07124 436 DTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALvGRQPFGGFKMSGTGSKA-GGPDYLLQFMQPKTVTENF 512
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
5-485 |
1.17e-102 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 315.92 E-value: 1.17e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 5 GNFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAF-PAWSKMTPLRRARILFEFKVLLEKHRDEL 83
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 84 AALIVSEHGKvwsdaLGELTRGIEV---VEF----------------ACGIPHLSKGEYSfnvgsgvdSFSLMQPLGVVA 144
Cdd:cd07113 81 AQLETLCSGK-----SIHLSRAFEVgqsANFlryfagwatkingetlAPSIPSMQGERYT--------AFTRREPVGVVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 145 GITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFV 224
Cdd:cd07113 148 GIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 225 GSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCmALPVVVAVGDETADRLIERLKP 304
Cdd:cd07113 228 GSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVC-AAPERFYVHRSKFDELVTKLKQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 305 LIAALRIGPgelrGKDENEM-GPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSvagyPEGFYVGGTLFDNVTPEMTIW 383
Cdd:cd07113 307 ALSSFQVGS----PMDESVMfGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA----GEGYFVQPTLVLARSADSRLM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 384 REEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGIN----IPVPVPmafhsFGGWKRS 459
Cdd:cd07113 379 REETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmhtfLDPAVP-----FGGMKQS 453
|
490 500
....*....|....*....|....*.
gi 446372874 460 VFGalNVHGPDGVRFYTRMKTVTSRW 485
Cdd:cd07113 454 GIG--REFGSAFIDDYTELKSVMIRY 477
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
25-481 |
3.64e-101 |
|
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: 311.30 E-value: 3.64e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 25 NPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALG-ELT 103
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 104 RGIEVVEFACGIPHLSKGEySFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSASL 183
Cdd:cd07115 83 RAADTFRYYAGWADKIEGE-VIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 184 RMAQLLQEAGLPDGVFNVVHC-GNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADL 262
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 263 DATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGElrgkDENEMGPVVSRAHQQKVLGYID 341
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLL-VHESIYDEFLERFTSLARSLRPGdPLD----PKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 342 KGVSEGATLVMDGRNYSvagyPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTT 421
Cdd:cd07115 317 VGREEGARLLTGGKRPG----ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446372874 422 NGHYAREFAQSVEAGMVGIN----IPVPVPmafhsFGGWKRSVFGalNVHGPDGVRFYTRMKTV 481
Cdd:cd07115 393 DLGRAHRVAAALKAGTVWINtynrFDPGSP-----FGGYKQSGFG--REMGREALDEYTEVKSV 449
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
7-482 |
1.91e-99 |
|
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: 307.19 E-value: 1.91e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAF--PAWSKMTPLRRARILFEFKVLLEKHRDELA 84
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 85 ALIVSEHGKVWS--------------DALGELTRGIEVVEfacgiPHLSKGeysfnvgsGVDSFSLMQPLGVVAGITPFN 150
Cdd:cd07139 82 RLWTAENGMPISwsrraqgpgpaallRYYAALARDFPFEE-----RRPGSG--------GGHVLVRREPVGVVAAIVPWN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 151 FPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVA 230
Cdd:cd07139 149 APLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 231 EHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALR 310
Cdd:cd07139 229 RRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRIL-VPRSRYDEVVEALAAAVAALK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 311 IG-PGElrgkDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRnySVAGYPEGFYVGGTLFDNVTPEMTIWREEIFG 389
Cdd:cd07139 308 VGdPLD----PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGG--RPAGLDRGWFVEPTLFADVDNDMRIAQEEIFG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 390 PVLGIVRVPDYATAISTVNSHEFG-NGSViFTTNGHYAREFAQSVEAGMVGINIPvpvPMAFHS-FGGWKRSVFGalNVH 467
Cdd:cd07139 382 PVLSVIPYDDEDDAVRIANDSDYGlSGSV-WTADVERGLAVARRIRTGTVGVNGF---RLDFGApFGGFKQSGIG--REG 455
|
490
....*....|....*
gi 446372874 468 GPDGVRFYTRMKTVT 482
Cdd:cd07139 456 GPEGLDAYLETKSIY 470
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
7-481 |
6.93e-99 |
|
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: 306.16 E-value: 6.93e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAF--PAWSKMTPLRRARILFEFKVLLEKHRDELA 84
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 85 ALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEySFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVAL 164
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGE-VYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 165 ACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKR 243
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTgSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 244 VQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGElrgKDENE 323
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLL-VEESIHDKFVAALAERAKKIKLGNGL---DADTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 324 MGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATA 403
Cdd:cd07119 316 MGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 404 ISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINipvpvpmAFH------SFGGWKRSVFG-ALnvhGPDGVRFYT 476
Cdd:cd07119 396 IRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN-------DYHpyfaeaPWGGYKQSGIGrEL---GPTGLEEYQ 465
|
....*
gi 446372874 477 RMKTV 481
Cdd:cd07119 466 ETKHI 470
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
23-481 |
9.31e-99 |
|
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: 305.32 E-value: 9.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 23 VTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWS-KMTPLRRARILFEFKVLLEKHRDELAALIVSEHGkvwsdALGE 101
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVG-----APVM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 102 LTRGIEVVEFACGIPH----LSKGEYSFNVGSGVDSFSLMQ------PLGVVAGITPFNFPAMVPMWMFPVALACGNTFV 171
Cdd:cd07089 76 TARAMQVDGPIGHLRYfadlADSFPWEFDLPVPALRGGPGRrvvrrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 172 LKPPALVPSASLRMAQLLQEAGLPDGVFNVV-HCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAA 250
Cdd:cd07089 156 LKPAPDTPLSALLLGEIIAETDLPAGVVNVVtGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 251 KNHAIVMPDADLDATVNAIMGGAFGSAGERCmALPVVVAVGDETADRLIERLKPLIAALRIG----PGelrgkdeNEMGP 326
Cdd:cd07089 236 KSANIVLDDADLAAAAPAAVGVCMHNAGQGC-ALTTRLLVPRSRYDEVVEALAAAFEALPVGdpadPG-------TVMGP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 327 VVSRAHQQKVLGYIDKGVSEGATLVMDGRnySVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAIST 406
Cdd:cd07089 308 LISAAQRDRVEGYIARGRDEGARLVTGGG--RPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRI 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446372874 407 VNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINiPVPVPMAFHSFGGWKRSVFGALNvhGPDGVRFYTRMKTV 481
Cdd:cd07089 386 ANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN-GGGGYGPDAPFGGYKQSGLGREN--GIEGLEEFLETKSI 457
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
45-465 |
5.40e-98 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 302.14 E-value: 5.40e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 45 AAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEYS 124
Cdd:cd07104 4 RAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 125 FNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKP-PALVPSASLRMAQLLQEAGLPDGVFNVVH 203
Cdd:cd07104 84 PSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPdSRTPVTGGLLIAEIFEEAGLPKGVLNVVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 204 C-GNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCM 282
Cdd:cd07104 164 GgGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 283 ALPVVVaVGDETADRLIERLKPLIAALRIgpGELRGKDeNEMGPVVSRAHQQKVLGYIDKGVSEGATLVmdgrnysVAGY 362
Cdd:cd07104 244 AAGRIL-VHESVYDEFVEKLVAKAKALPV--GDPRDPD-TVIGPLINERQVDRVHAIVEDAVAAGARLL-------TGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 363 PEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINI 442
Cdd:cd07104 313 YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420
....*....|....*....|....
gi 446372874 443 PvPVPMAFH-SFGGWKRSVFGALN 465
Cdd:cd07104 393 Q-TVNDEPHvPFGGVKASGGGRFG 415
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
23-484 |
1.40e-96 |
|
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: 299.68 E-value: 1.40e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 23 VTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGEL 102
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 103 TRGIEVVEFACGIPHLSKGEySFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSAS 182
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGE-TIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 183 LRMAQLLQEAgLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDAD 261
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPgDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 262 LDATVNAIMGGA-FGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGElrgKDENEMGPVVSRAHQQKVLGYI 340
Cdd:cd07107 239 PEAAADAAVAGMnFTWCGQSCGSTSRLF-VHESIYDEVLARVVERVAAIKVGDPT---DPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 341 DKGVSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFT 420
Cdd:cd07107 315 DSAKREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 421 TNGHYAREFAQSVEAGMVGIN------IPVPvpmafhsFGGWKRSVFGalNVHGPDGVRFYTRMKTVTSR 484
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINgssrhfLGAP-------FGGVKNSGIG--REECLEELLSYTQEKNVNVR 455
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
23-482 |
8.36e-96 |
|
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: 297.34 E-value: 8.36e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 23 VTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGEL 102
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 103 TRGIEVVEFACGIPHLSKGEYSFNVGSGVDSFS---LMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVP 179
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKarvRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 180 SASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMP 258
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTgTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 259 DADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGELRGKDeneMGPVVSRAHQQKVLG 338
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLL-VHESIADAFLERLATAAEAIRVGDPLEEGVR---LGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 339 YIDKGVSEGATLVMDGRNysVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVI 418
Cdd:cd07110 317 FIARGKEEGARLLCGGRR--PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446372874 419 FTTNGHYAREFAQSVEAGMVGINIPVPVpMAFHSFGGWKRSVFG-ALnvhGPDGVRFYTRMKTVT 482
Cdd:cd07110 395 ISRDAERCDRVAEALEAGIVWINCSQPC-FPQAPWGGYKRSGIGrEL---GEWGLDNYLEVKQIT 455
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-481 |
9.41e-96 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 298.91 E-value: 9.41e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAAL 86
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 87 IVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEYSFNVGSGVDSFSLMQPLGVVAGITPFNFP-AMVPMWMFPvALA 165
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITRKVGP-ALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 166 CGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVhCGNEAA---SLLTSdPRVQAVSFVGSSAVAEHIYTTASAHGK 242
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVV-MGDAPEigdALLAS-PKVRKITFTGSTAVGKKLMAGAAATVK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 243 RVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGELRGKDen 322
Cdd:PLN02278 265 RVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVT-- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 323 eMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYpegFYVgGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYAT 402
Cdd:PLN02278 342 -QGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGT---FYE-PTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEE 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446372874 403 AISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVpVPMAFHSFGGWKRSVFGalNVHGPDGVRFYTRMKTV 481
Cdd:PLN02278 417 AIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLG--REGSKYGIDEYLEIKYV 492
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
6-459 |
9.50e-95 |
|
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: 295.18 E-value: 9.50e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 6 NFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAA 85
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 86 LIVSEHGkvwsdALGELTRGIEVvefACGIPHLSK-----GEYSFNVGSGvDSFSLMQPLGVVAGITPFNFPAMVPMWMF 160
Cdd:cd07138 81 AITLEMG-----APITLARAAQV---GLGIGHLRAaadalKDFEFEERRG-NSLVVREPIGVCGLITPWNWPLNQIVLKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 161 PVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASA 239
Cdd:cd07138 152 APALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNgDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 240 HGKRV-QAFGAaKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGElrg 318
Cdd:cd07138 232 TVKRVaLELGG-KSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRML-VPRSRYAEAEEIAAAAAEAYVVGDPR--- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 319 KDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGrnysvAGYPE----GFYVGGTLFDNVTPEMTIWREEIFGPVLGI 394
Cdd:cd07138 307 DPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG-----PGRPEglerGYFVKPTVFADVTPDMTIAREEIFGPVLSI 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446372874 395 VRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAfhSFGGWKRS 459
Cdd:cd07138 382 IPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGA--PFGGYKQS 444
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
21-459 |
1.59e-94 |
|
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: 294.26 E-value: 1.59e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 21 LPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALG 100
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 101 ELTRGIEVVEFACGIPHLSKGE------YSFNVGSGVdsFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKP 174
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGEtipvdaYEYNERRIA--FTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 175 PALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNH 253
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTgYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 254 AIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PgelrgKDEN-EMGPVVSRA 331
Cdd:cd07145 239 MIVLKDADLERAVSIAVRGRFENAGQVCNAVKRIL-VEEEVYDKFLKLLVEKVKKLKVGdP-----LDEStDLGPLISPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 332 HQQKVLGYIDKGVSEGATLVMDGRNysvagyPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHE 411
Cdd:cd07145 313 AVERMENLVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTE 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446372874 412 FGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAFHSFGGWKRS 459
Cdd:cd07145 387 YGLQASVFTNDINRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKS 434
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
18-481 |
1.92e-94 |
|
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: 294.12 E-value: 1.92e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 18 GETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPA--WSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVW 95
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 96 SDALGeltrgIEVVEFACGIPH----LSK--GEYSfNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNT 169
Cdd:cd07112 81 SDALA-----VDVPSAANTFRWyaeaIDKvyGEVA-PTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 170 FVLKPPALVPSASLRMAQLLQEAGLPDGVFNVV-HCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTAS-AHGKRVQAF 247
Cdd:cd07112 155 VVLKPAEQSPLTALRLAELALEAGLPAGVLNVVpGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNLKRVWLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 248 GAAKNHAIVMPDA-DLDATVNAIMGGAFGSAGERCMA---LPVVVAVGDETADRLIERLKpliaalrigpgELRGKD--- 320
Cdd:cd07112 235 CGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAgsrLLVHESIKDEFLEKVVAAAR-----------EWKPGDpld 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 321 -ENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGypEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPD 399
Cdd:cd07112 304 pATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 400 YATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGIN------IPVPvpmafhsFGGWKRSVFGA-LNVHGPDGv 472
Cdd:cd07112 382 EEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNcfdegdITTP-------FGGFKQSGNGRdKSLHALDK- 453
|
....*....
gi 446372874 473 rfYTRMKTV 481
Cdd:cd07112 454 --YTELKTT 460
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
16-481 |
2.67e-94 |
|
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: 294.09 E-value: 2.67e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 16 SSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPL-RRARILFEFKVLLEKHRDELAALIVSEHGKV 94
Cdd:cd07082 13 SSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLeERIDCLHKFADLLKENKEEVANLLMWEIGKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 95 WSDALGELTRGIEVVEFACG-----IPHLSKGEySFNVGSGVDSFSLMQPLGVVAGITPFNFP------AMVPmwmfpvA 163
Cdd:cd07082 93 LKDALKEVDRTIDYIRDTIEelkrlDGDSLPGD-WFPGTKGKIAQVRREPLGVVLAIGPFNYPlnltvsKLIP------A 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 164 LACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHC-GNEAASLLTSDPRVQAVSFVGSSAVAEHIytTASAHGK 242
Cdd:cd07082 166 LIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGNRL--KKQHPMK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 243 RVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGELRGKDen 322
Cdd:cd07082 244 RLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVL-VHESVADELVELLKEEVAKLKVGMPWDNGVD-- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 323 eMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGrnysvaGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYAT 402
Cdd:cd07082 321 -ITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 403 AISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGIN---------IPvpvpmafhsFGGWKRSVFGALNVHgpDGVR 473
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINskcqrgpdhFP---------FLGRKDSGIGTQGIG--DALR 462
|
....*...
gi 446372874 474 FYTRMKTV 481
Cdd:cd07082 463 SMTRRKGI 470
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
5-481 |
7.90e-94 |
|
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: 293.16 E-value: 7.90e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 5 GNFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPA-WSKMTPLRRARILFEFKVLLEKHRDEL 83
Cdd:cd07144 9 GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 84 AALIVSEHGKVW-SDALGELTRGIEVVEFACGIPHLSKGEySFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPV 162
Cdd:cd07144 89 AAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGK-TIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 163 ALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHG 241
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPgYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 242 KRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIA-ALRIGPGElrgKD 320
Cdd:cd07144 248 KAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIY-VQESIYDKFVEKFVEHVKqNYKVGSPF---DD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 321 ENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGyPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDY 400
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGL-GKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 401 ATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGIN------IPVPvpmafhsFGGWKRSVFGalNVHGPDGVRF 474
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINssndsdVGVP-------FGGFKMSGIG--RELGEYGLET 473
|
....*..
gi 446372874 475 YTRMKTV 481
Cdd:cd07144 474 YTQTKAV 480
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
26-482 |
8.97e-94 |
|
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: 292.32 E-value: 8.97e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 26 PATGKVIRQVTQSTREEMLAAIQSAHEAFPA--WSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGELT 103
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 104 RGIEVVEFACGIPHLSKGEYSFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSASL 183
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 184 RMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADL 262
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTgYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 263 DATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGpgeLRGKDENEMGPVVSRAHQQKVLGYIDK 342
Cdd:cd07118 244 DAAADAVVFGVYFNAGECCNSGSRLL-VHESIADAFVAAVVARSRKVRVG---DPLDPETKVGAIINEAQLAKITDYVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 343 GVSEGATLVMDGrnySVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTN 422
Cdd:cd07118 320 GRAEGATLLLGG---ERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446372874 423 GHYAREFAQSVEAGMVGINI----PVPVPmafhsFGGWKRSVFGALNvhGPDGVRFYTRMKTVT 482
Cdd:cd07118 397 IDTALTVARRIRAGTVWVNTfldgSPELP-----FGGFKQSGIGREL--GRYGVEEYTELKTVH 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
21-482 |
9.04e-89 |
|
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: 279.10 E-value: 9.04e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 21 LPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALG 100
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 101 ELTRGIEVVEFACGIPHLSKGE-YSFNVGSGVDS---FSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPA 176
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGEtIPFDASPGGEGrigFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 177 LVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTAsahGKRVQAFGAAKNHA- 254
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTgSGETVGDALVTDPRVRMISFTGSPAVGEAIARKA---GLKKVTLELGSNAAv 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 255 IVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGElrgkDENEMGPVVSRAHQ 333
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCISVQRIF-VHEDIYDEFLERFVAATKKLVVGdPLD----EDTDVGPMISEAEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 334 QKVLGYIDKGVSEGATLVmdgrnysVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFG 413
Cdd:cd07149 313 ERIEEWVEEAVEGGARLL-------TGGKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 414 NGSVIFTTNGHYAREFAQSVEAGMVGIN-IP------VPvpmafhsFGGWKRSVFGAlnvhgpDGVRF----YTRMKTVT 482
Cdd:cd07149 386 LQAGVFTNDLQKALKAARELEVGGVMINdSStfrvdhMP-------YGGVKESGTGR------EGPRYaieeMTEIKLVC 452
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
23-483 |
1.10e-88 |
|
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: 278.83 E-value: 1.10e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 23 VTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDAL-GE 101
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 102 LTRGIEVVEFACG----IPHLSKGEYSfnvgSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPAL 177
Cdd:cd07092 81 LPGAVDNFRFFAGaartLEGPAAGEYL----PGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 178 VPSASLRMAQLLQEaGLPDGVFNVVHCGNEAA-SLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIV 256
Cdd:cd07092 157 TPLTTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 257 MPDADLDATVNAIMGGAFGSAGERCMAlPVVVAVGDETADRLIERLKPLIAALRIGPGElrgKDENEMGPVVSRAHQQKV 336
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTA-ACRVYVHESVYDEFVAALVEAVSAIRVGDPD---DEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 337 LGYIDKgVSEGATLVMDGRnysvAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGS 416
Cdd:cd07092 312 AGFVER-APAHARVLTGGR----RAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLAS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446372874 417 VIFTTNGHYAREFAQSVEAGMVGIN--IPVPVPMafhSFGGWKRSVFGALNvhGPDGVRFYTRMKTVTS 483
Cdd:cd07092 387 SVWTRDVGRAMRLSARLDFGTVWVNthIPLAAEM---PHGGFKQSGYGKDL--SIYALEDYTRIKHVMV 450
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
23-482 |
3.30e-88 |
|
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: 278.09 E-value: 3.30e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 23 VTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGK-VWSDALGE 101
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNaLRTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 102 LTRGIEVVEFACGIPHLSKGEySFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSA 181
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGE-TLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 182 SLRMAQLLQEAgLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDA 260
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITgYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 261 DLDATVN-AIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PgelrgKDE-NEMGPVVSRAHQQKVL 337
Cdd:cd07108 239 DLDDAVDgAIAGMRFTRQGQSCTAGSRLF-VHEDIYDAFLEKLVAKLSKLKIGdP-----LDEaTDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 338 GYIDKGVSE-GATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGS 416
Cdd:cd07108 313 GYIDLGLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 417 VIFTTNGHYAREFAQSVEAGMVGINIPVpVPMAFHSFGGWKRSVFG---ALnvhgpDG-VRFYTRMKTVT 482
Cdd:cd07108 393 YVWTRDLGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLGreaSL-----EGmLEHFTQKKTVN 456
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
19-485 |
4.71e-88 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 279.13 E-value: 4.71e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 19 ETLPVTNPA-TGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSD 97
Cdd:PRK03137 50 DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 98 ALGELTRGI--------EVVEFACGIPHLSK-GEysfnvgsgvDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGN 168
Cdd:PRK03137 130 ADADTAEAIdfleyyarQMLKLADGKPVESRpGE---------HNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 169 TFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTAS------AHG 241
Cdd:PRK03137 201 TVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPgSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAkvqpgqIWL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 242 KRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVAVgDETADRLIERLKPLIAALRIGPGElrgkDE 321
Cdd:PRK03137 281 KRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVH-EDVYDEVLEKVVELTKELTVGNPE----DN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 322 NEMGPVVSRAHQQKVLGYIDKGVSEGaTLVMDGRnysvAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYA 401
Cdd:PRK03137 356 AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGE----GDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 402 TAISTVNSHEFG-NGSVIFTTNGH--YARE--------FAQSVEAGMVGinipvpvpmaFHSFGGWKRSVFGAlNVHGPD 470
Cdd:PRK03137 431 HALEIANNTEYGlTGAVISNNREHleKARRefhvgnlyFNRGCTGAIVG----------YHPFGGFNMSGTDS-KAGGPD 499
|
490
....*....|....*
gi 446372874 471 GVRFYTRMKTVTSRW 485
Cdd:PRK03137 500 YLLLFLQAKTVSEMF 514
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
23-482 |
6.92e-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: 276.81 E-value: 6.92e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 23 VTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPA-WSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGE 101
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 102 LTRGIEVVEFACGIPHLSKGEySFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSA 181
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGE-TIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 182 SLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDA 260
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTgLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 261 DLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGElrgkDENEMGPVVSRAHQQKVLGYI 340
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLL-VHRSIYDEVLERLVERFRALRVGPGL----EDPDLGPLISAKQLDRVEGFV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 341 DKGVSEGATLVMDGRNYSVAgYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFT 420
Cdd:cd07109 315 ARARARGARIVAGGRIAEGA-PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWT 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446372874 421 TNGHYAREFAQSVEAGMVGIN-------IPVPvpmafhsFGGWKRSVFGalNVHGPDGVRFYTRMKTVT 482
Cdd:cd07109 394 RDGDRALRVARRLRAGQVFVNnygagggIELP-------FGGVKKSGHG--REKGLEALYNYTQTKTVA 453
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
23-481 |
7.34e-88 |
|
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: 276.72 E-value: 7.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 23 VTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGEL 102
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 103 TRGIEVVEFACGI-----------PHLSKGEYsfnvgsgvdsfslmQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFV 171
Cdd:cd07106 81 GGAVAWLRYTASLdlpdeviedddTRRVELRR--------------KPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 172 LKPPALVPSASLRMAQLLQEAgLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAK 251
Cdd:cd07106 147 LKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 252 NHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGElrgKDENEMGPVVSRA 331
Cdd:cd07106 226 DAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLY-VHESIYDEFCEALVALAKAAVVGDGL---DPGTTLGPVQNKM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 332 HQQKVLGYIDKGVSEGATLVMDGRNYSVAGYpegfYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHE 411
Cdd:cd07106 302 QYDKVKELVEDAKAKGAKVLAGGEPLDGPGY----FIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSE 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446372874 412 FGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPV-PMAfhSFGGWKRSVFGAlnVHGPDGVRFYTRMKTV 481
Cdd:cd07106 378 YGLGASVWSSDLERAEAVARRLEAGTVWINTHGALdPDA--PFGGHKQSGIGV--EFGIEGLKEYTQTQVI 444
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
6-485 |
2.44e-86 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 273.71 E-value: 2.44e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 6 NFIHGKTtLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAA 85
Cdd:PRK13473 5 LLINGEL-VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 86 LIVSEHGKVWSDALG-ELTRGIEVVEFACG----IPHLSKGEYSfnvgSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMF 160
Cdd:PRK13473 84 LESLNCGKPLHLALNdEIPAIVDVFRFFAGaarcLEGKAAGEYL----EGHTSMIRRDPVGVVASIAPWNYPLMMAAWKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 161 PVALACGNTFVLKPPALVPSASLRMAQLLQEAgLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASA 239
Cdd:PRK13473 160 APALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTgRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 240 HGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMAlPVVVAVGDETADRLIERLKPLIAALRIGPGElrgK 319
Cdd:PRK13473 239 SVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTA-ACRIYAQRGIYDDLVAKLAAAVATLKVGDPD---D 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 320 DENEMGPVVSRAHQQKVLGYIDKGVSEG-ATLVMDGRnysVAGYPeGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVP 398
Cdd:PRK13473 315 EDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGE---APDGK-GYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 399 DYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGIN--IPVPVPMAfHsfGGWKRSVFGA-LNVhgpDGVRFY 475
Cdd:PRK13473 391 DEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNthFMLVSEMP-H--GGQKQSGYGKdMSL---YGLEDY 464
|
490
....*....|
gi 446372874 476 TRMKTVTSRW 485
Cdd:PRK13473 465 TVVRHVMVKH 474
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
45-482 |
5.80e-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: 5.80e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 45 AAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHG--KVWSDALGELtrGIEVVEFACGIPHLSKGE 122
Cdd:cd07105 4 QAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGatAAWAGFNVDL--AAGMLREAASLITQIIGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 123 YSFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVV 202
Cdd:cd07105 82 SIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 203 HCGNEAAS----LLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAG 278
Cdd:cd07105 162 THSPEDAPevveALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 279 ERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGELrgkdenemGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNys 358
Cdd:cd07105 242 QICMSTERII-VHESIADEFVEKLKAAAEKLFAGPVVL--------GSLVSAAAADRVKELVDDALSKGAKLVVGGLA-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 359 vAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMV 438
Cdd:cd07105 311 -DESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 446372874 439 GINIPVPVPMAFHSFGGWKRSVFGALNvhGPDGVRFYTRMKTVT 482
Cdd:cd07105 390 HINGMTVHDEPTLPHGGVKSSGYGRFN--GKWGIDEFTETKWIT 431
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
21-482 |
2.83e-84 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 267.76 E-value: 2.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 21 LPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALG 100
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 101 ELTRGIEVVEFACGIPHLSKGEY-SFNVGSGVDS---FSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPA 176
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEiPLDATQGSDNrlaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 177 LVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIytTASAHGKRVQAFGAAKNHAI 255
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTgEREVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 256 VMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGElrgkDENEMGPVVSRAHQQ 334
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIY-VHEELYDEFIEAFVAAVKKLKVGdPLD----EDTDVGPLISEEAAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 335 KVLGYIDKGVSEGATLVMdgrnysvAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGN 414
Cdd:cd07094 314 RVERWVEEAVEAGARLLC-------GGERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGL 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446372874 415 GSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAFHSFGGWKRSVFGAlnvhgpDGVRF----YTRMKTVT 482
Cdd:cd07094 387 QAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGR------EGVPYameeMTEEKTVV 452
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
25-482 |
4.38e-84 |
|
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: 267.29 E-value: 4.38e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 25 NPATGKVIRQVTQSTREEMLAAIQSAHEAF--PAWSKmTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGEL 102
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 103 TRGIEVVEFACGiphLSKGEYSFNVGSGVDSFSLM--QPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPS 180
Cdd:cd07120 82 SGAISELRYYAG---LARTEAGRMIEPEPGSFSLVlrEPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 181 ASLRMAQLLQEA-GLPDGVFNVV-HCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMP 258
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFtESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 259 DADLDATVNAIMGGAFGSAGERCMA---LPVVVAVGDETADRLIERLkpliAALRIGPGELRGkdeNEMGPVVSRAHQQK 335
Cdd:cd07120 239 DADLDAALPKLERALTIFAGQFCMAgsrVLVQRSIADEVRDRLAARL----AAVKVGPGLDPA---SDMGPLIDRANVDR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 336 VLGYIDKGVSEGATLVMDGRNySVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNG 415
Cdd:cd07120 312 VDRMVERAIAAGAEVVLRGGP-VTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446372874 416 SVIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAFHsFGGWKRSVFGALnvHGPDGVRFYTRMKTVT 482
Cdd:cd07120 391 ASVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAE-EGGYRQSGLGRL--HGVAALEDFIEYKHIY 454
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
16-465 |
5.28e-84 |
|
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: 267.25 E-value: 5.28e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 16 SSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVW 95
Cdd:cd07151 7 TSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 96 SDALGELTRGIEVVEFACGIPHLSKGEYSFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPP 175
Cdd:cd07151 87 IKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 176 ALVP-SASLRMAQLLQEAGLPDGVFNVV-HCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNH 253
Cdd:cd07151 167 SDTPiTGGLLLAKIFEEAGLPKGVLNVVvGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 254 AIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGElrgkDENEMGPVVSRAH 332
Cdd:cd07151 247 FVVLEDADIDAAVNAAVFGKFLHQGQICMAINRII-VHEDVYDEFVEKFVERVKALPYGdPSD----PDTVVGPLINESQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 333 QQKVLGYIDKGVSEGATLVmdgrnysVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEF 412
Cdd:cd07151 322 VDGLLDKIEQAVEEGATLL-------VGGEAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEY 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 446372874 413 GNGSVIFTTNGHYAREFAQSVEAGMVGIN-IPVPvPMAFHSFGGWKRSVFGALN 465
Cdd:cd07151 395 GLSGAVFTSDLERGVQFARRIDAGMTHINdQPVN-DEPHVPFGGEKNSGLGRFN 447
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
5-462 |
3.04e-82 |
|
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: 263.05 E-value: 3.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 5 GNFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELA 84
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 85 ALIVSEHGKvwsdALGElTRGIEV---VE----FACGIphlSKGEYSFNVgsgVD----SFSLMQPLGVVAGITPFNFPA 153
Cdd:cd07559 82 VAETLDNGK----PIRE-TLAADIplaIDhfryFAGVI---RAQEGSLSE---IDedtlSYHFHEPLGVVGQIIPWNFPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 154 MVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAgLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEH 232
Cdd:cd07559 151 LMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTgFGSEAGKPLASHPRIAKLAFTGSTTVGRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 233 IYTTASAH---------GKRVQAFGAaknHAIVMPDADLDATVNAIMGGAFGSaGERCMAlPVVVAVGDETADRLIERLK 303
Cdd:cd07559 230 IMQYAAENlipvtlelgGKSPNIFFD---DAMDADDDFDDKAEEGQLGFAFNQ-GEVCTC-PSRALVQESIYDEFIERAV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 304 PLIAALRIG-PGElrgkDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTI 382
Cdd:cd07559 305 ERFEAIKVGnPLD----PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 383 WREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPmAFHSFGGWKRSVFG 462
Cdd:cd07559 381 FQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYP-AHAPFGGYKKSGIG 459
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
45-481 |
1.83e-81 |
|
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: 259.31 E-value: 1.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 45 AAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGEltrgievVEFACGI--------P 116
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAE-------VEKCAWIcryyaenaE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 117 HLSKGEYsFNVGSGvDSFSLMQPLGVVAGITPFNFP------AMVPmwmfpvALACGNTFVLKPPALVPSASLRMAQLLQ 190
Cdd:cd07100 76 AFLADEP-IETDAG-KAYVRYEPLGVVLGIMPWNFPfwqvfrFAAP------NLMAGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 191 EAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGS----SAVAEhiytTASAHGKRV-------QAFgaaknhaIVMPD 259
Cdd:cd07100 148 EAGFPEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSeragRAVAA----EAGKNLKKSvlelggsDPF-------IVLDD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 260 ADLDATVNAIMGGAFGSAGERCMAlpvvvA----VGDETADRLIERLKPLIAALRIG-PGElrgkDENEMGPVVSRAHQQ 334
Cdd:cd07100 217 ADLDKAVKTAVKGRLQNAGQSCIA-----AkrfiVHEDVYDEFLEKFVEAMAALKVGdPMD----EDTDLGPLARKDLRD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 335 KVLGYIDKGVSEGATLVMDGrnysVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGN 414
Cdd:cd07100 288 ELHEQVEEAVAAGATLLLGG----KRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGL 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446372874 415 GSVIFTTNGHYAREFAQSVEAGMVGINIPV---P-VPmafhsFGGWKRSVFGalNVHGPDGVRFYTRMKTV 481
Cdd:cd07100 364 GGSVFTTDLERAERVARRLEAGMVFINGMVksdPrLP-----FGGVKRSGYG--RELGRFGIREFVNIKTV 427
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
21-474 |
3.06e-80 |
|
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: 257.17 E-value: 3.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 21 LPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALG 100
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 101 ELTRGIEVVEFACGIPHLSKGEY----SFNVGSGVDSFSLMQPLGVVAGITPFNFPA-MVPMWMFPvALACGNTFVLKPP 175
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVlpldISARGEGRQGLVRRFPIGPVSAITPFNFPLnLVAHKVAP-AIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 176 ALVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIytTASAHGKRV--QAFGAAKnh 253
Cdd:cd07147 160 SRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDL--KARAGKKKVvlELGGNAA-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 254 AIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGElrgkDENEMGPVVSRAH 332
Cdd:cd07147 236 VIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVL-VHRSVYDEFKSRLVARVKALKTGdPKD----DATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 333 QQKVLGYIDKGVSEGATLVMDGRNysvagypEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEF 412
Cdd:cd07147 311 AERVEGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKF 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446372874 413 GNGSVIFTTNGHYAREFAQSVEAGMVGINiPVPVPMAFH-SFGGWKRSVFGAlnvhgpDGVRF 474
Cdd:cd07147 384 GLQAGVFTRDLEKALRAWDELEVGGVVIN-DVPTFRVDHmPYGGVKDSGIGR------EGVRY 439
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
7-482 |
4.94e-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: 257.28 E-value: 4.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAF---PAWSKMTPLRRARILFEFKVLLEKHRDEL 83
Cdd:cd07141 10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 84 AALIVSEHGKVWSDA-LGELTRGIEVVEFACG---------IPhlSKGEYsFnvgsgvdSFSLMQPLGVVAGITPFNFPA 153
Cdd:cd07141 90 ASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGwadkihgktIP--MDGDF-F-------TYTRHEPVGVCGQIIPWNFPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 154 MVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVV-HCGNEAASLLTSDPRVQAVSFVGSSAVAEH 232
Cdd:cd07141 160 LMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVpGYGPTAGAAISSHPDIDKVAFTGSTEVGKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 233 IYTTASAHG-KRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMA---LPVVVAVGDETADRLIERLKpliaA 308
Cdd:cd07141 240 IQQAAGKSNlKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAgsrTFVQESIYDEFVKRSVERAK----K 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 309 LRIG-PGELRgkdeNEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYpegfYVGGTLFDNVTPEMTIWREEI 387
Cdd:cd07141 316 RVVGnPFDPK----TEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGY----FIQPTVFSDVTDDMRIAKEEI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 388 FGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPV-PMAfhSFGGWKRSVFGALNv 466
Cdd:cd07141 388 FGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVsPQA--PFGGYKMSGNGREL- 464
|
490
....*....|....*.
gi 446372874 467 hGPDGVRFYTRMKTVT 482
Cdd:cd07141 465 -GEYGLQEYTEVKTVT 479
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
23-482 |
3.09e-79 |
|
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: 254.59 E-value: 3.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 23 VTNPATGKVIRQVTQSTREEMLAAIQSAHeAFPawSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGEL 102
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALAA-SYR--STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 103 TRGIEVVEFACGIPHLSKGE-YSFNVGSGVDS---FSLMQPLGVVAGITPFNFPA-MVPMWMFPvALACGNTFVLKPPAL 177
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGEsFSCDLTANGKArkiFTLREPLGVVLAITPFNHPLnQVAHKIAP-AIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 178 VPSASLRMAQLLQEAGLPDGVFNVVhCGN--EAASLLTSDPRVQAVSFVGSSAVAEHIyttASAHGKRVQAFGAAKNHA- 254
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVV-TGEpgEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGNDPl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 255 IVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGelrgKDENEMGPVVSRAHQ 333
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRIL-VHESVADEFVDLLVEKSAALVVGdPM----DPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 334 QKVLGYIDKGVSEGATLVMDGRNysvagypEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFG 413
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYG 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446372874 414 NGSVIFTTNGHYAREFAQSVEAGMVGINiPVPVPMAFHS-FGGWKRSVFGalnvhGPDGVR----FYTRMKTVT 482
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSpFGGVKDSGLG-----GKEGVReamkEMTNVKTYS 450
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
24-482 |
5.16e-79 |
|
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: 254.07 E-value: 5.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 24 TNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGELT 103
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 104 RGIEVVEFACGI-------PHLSKGEYSFNVGSGVDSfslmQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPA 176
Cdd:cd07099 81 LALEAIDWAARNaprvlapRKVPTGLLMPNKKATVEY----RPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 177 LVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTsDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIV 256
Cdd:cd07099 157 VTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 257 MPDADLDATVNAIMGGAFGSAGERCMALPVVVAVgDETADRLIERLKPLIAALRIGPGELRGKDeneMGPVVSRAHQQKV 336
Cdd:cd07099 236 LADADLERAAAAAVWGAMVNAGQTCISVERVYVH-ESVYDEFVARLVAKARALRPGADDIGDAD---IGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 337 LGYIDKGVSEGATLVMDGRNYSVagypEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGS 416
Cdd:cd07099 312 RRHVDDAVAKGAKALTGGARSNG----GGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSA 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446372874 417 VIFTTNGHYAREFAQSVEAGMVGINipvpVPMAFHS-----FGGWKRSVFGalNVHGPDGVRFYTRMKTVT 482
Cdd:cd07099 388 SVFSRDLARAEAIARRLEAGAVSIN----DVLLTAGipalpFGGVKDSGGG--RRHGAEGLREFCRPKAIA 452
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
5-477 |
7.82e-78 |
|
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: 251.55 E-value: 7.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 5 GNFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELA 84
Cdd:cd07111 23 GHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 85 ALIVSEHGKvwsdALGElTRGIEVVEFACGIPH----LSKGEYSFNVgsgvdsfslMQPLGVVAGITPFNFPAMVPMWMF 160
Cdd:cd07111 103 VLESLDNGK----PIRE-SRDCDIPLVARHFYHhagwAQLLDTELAG---------WKPVGVVGQIVPWNFPLLMLAWKI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 161 PVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAH 240
Cdd:cd07111 169 CPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 241 GKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGpgelRGKD 320
Cdd:cd07111 249 GKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLL-VQESVAEELIRKLKERMSHLRVG----DPLD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 321 EN-EMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSvagyPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIV--RV 397
Cdd:cd07111 324 KAiDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLP----SKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLtfRT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 398 PDYATAIStvNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGIN----IPVPVPmafhsFGGWKRSVFGALNvhGPDGVR 473
Cdd:cd07111 400 AKEAVALA--NNTPYGLAASVWSENLSLALEVALSLKAGVVWINghnlFDAAAG-----FGGYRESGFGREG--GKEGLY 470
|
....
gi 446372874 474 FYTR 477
Cdd:cd07111 471 EYLR 474
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
7-482 |
5.75e-77 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 250.03 E-value: 5.75e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPA-----WSKMTPLRRARILFEFKVLLEKHRD 81
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 82 ELAALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEYSFNVGSGVDSFS---LMQPLGVVAGITPFNFPAMVPMW 158
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKgyvLKEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 159 MFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTA 237
Cdd:PLN02467 171 KVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTgLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 238 SAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGEl 316
Cdd:PLN02467 251 AQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLL-VHERIASEFLEKLVKWAKNIKISdPLE- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 317 rgkDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRnySVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVR 396
Cdd:PLN02467 329 ---EGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGK--RPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 397 VPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVpMAFHSFGGWKRSVFG-ALnvhGPDGVRFY 475
Cdd:PLN02467 404 FSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPC-FCQAPWGGIKRSGFGrEL---GEWGLENY 479
|
....*..
gi 446372874 476 TRMKTVT 482
Cdd:PLN02467 480 LSVKQVT 486
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
4-481 |
9.66e-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: 248.98 E-value: 9.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 4 VGNFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAF--PAWSKMTPLRRARILFEFKVLLEKHRD 81
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFetDWGLKVSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 82 ELAALIVSEHGKVWSDAlgeltRGIEVVEFACGIPHLSkGEYSFNVGSGVDS------FSLMQPLGVVAGITPFNFPAMV 155
Cdd:cd07143 87 YLASIEALDNGKTFGTA-----KRVDVQASADTFRYYG-GWADKIHGQVIETdikkltYTRHEPIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 156 PMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHC-GNEAASLLTSDPRVQAVSFVGSSAVAEHIY 234
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGyGRTCGNAISSHMDIDKVAFTGSTLVGRKVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 235 TTASAHG-KRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGP 313
Cdd:cd07143 241 EAAAKSNlKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIY-VQEGIYDKFVKRFKEKAKKLKVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 314 GELRGKDEnemGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSvagyPEGFYVGGTLFDNVTPEMTIWREEIFGPVLG 393
Cdd:cd07143 320 PFAEDTFQ---GPQVSQIQYERIMSYIESGKAEGATVETGGKRHG----NEGYFIEPTIFTDVTEDMKIVKEEIFGPVVA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 394 IVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGIN----IPVPVPmafhsFGGWKRSVFGalNVHGP 469
Cdd:cd07143 393 VIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcynlLHHQVP-----FGGYKQSGIG--RELGE 465
|
490
....*....|..
gi 446372874 470 DGVRFYTRMKTV 481
Cdd:cd07143 466 YALENYTQIKAV 477
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
7-481 |
2.23e-76 |
|
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: 247.79 E-value: 2.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFP--AWSKMTPLRRARILFEFKVLLEKHRDELA 84
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 85 ALIVSEHGKVWSDA-LGELTRGIEVVEFACGIPHLSKGEySFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVA 163
Cdd:cd07142 87 ALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGM-TLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 164 LACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHG- 241
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTgFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSNl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 242 KRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGELRGKDE 321
Cdd:cd07142 246 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTF-VHESIYDEFVEKAKARALKRVVGDPFRKGVEQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 322 nemGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYpegfYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYA 401
Cdd:cd07142 325 ---GPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGY----YIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 402 TAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGIN----IPVPVPmafhsFGGWKRSVFGALNvhGPDGVRFYTR 477
Cdd:cd07142 398 EVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcydvFDASIP-----FGGYKMSGIGREK--GIYALNNYLQ 470
|
....
gi 446372874 478 MKTV 481
Cdd:cd07142 471 VKAV 474
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
29-482 |
1.82e-75 |
|
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: 244.51 E-value: 1.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 29 GKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGELTRGIEV 108
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 109 VEFACGIPHLSKGEYsFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVP-SASLRMAQ 187
Cdd:cd07152 81 LHEAAGLPTQPQGEI-LPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvSGGVVIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 188 LLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATVN 267
Cdd:cd07152 160 LFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 268 AIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGElrgkDENEMGPVVSRAHQQKVLGYIDKGVSE 346
Cdd:cd07152 240 NGAWGAFLHQGQICMAAGRHL-VHESVADAYTAKLAAKAKHLPVGdPAT----GQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 347 GATLVMDGRNysvagypEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYA 426
Cdd:cd07152 315 GARLEAGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446372874 427 REFAQSVEAGMVGINIPVPVPMAFHSFGGWKRSVFGAlNVHGPDGVRFYTRMKTVT 482
Cdd:cd07152 388 MALADRLRTGMLHINDQTVNDEPHNPFGGMGASGNGS-RFGGPANWEEFTQWQWVT 442
|
|
| lactal_redase_Meth |
NF040648 |
lactaldehyde dehydrogenase; |
7-481 |
2.58e-75 |
|
lactaldehyde dehydrogenase;
Pssm-ID: 468615 [Multi-domain] Cd Length: 463 Bit Score: 244.52 E-value: 2.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSssgETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAAL 86
Cdd:NF040648 2 FINGKWIDR---EDIDVINPYNLEVIDKIPSLSREEVKEAIEIANEAKEVMKNLSPRKRYNILMDIAEELKKNKEELAKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 87 IVSEHGKVWSDALGELTRGIEVVEFAcgiphlskGEYSFNV-GSGVDS-----FSLMQPLGVVAGITPFNFPAMVPMWMF 160
Cdd:NF040648 79 ITIDAGKPIKQSIIEVDRSIETFKLA--------AFYAKEIrGETIPSdagliFTKKEPLGVVGAITPFNYPLNLAAHKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 161 PVALACGNTFVLKPPALVPSASLRMAQLLQEA----GLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIyt 235
Cdd:NF040648 151 APAIATGNSVVLHPSSKAPLAAIELAKIIEKVlkkmNIPLGVFNLVTgYGEVVGDEIVKNEKVNKISFTGSVEVGESI-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 236 TASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PG 314
Cdd:NF040648 229 SKKAGMKKITLELGGNNPLIVLKDADIEKAVESAVKGSFLNSGQVCISVGRVI-VEEEIADEFIKKLVEETKKLKVGnPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 315 ElrgkDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNysvagypEGFYVGGTLFDnVTPEMTIWREEIFGPVLGI 394
Cdd:NF040648 308 D----EKTDIGPLITEEAAIRVENLVNEAIEEGAKLLCGGNR-------EGSLFYPTVLD-VDEDNILVKVETFGPVLPI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 395 VRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAFHSFGGWKRSVFGAlnvhgpDGVRF 474
Cdd:NF040648 376 IRVKDIDEAIEIANNTKYGLQAGVFTNDINKALKFADELEYGGVIINKSSTFRTDNMPFGGFKKSGLGK------EGIKY 449
|
490
....*....|.
gi 446372874 475 ----YTRMKTV 481
Cdd:NF040648 450 aveeMTEIKTI 460
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
7-482 |
1.02e-73 |
|
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: 241.25 E-value: 1.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPA--WSKMTPLRRARILFEFKVLLEKHRDELA 84
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 85 ALIVSEHGKVWSDALG-ELTRGIEVVEFACG---------IPhLSKGEYSFNVgsgvdSFSLMQPLGVVAGITPFNFPAM 154
Cdd:cd07140 89 TIESLDSGAVYTLALKtHVGMSIQTFRYFAGwcdkiqgktIP-INQARPNRNL-----TLTKREPIGVCGIVIPWNYPLM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 155 VPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVV-HCGNEAASLLTSDPRVQAVSFVGSSAVAEHI 233
Cdd:cd07140 163 MLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILpGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 234 Y-TTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMA---LPVVVAVGDETADRLIERLKpliaAL 309
Cdd:cd07140 243 MkSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAagrLFVEESIHDEFVRRVVEEVK----KM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 310 RIGPGELRGKDEnemGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVagypEGFYVGGTLFDNVTPEMTIWREEIFG 389
Cdd:cd07140 319 KIGDPLDRSTDH---GPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDR----PGFFFEPTVFTDVEDHMFIAKEESFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 390 PVLGIVRVP--DYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAfHSFGGWKRSVFGalNVH 467
Cdd:cd07140 392 PIMIISKFDdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVA-APFGGFKQSGFG--KDL 468
|
490
....*....|....*
gi 446372874 468 GPDGVRFYTRMKTVT 482
Cdd:cd07140 469 GEEALNEYLKTKTVT 483
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
5-462 |
3.79e-72 |
|
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: 236.58 E-value: 3.79e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 5 GNFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELA 84
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 85 ALIVSEHGKVWSDalgelTRGIEVvEFACGIPHLSKGEYSFNVGSGVD------SFSLMQPLGVVAGITPFNFPAMVPMW 158
Cdd:cd07117 82 MVETLDNGKPIRE-----TRAVDI-PLAADHFRYFAGVIRAEEGSANMidedtlSIVLREPIGVVGQIIPWNFPFLMAAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 159 MFPVALACGNTFVLKPPALVPSASLRMAQLLQEAgLPDGVFNVVHC-GNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTA 237
Cdd:cd07117 156 KLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGkGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 238 SAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGEl 316
Cdd:cd07117 235 AKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIF-VQEGIYDEFVAKLKEKFENVKVGnPLD- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 317 rgkDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVR 396
Cdd:cd07117 313 ---PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIK 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446372874 397 VPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPmAFHSFGGWKRSVFG 462
Cdd:cd07117 390 FKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIP-AGAPFGGYKKSGIG 454
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
7-487 |
4.76e-72 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 237.03 E-value: 4.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFP--AWSKMTPLRRARILFEFKVLLEKHRDELA 84
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 85 ALIVSEHGKVWS-DALGELTRGIEVVEFACGIPHLSKGEySFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVA 163
Cdd:PLN02766 104 ALDTIDAGKLFAlGKAVDIPAAAGLLRYYAGAADKIHGE-TLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 164 LACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHG- 241
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTgFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNl 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 242 KRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGELRGKd 320
Cdd:PLN02766 263 KQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVY-VQEGIYDEFVKKLVEKAKDWVVGdPFDPRAR- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 321 eneMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRnysvAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDY 400
Cdd:PLN02766 341 ---QGPQVDKQQFEKILSYIEHGKREGATLLTGGK----PCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 401 ATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINipvpVPMAFHS---FGGWKRSVFGalNVHGPDGVRFYTR 477
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN----CYFAFDPdcpFGGYKMSGFG--RDQGMDALDKYLQ 487
|
490
....*....|
gi 446372874 478 MKTVTSRWPN 487
Cdd:PLN02766 488 VKSVVTPLYN 497
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
18-463 |
1.24e-71 |
|
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: 236.32 E-value: 1.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 18 GETLPVTNPA-TGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWS 96
Cdd:cd07125 45 GEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 97 DALGELTrgiEVVEFACGIPHLSKGEYSFNVGSGVDS---FSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLK 173
Cdd:cd07125 125 DADAEVR---EAIDFCRYYAAQARELFSDPELPGPTGelnGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 174 PPALVPSASLRMAQLLQEAGLPDGVFNVVHC-GNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGA--- 249
Cdd:cd07125 202 PAEQTPLIAARAVELLHEAGVPRDVLQLVPGdGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPILPLIAetg 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 250 AKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVAVGDeTADRLIERLKPLIAALRIGPGELRGKDeneMGPVVS 329
Cdd:cd07125 282 GKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEE-IAERFIEMLKGAMASLKVGDPWDLSTD---VGPLID 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 330 RAHQQKVLGYIDKGVSEG---ATLVMDGRNysvagypeGFYVGGTLFDNVtpemTIW--REEIFGPVLGIVR--VPDYAT 402
Cdd:cd07125 358 KPAGKLLRAHTELMRGEAwliAPAPLDDGN--------GYFVAPGIIEIV----GIFdlTTEVFGPILHVIRfkAEDLDE 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446372874 403 AISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIP-----VPVpmafHSFGGWKRSVFGA 463
Cdd:cd07125 426 AIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNitgaiVGR----QPFGGWGLSGTGP 487
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
13-443 |
1.16e-70 |
|
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: 232.87 E-value: 1.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 13 TLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHG 92
Cdd:cd07130 6 EWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 93 KVWSDALGELTRGIEVVEFACGiphLSKGEYSFNVGSGVDSFSLM---QPLGVVAGITPFNFPAMVPMWMFPVALACGNT 169
Cdd:cd07130 86 KILPEGLGEVQEMIDICDFAVG---LSRQLYGLTIPSERPGHRMMeqwNPLGVVGVITAFNFPVAVWGWNAAIALVCGNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 170 FVLKPPALVPSASLR----MAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIyttasahGKRVQ 245
Cdd:cd07130 163 VVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQV-------GQAVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 246 A-FG------AAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGElr 317
Cdd:cd07130 236 ArFGrsllelGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLI-VHESIYDEVLERLKKAYKQVRIGdPLD-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 318 gkDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYpegfYVGGTLFDnVTPEMTIWREEIFGPVLGIVRV 397
Cdd:cd07130 313 --DGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGN----YVEPTIVE-GLSDAPIVKEETFAPILYVLKF 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446372874 398 PDYATAISTVNSHEFGNGSVIFTTNGHYAREF--AQSVEAGMVGINIP 443
Cdd:cd07130 386 DTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNIG 433
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
25-483 |
4.77e-70 |
|
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: 231.03 E-value: 4.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 25 NPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDA-LGELT 103
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 104 RGIEVVEFAcgiphLSKGEYSFNVGSGVDSFSLM--------QPLGVVAGITPFNFP---AMVPMWmfpVALACGNTFVL 172
Cdd:cd07098 82 VTCEKIRWT-----LKHGEKALRPESRPGGLLMFykrarveyEPLGVVGAIVSWNYPfhnLLGPII---AALFAGNAIVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 173 KPPALVPSAS---LRMAQ-LLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFG 248
Cdd:cd07098 154 KVSEQVAWSSgffLSIIReCLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 249 AAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGELRGKDeneMGPVV 328
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVI-VHEKIYDKLLEILTDRVQALRQGPPLDGDVD---VGAMI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 329 SRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVN 408
Cdd:cd07098 310 SPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIAN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 409 SHEFGNGSVIFTTNGHYAREFAQSVEAGMVGIN------IPVPVPmafhsFGGWKRSVFGALNvhGPDGVRFYTRMKTVT 482
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAINdfgvnyYVQQLP-----FGGVKGSGFGRFA--GEEGLRGLCNPKSVT 462
|
.
gi 446372874 483 S 483
Cdd:cd07098 463 E 463
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
7-462 |
9.73e-70 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 230.56 E-value: 9.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAAL 86
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 87 IVSEHGKVWSDALGELTRGIEVVE-FAcgipHLSKGEYSFNV-GSGVDS--FSLMQPLGVVAGITPFNFP-AMVPMWMFP 161
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEwFA----EEGKRIYGDTIpGHQADKrlIVIKQPIGVTAAITPWNFPaAMITRKAGP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 162 vALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAH 240
Cdd:PRK11241 170 -ALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTgSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 241 GKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGElrgKD 320
Cdd:PRK11241 249 IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLY-VQDGVYDRFAEKLQQAVSKLHIGDGL---EK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 321 ENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVagypEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDY 400
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHEL----GGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446372874 401 ATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVpVPMAFHSFGGWKRSVFG 462
Cdd:PRK11241 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLG 461
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
7-483 |
1.96e-69 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 231.24 E-value: 1.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFP--AWSKMTPLRRARILFEFKVLLEKHRDELA 84
Cdd:PLN02466 61 LINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 85 ALIVSEHGKVWSDALG-ELTRGIEVVEFACG---------IPhlSKGEYSFNVgsgvdsfsLMQPLGVVAGITPFNFPAM 154
Cdd:PLN02466 141 ALETWDNGKPYEQSAKaELPMFARLFRYYAGwadkihgltVP--ADGPHHVQT--------LHEPIGVAGQIIPWNFPLL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 155 VPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHI 233
Cdd:PLN02466 211 MFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSgFGPTAGAALASHMDVDKLAFTGSTDTGKIV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 234 YTTAS-AHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPliAALRIG 312
Cdd:PLN02466 291 LELAAkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTF-VHERVYDEFVEKAKA--RALKRV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 313 PGElRGKDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSvagyPEGFYVGGTLFDNVTPEMTIWREEIFGPVL 392
Cdd:PLN02466 368 VGD-PFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG----SKGYYIQPTVFSNVQDDMLIAQDEIFGPVQ 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 393 GIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIpVPVPMAFHSFGGWKRSVFGalNVHGPDGV 472
Cdd:PLN02466 443 SILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNC-FDVFDAAIPFGGYKMSGIG--REKGIYSL 519
|
490
....*....|.
gi 446372874 473 RFYTRMKTVTS 483
Cdd:PLN02466 520 NNYLQVKAVVT 530
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
7-443 |
1.10e-68 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 228.10 E-value: 1.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKmTPL-RRARILFEFKVLLEKHRDELAA 85
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAK-TPLwKRAELLHKAAAILKEHKAPIAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 86 LIVSEHGKVWSDALGELTRGIEVVEFAC--GIPHLSKGEY----SFNvGSGVDSFSLMQ--PLGVVAGITPFNFPAMVPM 157
Cdd:PLN00412 98 CLVKEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFlvsdSFP-GNERNKYCLTSkiPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 158 WMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHC-GNEAASLLTSDPRVQAVSFVGSSAvaeHIYTT 236
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGkGSEIGDFLTMHPGVNCISFTGGDT---GIAIS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 237 ASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVAVgDETADRLIERLKPLIAALRIGPGEl 316
Cdd:PLN00412 254 KKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVM-ESVADALVEKVNAKVAKLTVGPPE- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 317 rgkDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNysvagypEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVR 396
Cdd:PLN00412 332 ---DDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIR 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446372874 397 VPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIP 443
Cdd:PLN00412 402 INSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA 448
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
25-441 |
1.47e-68 |
|
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: 226.74 E-value: 1.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 25 NPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGELTR 104
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 105 GIEVVEFACGI--------PHLSKGeysfnvgsGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPA 176
Cdd:cd07102 82 MLERARYMISIaeealadiRVPEKD--------GFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 177 LVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIV 256
Cdd:cd07102 154 QTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 257 MPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGElrgkDENEMGPVVSRAHQQK 335
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIY-VHESIYDAFVEAFVAVVKGYKLGdPLD----PSTTLGPVVSARAADF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 336 VLGYIDKGVSEGATLVMDGRNYSVAGyPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNG 415
Cdd:cd07102 309 VRAQIADAIAKGARALIDGALFPEDK-AGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLT 387
|
410 420
....*....|....*....|....*.
gi 446372874 416 SVIFTTNGHYAREFAQSVEAGMVGIN 441
Cdd:cd07102 388 ASVWTKDIARAEALGEQLETGTVFMN 413
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
7-459 |
7.65e-68 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 225.93 E-value: 7.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPA--WSKMTPLRRARILFEFKVLLEKHRDELA 84
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 85 ALIVSEHGKVWSDALGELTRG-IEVVEFACGIPHLSKGEYSfNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVA 163
Cdd:PRK09847 103 LLETLDTGKPIRHSLRDDIPGaARAIRWYAEAIDKVYGEVA-TTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 164 LACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTA-SAHG 241
Cdd:PRK09847 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTgFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAgDSNM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 242 KRVQAFGAAKNHAIVMPDA-DLDATVNAIMGGAFGSAGERCMAlPVVVAVGDETADRLIERLKPLIAALRigPGELRGKD 320
Cdd:PRK09847 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIA-GTRLLLEESIADEFLALLKQQAQNWQ--PGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 321 eNEMGPVVSRAHQQKVLGYIDKGVSEGaTLVMDGRNysvAGYPEgfYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDY 400
Cdd:PRK09847 339 -TTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRN---AGLAA--AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSE 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446372874 401 ATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGIN------IPVPvpmafhsFGGWKRS 459
Cdd:PRK09847 412 EQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNnyndgdMTVP-------FGGYKQS 469
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
17-484 |
3.80e-65 |
|
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: 218.99 E-value: 3.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 17 SGETLPVTNP-ATGKVIRQVTQSTREEMLAAIQSAHEAFPAWsKMTPLR-RARILFEFKVLLEKHRDELAALIVSEHGKV 94
Cdd:cd07083 30 TKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTW-KDWPQEdRARLLLKAADLLRRRRRELIATLTYEVGKN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 95 WSDALGELTRGIEVVEFACGIPHLSKGEYSFNVG-SGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLK 173
Cdd:cd07083 109 WVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPyPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 174 PPALVPSASLRMAQLLQEAGLPDGVFNVV-HCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAA-- 250
Cdd:cd07083 189 PAEDAVVVGYKVFEIFHEAGFPPGVVQFLpGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPGQTWFKRLyv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 251 ----KNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGElrgKDENEMGP 326
Cdd:cd07083 269 etggKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLI-LTQGAYEPVLERLLKRAERLSVGPPE---ENGTDLGP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 327 VVSRAHQQKVLGYIDKGVSEGaTLVMDGRnySVAGypEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVP--DYATAI 404
Cdd:cd07083 345 VIDAEQEAKVLSYIEHGKNEG-QLVLGGK--RLEG--EGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKddDFAEAL 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 405 STVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGIN-IPVPVPMAFHSFGGWKRSVFGAlNVHGPDGVRFYTRMKTVTS 483
Cdd:cd07083 420 EVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrKITGALVGVQPFGGFKLSGTNA-KTGGPHYLRRFLEMKAVAE 498
|
.
gi 446372874 484 R 484
Cdd:cd07083 499 R 499
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
15-487 |
1.80e-64 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 217.82 E-value: 1.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 15 SSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKV 94
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 95 WSDALGEL------TRgievvEFACGIPHLSKGEysfNVGSGV----DSFSLMQPLGVVAGITPFNFPA------MVPmw 158
Cdd:PRK09407 108 RRHAFEEVldvaltAR-----YYARRAPKLLAPR---RRAGALpvltKTTELRQPKGVVGVISPWNYPLtlavsdAIP-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 159 mfpvALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVhcgneaasllTSDPRVqavsfVGSsAVAEHI----Y 234
Cdd:PRK09407 178 ----ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVV----------TGPGPV-----VGT-ALVDNAdylmF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 235 TTASAHGKRVqAFGAA------------KNHAIVMPDADLDATVNAIMGGAFGSAGERCMA---LPVVVAVGDETADRLI 299
Cdd:PRK09407 238 TGSTATGRVL-AEQAGrrligfslelggKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISierIYVHESIYDEFVRAFV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 300 ERLKpliaALRIGPGElrgKDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRnysvaGYPE-G--FYvGGTLFDNV 376
Cdd:PRK09407 317 AAVR----AMRLGAGY---DYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGK-----ARPDlGplFY-EPTVLTGV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 377 TPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFG-NGSViFTTNGHYAREFAQSVEAGMVGINIP-------VPVPM 448
Cdd:PRK09407 384 TPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGlNASV-WTGDTARGRAIAARIRAGTVNVNEGyaaawgsVDAPM 462
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446372874 449 afhsfGGWKRSVFGALnvHGPDGVRFYTRMKTV-TSRWPN 487
Cdd:PRK09407 463 -----GGMKDSGLGRR--HGAEGLLKYTESQTIaTQRVLP 495
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
24-481 |
3.43e-64 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 215.37 E-value: 3.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 24 TNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGELT 103
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 104 RGIEVVEF-ACGIPHLSKGEYSFNVGSG-VDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSA 181
Cdd:PRK09406 86 KCAKGFRYyAEHAEALLADEPADAAAVGaSRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 182 SLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKR-VQAFGAAkNHAIVMPDA 260
Cdd:PRK09406 166 ALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKtVLELGGS-DPFIVMPSA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 261 DLDATVNAIMGGAFGSAGERCMALPVVVA---VGDETADRLIERLkpliAALRIG-PGElrgkDENEMGPVVSRAHQQKV 336
Cdd:PRK09406 245 DLDRAAETAVTARVQNNGQSCIAAKRFIVhadVYDAFAEKFVARM----AALRVGdPTD----PDTDVGPLATEQGRDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 337 LGYIDKGVSEGATLVMDGRnySVAGypEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGS 416
Cdd:PRK09406 317 EKQVDDAVAAGATILCGGK--RPDG--PGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446372874 417 VIFTTNGHYAREFAQSVEAGMVGIN-IPVPVPMAfhSFGGWKRSVFG-ALNVHgpdGVRFYTRMKTV 481
Cdd:PRK09406 393 NAWTRDEAEQERFIDDLEAGQVFINgMTVSYPEL--PFGGVKRSGYGrELSAH---GIREFCNIKTV 454
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
42-459 |
2.24e-63 |
|
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: 212.52 E-value: 2.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 42 EMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKG 121
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 122 EYSfNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNV 201
Cdd:cd07095 81 ERA-TPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 202 VHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHA-IVMPDADLDATVNAIMGGAFGSAGER 280
Cdd:cd07095 160 VQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPlVVWDVADIDAAAYLIVQSAFLTAGQR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 281 CMALPVVVAVGDETADRLIERLKPLIAALRIGpgelrGKDENE--MGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYS 358
Cdd:cd07095 240 CTCARRLIVPDGAVGDAFLERLVEAAKRLRIG-----APDAEPpfMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 359 VAGYpegfYVGGTLFDnVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMV 438
Cdd:cd07095 315 AGTA----FLSPGIID-VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIV 389
|
410 420
....*....|....*....|.
gi 446372874 439 GINIPVPVPMAFHSFGGWKRS 459
Cdd:cd07095 390 NWNRPTTGASSTAPFGGVGLS 410
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
26-483 |
3.14e-62 |
|
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: 209.86 E-value: 3.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 26 PATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGELTRG 105
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 106 IEVVEF--------------ACGIPHLSKGEYSFnvgsgvdsfslmQPLGVVAGITPFNFP-AMVPMWMFPvALACGNTF 170
Cdd:cd07101 83 AIVARYyarraerllkprrrRGAIPVLTRTTVNR------------RPKGVVGVISPWNYPlTLAVSDAIP-ALLAGNAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 171 VLKPPALVPSASLRMAQLLQEAGLPDGVFNVVhCG--NEAASLLTSdpRVQAVSFVGSSAVAEHIyttASAHGKRVQAFG 248
Cdd:cd07101 150 VLKPDSQTALTALWAVELLIEAGLPRDLWQVV-TGpgSEVGGAIVD--NADYVMFTGSTATGRVV---AERAGRRLIGCS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 249 A---AKNHAIVMPDADLDATVNAIMGGAFGSAGERCMA---LPVVVAVGDETADRLIERLKpliaALRIGPGELRGkdeN 322
Cdd:cd07101 224 LelgGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSierIYVHESVYDEFVRRFVARTR----ALRLGAALDYG---P 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 323 EMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGyPegFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYAT 402
Cdd:cd07101 297 DMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLG-P--YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 403 AISTVNSHEFG-NGSViFTTNGHYAREFAQSVEAGMVGIN-------IPVPVPMafhsfGGWKRSVFGALnvHGPDGVRF 474
Cdd:cd07101 374 AIELANDTDYGlNASV-WTRDGARGRRIAARLRAGTVNVNegyaaawASIDAPM-----GGMKDSGLGRR--HGAEGLLK 445
|
....*....
gi 446372874 475 YTRMKTVTS 483
Cdd:cd07101 446 YTETQTVAV 454
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
5-462 |
5.23e-62 |
|
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: 210.00 E-value: 5.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 5 GNFIHGKTTLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELA 84
Cdd:cd07116 2 DNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 85 ALIVSEHGKVWSDALG-ELTRGIEVVEFACGIPHLSKGEYSfNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVA 163
Cdd:cd07116 82 VAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSIS-EIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 164 LACGNTFVLKPPALVPSASLRMAQLLQEAgLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAH-- 240
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNgFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENii 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 241 -------GKRVQAFGAAknhaiVMP--DADLDATVNAIMGGAFGSaGERCMAlPVVVAVGDETADRLIERLKPLIAALRI 311
Cdd:cd07116 240 pvtlelgGKSPNIFFAD-----VMDadDAFFDKALEGFVMFALNQ-GEVCTC-PSRALIQESIYDRFMERALERVKAIKQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 312 G-PGElrgkDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNvTPEMTIWREEIFGP 390
Cdd:cd07116 313 GnPLD----TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGP 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446372874 391 VLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPmAFHSFGGWKRSVFG 462
Cdd:cd07116 388 VLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYP-AHAAFGGYKQSGIG 458
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
13-462 |
8.41e-61 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 206.64 E-value: 8.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 13 TLSSSGETLPVtNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHG 92
Cdd:PRK13968 2 TITPATHAISV-NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 93 KVWSDALGELTRGIEVVE-FACGIPHLSKGEYSF--NVGSGVDsfslMQPLGVVAGITPFNFPamvpMWMF-----PVAL 164
Cdd:PRK13968 81 KPINQARAEVAKSANLCDwYAEHGPAMLKAEPTLveNQQAVIE----YRPLGTILAIMPWNFP----LWQVmrgavPILL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 165 AcGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKR- 243
Cdd:PRK13968 153 A-GNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKc 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 244 VQAFGAAkNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGElrgKDENE 323
Cdd:PRK13968 232 VLELGGS-DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFI-IEEGIASAFTERFVAAAAALKMGDPR---DEENA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 324 MGPVV-----SRAHQQkvlgyIDKGVSEGATLVMDGRNysVAGypEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVP 398
Cdd:PRK13968 307 LGPMArfdlrDELHHQ-----VEATLAEGARLLLGGEK--IAG--AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAK 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446372874 399 DYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINiPVPVPMAFHSFGGWKRSVFG 462
Cdd:PRK13968 378 DAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN-GYCASDARVAFGGVKKSGFG 440
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
69-468 |
1.99e-59 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 201.50 E-value: 1.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 69 LFEFKVLLEKHRDELAALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEYSFNVGSGVDSFSLMQPLGVVAGITP 148
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 149 FNFPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSS 227
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLgRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 228 AVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIA 307
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVY-VQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 308 ALRIG-PGElrgKDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGYpegfYVGGTLFDNVTPEMTIWREE 386
Cdd:PRK10090 240 AVQFGnPAE---RNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGY----YYPPTLLLDVRQEMSIMHEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 387 IFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPM-AFHSfgGWKRS-VFGAL 464
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMqGFHA--GWRKSgIGGAD 390
|
....
gi 446372874 465 NVHG 468
Cdd:PRK10090 391 GKHG 394
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
15-396 |
4.87e-55 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 199.01 E-value: 4.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 15 SSSGETLPVTNPA-TGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGK 93
Cdd:COG4230 566 AASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGK 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 94 VWSDALGELtRgiEVVEF----ACGIPHLskgeysfnvgsgVDSFSLMQPLGVVAGITPFNFP---------Amvpmwmf 160
Cdd:COG4230 646 TLPDAIAEV-R--EAVDFcryyAAQARRL------------FAAPTVLRGRGVFVCISPWNFPlaiftgqvaA------- 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 161 pvALACGNTfVLKPPAlvPSASL---RMAQLLQEAGLPDGvfnVVHC----GNEAASLLTSDPRVQAVSFVGSSAVAEHI 233
Cdd:COG4230 704 --ALAAGNT-VLAKPA--EQTPLiaaRAVRLLHEAGVPAD---VLQLlpgdGETVGAALVADPRIAGVAFTGSTETARLI 775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 234 YTTASAHGKRVQAFGA---AKNHAIVmpdadlDAT------VNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKP 304
Cdd:COG4230 776 NRTLAARDGPIVPLIAetgGQNAMIV------DSSalpeqvVDDVLASAFDSAGQRCSALRVLC-VQEDIADRVLEMLKG 848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 305 LIAALRIG-PGELrgkdENEMGPVVSRAHQQKVLGYIDKgvsegatlvMDGRNYSV--AGYPE----GFYVGGTLF--DN 375
Cdd:COG4230 849 AMAELRVGdPADL----STDVGPVIDAEARANLEAHIER---------MRAEGRLVhqLPLPEecanGTFVAPTLIeiDS 915
|
410 420
....*....|....*....|.
gi 446372874 376 VTpEMTiwrEEIFGPVLGIVR 396
Cdd:COG4230 916 IS-DLE---REVFGPVLHVVR 932
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
7-443 |
4.22e-54 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 189.01 E-value: 4.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 7 FIHGKTtLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAAL 86
Cdd:PRK09457 4 WINGDW-IAGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 87 IVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKGEYSFNVGSGVdSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALAC 166
Cdd:PRK09457 83 IARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKRSEMADGA-AVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 167 GNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQA 246
Cdd:PRK09457 162 GNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKILA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 247 FGAAKNHAIVMPD-ADLDATVNAIMGGAFGSAGERCM-ALPVVVAVGDEtADRLIERLKPLIAALRIGPGElrgkDENE- 323
Cdd:PRK09457 242 LEMGGNNPLVIDEvADIDAAVHLIIQSAFISAGQRCTcARRLLVPQGAQ-GDAFLARLVAVAKRLTVGRWD----AEPQp 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 324 -MGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNysvagypegfYVGGTLFdnVTP---EMTIWR----EEIFGPVLGIV 395
Cdd:PRK09457 317 fMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQ----------LQAGTGL--LTPgiiDVTGVAelpdEEYFGPLLQVV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 446372874 396 RVPDYATAISTVNSHEFG-NGSVIFTTNGHYAReFAQSVEAGMVGINIP 443
Cdd:PRK09457 385 RYDDFDEAIRLANNTRFGlSAGLLSDDREDYDQ-FLLEIRAGIVNWNKP 432
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
15-396 |
1.12e-52 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 192.39 E-value: 1.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 15 SSSGETLPVTNPA-TGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGK 93
Cdd:PRK11905 563 DVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGK 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 94 VWSDALGELtRgiEVVEF----ACGIPHLSKGEYSfnvgsgvdsfslmQPLGVVAGITPFNFPAMVPMWMFPVALACGNT 169
Cdd:PRK11905 643 TLANAIAEV-R--EAVDFlryyAAQARRLLNGPGH-------------KPLGPVVCISPWNFPLAIFTGQIAAALVAGNT 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 170 FVLKPPALVPSASLRMAQLLQEAGLPDGvfnVVHC----GNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQ 245
Cdd:PRK11905 707 VLAKPAEQTPLIAARAVRLLHEAGVPKD---ALQLlpgdGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPV 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 246 AFGA---AKNHAIVmpdadlDAT------VNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGE 315
Cdd:PRK11905 784 PLIAetgGQNAMIV------DSSalpeqvVADVIASAFDSAGQRCSALRVLC-LQEDVADRVLTMLKGAMDELRIGdPWR 856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 316 LRgkdeNEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSVAGypeGFYVGGTLF--DNVtPEMTiwrEEIFGPVLG 393
Cdd:PRK11905 857 LS----TDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEK---GTFVAPTLIeiDSI-SDLE---REVFGPVLH 925
|
...
gi 446372874 394 IVR 396
Cdd:PRK11905 926 VVR 928
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
18-441 |
1.67e-52 |
|
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: 185.11 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 18 GETLPVTNPATGK-VIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWS 96
Cdd:TIGR01238 50 GEAQPVTNPADRRdIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 97 DALGELTRGIEVVEFacgiphlskgeYSFNVGSGVDSFSlMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPA 176
Cdd:TIGR01238 130 NAIAEVREAVDFCRY-----------YAKQVRDVLGEFS-VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 177 LVPSASLRMAQLLQEAGLPDGVFNVV-HCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGA---AKN 252
Cdd:TIGR01238 198 QTSLIAYRAVELMQEAGFPAGTIQLLpGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLIAetgGQN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 253 HAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIG-PGELrgkdENEMGPVVSRA 331
Cdd:TIGR01238 278 AMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLC-VQEDVADRVLTMIQGAMQELKVGvPHLL----TTDVGPVIDAE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 332 HQQKVLGYIDKGVSEGATLVMDGRNYSVAgYPEGFYVGGTLFDnvTPEMTIWREEIFGPVLGIVR--VPDYATAISTVNS 409
Cdd:TIGR01238 353 AKQNLLAHIEHMSQTQKKIAQLTLDDSRA-CQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRykARELDQIVDQINQ 429
|
410 420 430
....*....|....*....|....*....|..
gi 446372874 410 HEFGNGSVIFTTNGHYAREFAQSVEAGMVGIN 441
Cdd:TIGR01238 430 TGYGLTMGVHSRIETTYRWIEKHARVGNCYVN 461
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
21-462 |
7.00e-52 |
|
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: 182.62 E-value: 7.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 21 LPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAF-------PAWSKMTPLRRArilfefKVLLEKHRDELAALIVSEHGK 93
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFldrnnwlPAHERIAILERL------ADLMEERADELALLIAREGGK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 94 VWSDALGELTRGIEVVEFAcgIPHLSKGEYS------FNVGSGVDSFSLMQPLGVVAGITPFNFP------AMVPmwmfp 161
Cdd:cd07148 75 PLVDAKVEVTRAIDGVELA--ADELGQLGGReipmglTPASAGRIAFTTREPIGVVVAISAFNHPlnlivhQVAP----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 162 vALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASAhG 241
Cdd:cd07148 148 -AIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAP-G 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 242 KRV--QAFGAAKnhAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGPGELrgk 319
Cdd:cd07148 226 TRCalEHGGAAP--VIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVF-VPAEIADDFAQRLAAAAEKLVVGDPTD--- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 320 DENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSvagypEGFYVGGTLFDNvTPEMTIWREEIFGPVLGIVRVPD 399
Cdd:cd07148 300 PDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLS-----DTTYAPTVLLDP-PRDAKVSTQEIFGPVVCVYSYDD 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446372874 400 YATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVPVPMAFHSFGGWKRSVFG 462
Cdd:cd07148 374 LDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
15-413 |
7.93e-47 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 175.00 E-value: 7.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 15 SSSGETLPVTNPA-TGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGK 93
Cdd:PRK11904 558 NGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGK 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 94 VWSDALGELtRgiEVVEFaC------GIPHLSKGEySFNVGSGVDSFSLMQPLGVVAGITPFNFPamVPMWMFPV--ALA 165
Cdd:PRK11904 638 TLQDAIAEV-R--EAVDF-CryyaaqARRLFGAPE-KLPGPTGESNELRLHGRGVFVCISPWNFP--LAIFLGQVaaALA 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 166 CGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVH-CGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTAsahgkrv 244
Cdd:PRK11904 711 AGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPgDGATVGAALTADPRIAGVAFTGSTETARIINRTL------- 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 245 qafgAAKNHAIVMPDAD--------LDAT------VNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALR 310
Cdd:PRK11904 784 ----AARDGPIVPLIAEtggqnamiVDSTalpeqvVDDVVTSAFRSAGQRCSALRVLF-VQEDIADRVIEMLKGAMAELK 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 311 IGPGELRGKDeneMGPVVSRAHQQKVLGYIDKgVSEGATLVmdgrnYSV---AGYPEGFYVGGTLFDnvTPEMTIWREEI 387
Cdd:PRK11904 859 VGDPRLLSTD---VGPVIDAEAKANLDAHIER-MKREARLL-----AQLplpAGTENGHFVAPTAFE--IDSISQLEREV 927
|
410 420
....*....|....*....|....*...
gi 446372874 388 FGPVLGIVRVP--DYATAISTVNSHEFG 413
Cdd:PRK11904 928 FGPILHVIRYKasDLDKVIDAINATGYG 955
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
2-487 |
2.42e-43 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 160.38 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 2 ETVGNFIHGKttLSSSGETLPVTNPATGKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRD 81
Cdd:PLN02315 19 RNLGCYVGGE--WRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 82 ELAALIVSEHGKVWSDALGELTRGIEVVEFACGiphLSKGEYSFNVGSGVDSFSLMQ---PLGVVAGITPFNFPAMVPMW 158
Cdd:PLN02315 97 YLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVG---LSRQLNGSIIPSERPNHMMMEvwnPLGIVGVITAFNFPCAVLGW 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 159 MFPVALACGNTFVLKPPALVPSASLRM----AQLLQEAGLPDGVFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIY 234
Cdd:PLN02315 174 NACIALVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 235 TTASA-HGKRVQAFgAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLKPLIAALRIGP 313
Cdd:PLN02315 254 QTVNArFGKCLLEL-SGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLL-LHESIYDDVLEQLLTVYKQVKIGD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 314 GELRGkdeNEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSvagyPEGFYVGGTLFDnVTPEMTIWREEIFGPVLG 393
Cdd:PLN02315 332 PLEKG---TLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE----SEGNFVQPTIVE-ISPDADVVKEELFGPVLY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 394 IVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREF--AQSVEAGMVGINIPVPVPMAFHSFGGWKRSvfGALNVHGPDG 471
Cdd:PLN02315 404 VMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWigPLGSDCGIVNVNIPTNGAEIGGAFGGEKAT--GGGREAGSDS 481
|
490
....*....|....*.
gi 446372874 472 VRFYTRMKTVTSRWPN 487
Cdd:PLN02315 482 WKQYMRRSTCTINYGN 497
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
15-396 |
1.23e-40 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 156.67 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 15 SSSGETLPVTNPATGK-VIRQVTQSTREEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGK 93
Cdd:PRK11809 655 VAAGEMSPVINPADPRdIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 94 VWSDALGELTrgiEVVEFacgiphlskgeYSFNVGSGVDSFS--LMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFV 171
Cdd:PRK11809 735 TFSNAIAEVR---EAVDF-----------LRYYAGQVRDDFDndTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 172 LKPPALVPSASLRMAQLLQEAGLPDGVFNVV-HCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYTTASahgKRVQAFGA- 249
Cdd:PRK11809 801 AKPAEQTPLIAAQAVRILLEAGVPAGVVQLLpGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLA---GRLDPQGRp 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 250 --------AKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPvVVAVGDETADRLIERLKPLIAALRIG-PGELrgkd 320
Cdd:PRK11809 878 ipliaetgGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALR-VLCLQDDVADRTLKMLRGAMAECRMGnPDRL---- 952
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446372874 321 ENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDGRNYSvAGYPEGFYVGGTL--FDNVTpEMTiwrEEIFGPVLGIVR 396
Cdd:PRK11809 953 STDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENS-EDWQSGTFVPPTLieLDSFD-ELK---REVFGPVLHVVR 1025
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
138-481 |
1.04e-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: 143.05 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 138 QPLGVVAGITPFNFP---AMVPMwmfpV-ALACGNTFVLKPPALVPSASLRMAQLLQEAgLPDGVFNVVHCGNEAASLLT 213
Cdd:cd07087 99 EPLGVVLIIGPWNYPlqlALAPL----IgAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVATALL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 214 SDPrVQAVSFVGSSAVAEHIYTTASAH---------GKrvqafgaakNHAIVMPDADLDATVNAIMGGAFGSAGERCMAl 284
Cdd:cd07087 174 AEP-FDHIFFTGSPAVGKIVMEAAAKHltpvtlelgGK---------SPCIVDKDANLEVAARRIAWGKFLNAGQTCIA- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 285 PVVVAVGDETADRLIERLKPLIAALrIGPGELRGKDeneMGPVVSRAHQQKVLGYIDKGvsegaTLVMDGRnysvaGYPE 364
Cdd:cd07087 243 PDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPD---YGRIINERHFDRLASLLDDG-----KVVIGGQ-----VDKE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 365 GFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPV 444
Cdd:cd07087 309 ERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVL 388
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446372874 445 pvpmaFH------SFGGWKRSVFGALnvHGPDGVRFYTRMKTV 481
Cdd:cd07087 389 -----LHaaipnlPFGGVGNSGMGAY--HGKAGFDTFSHLKSV 424
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
17-409 |
2.19e-36 |
|
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: 141.18 E-value: 2.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 17 SGETLPVTNPAT-GKVIRQVTQSTREEMLAAIQSAHEAFPAWSKMtPLR-RARILFEFKVLLE-KHRDELAALIVSEHGK 93
Cdd:cd07123 44 TGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARM-PFEdRAAIFLKAADLLSgKYRYELNAATMLGQGK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 94 -VWSdalGELTRGIEVVEFacgiphlskgeYSFNV--------------GSGVDSFSLMQPL-GVVAGITPFNFPAM--- 154
Cdd:cd07123 123 nVWQ---AEIDAACELIDF-----------LRFNVkyaeelyaqqplssPAGVWNRLEYRPLeGFVYAVSPFNFTAIggn 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 155 ---VPMWMfpvalacGNTFVLKP-PALVPSASLRMaQLLQEAGLPDGVFNVVHC-GNEAASLLTSDPRVQAVSFVGSSAV 229
Cdd:cd07123 189 lagAPALM-------GNVVLWKPsDTAVLSNYLVY-KILEEAGLPPGVINFVPGdGPVVGDTVLASPHLAGLHFTGSTPT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 230 AEHIYTTASAHGKRVQAF----G--AAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRLIERLK 303
Cdd:cd07123 261 FKSLWKQIGENLDRYRTYprivGetGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAY-VPESLWPEVKERLL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 304 PLIAALRIGPGElrgKDENEMGPVVSRAHQQKVLGYIDKGVSE-GATLVMDGrNYSVAgypEGFYVGGTLFDNVTPEMTI 382
Cdd:cd07123 340 EELKEIKMGDPD---DFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGG-KCDDS---VGYFVEPTVIETTDPKHKL 412
|
410 420
....*....|....*....|....*....
gi 446372874 383 WREEIFGPVLGIVRVPD--YATAISTVNS 409
Cdd:cd07123 413 MTEEIFGPVLTVYVYPDsdFEETLELVDT 441
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
46-409 |
1.14e-33 |
|
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: 131.96 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 46 AIQSAHeafpAWSKMTPLRRARI--LFEFKVLLEKHRDELAALIVSEHGKvwSDALGELTRGIEVV-EFACGIPHLSKGE 122
Cdd:cd07134 5 AAQQAH----ALALRASTAAERIakLKRLKKAILARREEIIAALAADFRK--PAAEVDLTEILPVLsEINHAIKHLKKWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 123 YSFNVGS-----GVDSFSLMQPLGVVAGITPFNFP---AMVPMwmfPVALACGNTFVLKPPALVPSASLRMAQLLQEAGL 194
Cdd:cd07134 79 KPKRVRTplllfGTKSKIRYEPKGVCLIISPWNYPfnlAFGPL---VSAIAAGNTAILKPSELTPHTSAVIAKIIREAFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 195 PDGVFnVVHCGNEAASLLTSDPrVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAF 274
Cdd:cd07134 156 EDEVA-VFEGDAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 275 GSAGERCMAlPVVVAVGDETADRLIERLKPLIAAlRIGPGELRgKDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVMDG 354
Cdd:cd07134 234 LNAGQTCIA-PDYVFVHESVKDAFVEHLKAEIEK-FYGKDAAR-KASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446372874 355 rnysvAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNS 409
Cdd:cd07134 311 -----QFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINA 360
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
114-481 |
1.62e-32 |
|
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: 128.88 E-value: 1.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 114 GIPHLSKGEYsfnVGSGVDSFSLM------QPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQ 187
Cdd:cd07135 80 NLKKWAKDEK---VKDGPLAFMFGkprirkEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 188 LLQEAgLPDGVFNVVHCG-NEAASLLTSdpRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATV 266
Cdd:cd07135 157 LVPKY-LDPDAFQVVQGGvPETTALLEQ--KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 267 NAIMGGAFGSAGERCMAlPVVVAVGDETADRLIERLKPLIAALRigPGELrgKDENEMGPVVSRAHQQKVLGYIDKgvsE 346
Cdd:cd07135 234 KRILWGKFGNAGQICVA-PDYVLVDPSVYDEFVEELKKVLDEFY--PGGA--NASPDYTRIVNPRHFNRLKSLLDT---T 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 347 GATLVMDGRnysvaGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYA 426
Cdd:cd07135 306 KGKVVIGGE-----MDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEI 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446372874 427 REFAQSVEAGMVGIN---IPVPVPMAfhSFGGWKRSVFGALnvHGPDGVRFYTRMKTV 481
Cdd:cd07135 381 DHILTRTRSGGVVINdtlIHVGVDNA--PFGGVGDSGYGAY--HGKYGFDTFTHERTV 434
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
138-481 |
2.69e-31 |
|
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: 125.29 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 138 QPLGVVAGITPFNFP---AMVPMwmfPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVfNVVhcgneaasllTS 214
Cdd:cd07133 100 QPLGVVGIIVPWNYPlylALGPL---IAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-AVV----------TG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 215 DPRV-QAVS--------FVGSSAVAEHIYTTASAH---------GKrvqafgaakNHAIVMPDADLDATVNAIMGGAFGS 276
Cdd:cd07133 166 GADVaAAFSslpfdhllFTGSTAVGRHVMRAAAENltpvtlelgGK---------SPAIIAPDADLAKAAERIAFGKLLN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 277 AGERCMAlPVVVAVGDETADRLIERLKPLIAALRigPgelRGKDENEMGPVVSRAHQQKVLGYIDKGVSEGATLVmdgrn 356
Cdd:cd07133 237 AGQTCVA-PDYVLVPEDKLEEFVAAAKAAVAKMY--P---TLADNPDYTSIINERHYARLQGLLEDARAKGARVI----- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 357 ySVAGYPEGFYVGG----TLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQS 432
Cdd:cd07133 306 -ELNPAGEDFAATRklppTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRR 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446372874 433 VEAGMVGINIPVpvpmaFH------SFGGWKRSVFGALnvHGPDGVRFYTRMKTV 481
Cdd:cd07133 385 THSGGVTINDTL-----LHvaqddlPFGGVGASGMGAY--HGKEGFLTFSHAKPV 432
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
132-484 |
2.03e-30 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 123.60 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 132 DSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAgLPDGVFNVVHCGNEAASL 211
Cdd:PTZ00381 102 KSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 212 LTSDPrVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMAlPVVVAVG 291
Cdd:PTZ00381 181 LLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVA-PDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 292 DETADRLIERLKPLIAALrIGPGElrgKDENEMGPVVSRAHQQKVLGYIDkgvSEGATLVMDGrNYSVAGYpegfYVGGT 371
Cdd:PTZ00381 259 RSIKDKFIEALKEAIKEF-FGEDP---KKSEDYSRIVNEFHTKRLAELIK---DHGGKVVYGG-EVDIENK----YVAPT 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 372 LFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVpvpmaFH 451
Cdd:PTZ00381 327 IIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCV-----FH 401
|
330 340 350
....*....|....*....|....*....|....*....
gi 446372874 452 ------SFGGWKRSVFGAlnVHGPDGVRFYTRMKTVTSR 484
Cdd:PTZ00381 402 llnpnlPFGGVGNSGMGA--YHGKYGFDTFSHPKPVLNK 438
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
45-477 |
3.67e-30 |
|
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: 122.35 E-value: 3.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 45 AAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWsDALGELTRGI------EVVEFACGIPHL 118
Cdd:cd07084 3 RALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGW-MFAENICGDQvqlrarAFVIYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 119 SKgeYSFNVGSGVDSFSLMQPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAG-LPDG 197
Cdd:cd07084 82 PG--NHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 198 VFNVVHCGNEAASLLTSDPRVQAVSFVGSSAVAEHIYttASAHGKRVQAFGAAKNHAIVMPDAD-LDATVNAIMGGAFGS 276
Cdd:cd07084 160 DVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLA--LDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 277 AGERCMALPVVVAVGDETADRLIERLKPLIAalRIGPGEL---RGKDENEMGPVVS-RAHQQKVLGYidkgvSEGATLVM 352
Cdd:cd07084 238 SGQKCTAQSMLFVPENWSKTPLVEKLKALLA--RRKLEDLllgPVQTFTTLAMIAHmENLLGSVLLF-----SGKELKNH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 353 DGRNYSVAGYPEGFYVGGTLFDNVTPemtIWREEIFGPVLGIVRVPDYATAiSTVNSHEFGNGSV---IFTTNGHYAREF 429
Cdd:cd07084 311 SIPSIYGACVASALFVPIDEILKTYE---LVTEEIFGPFAIVVEYKKDQLA-LVLELLERMHGSLtaaIYSNDPIFLQEL 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446372874 430 AQSVE-AGMVGINIPVP---VPMAFHSFGGwkRSVFGALNVHGPDGVRFYTR 477
Cdd:cd07084 387 IGNLWvAGRTYAILRGRtgvAPNQNHGGGP--AADPRGAGIGGPEAIKLVWR 436
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
138-468 |
2.17e-29 |
|
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: 119.82 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 138 QPLGVVAGITPFNFPAMVPMwmFPV--ALACGNTFVLKPPALVPSASLRMAQLLQEAgLPDGVFNVVHCG-NEAASLLts 214
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSL--EPVigAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGvPETTALL-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 215 DPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGS-AGERCMAlPVVVAVGDE 293
Cdd:cd07137 175 EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIA-PDYVLVEES 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 294 TADRLIERLKPLIAALrIGPGELRGKDeneMGPVVSRAHQQKVLGYI-DKGVSegATLVMDGRNYSvagypEGFYVGGTL 372
Cdd:cd07137 254 FAPTLIDALKNTLEKF-FGENPKESKD---LSRIVNSHHFQRLSRLLdDPSVA--DKIVHGGERDE-----KNLYIEPTI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 373 FDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVpVPMAFHS 452
Cdd:cd07137 323 LLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTV-VQYAIDT 401
|
330
....*....|....*...
gi 446372874 453 --FGGWKRSVFGALnvHG 468
Cdd:cd07137 402 lpFGGVGESGFGAY--HG 417
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
138-484 |
1.10e-26 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 112.21 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 138 QPLGVVAGITPFNFP---AMVPMwmfpV-ALACGNTFVLKPPALVPSASLRMAQLLQEAgLPDGVFNVVHCGNEAASLLT 213
Cdd:cd07136 99 EPYGVVLIIAPWNYPfqlALAPL----IgAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 214 SDPrVQAVSFVGSSAVAEHIYTTASAH---------GKrvqafgaakNHAIVMPDADLDATVNAIMGGAFGSAGERCMAl 284
Cdd:cd07136 174 DQK-FDYIFFTGSVRVGKIVMEAAAKHltpvtlelgGK---------SPCIVDEDANLKLAAKRIVWGKFLNAGQTCVA- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 285 PVVVAVGDETADRLIERLKPLIAALrIGPGELRGKDeneMGPVVSRAHQQKVLGYIDKGvsegaTLVMDGrNYSvagyPE 364
Cdd:cd07136 243 PDYVLVHESVKEKFIKELKEEIKKF-YGEDPLESPD---YGRIINEKHFDRLAGLLDNG-----KIVFGG-NTD----RE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 365 GFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPV 444
Cdd:cd07136 309 TLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTI 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446372874 445 pvpMAFHS----FGGWKRSVFGALnvHGPDGVRFYTRMKTVTSR 484
Cdd:cd07136 389 ---MHLANpylpFGGVGNSGMGSY--HGKYSFDTFSHKKSILKK 427
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
45-411 |
1.31e-21 |
|
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: 97.23 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 45 AAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGELTRGIEVVE-FAcgiPHLSKGEY 123
Cdd:cd07129 3 AAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRlFA---DLVREGSW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 124 ----------SFNVGSGVDSFSLMQPLGVVAGITPFNFP-AmvpmwmFPV-------ALACGNTFVLKPPALVPSASLRM 185
Cdd:cd07129 80 ldaridpadpDRQPLPRPDLRRMLVPLGPVAVFGASNFPlA------FSVaggdtasALAAGCPVVVKAHPAHPGTSELV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 186 AQL----LQEAGLPDGVFNVVHCGNEAASL-LTSDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFG--AAKNHAIVMP 258
Cdd:cd07129 154 ARAiraaLRATGLPAGVFSLLQGGGREVGVaLVKHPAIKAVGFTGSRRGGRALFDAAAARPEPIPFYAelGSVNPVFILP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 259 DAdLDATVNAIMGGAFGS----AGERCMALPVVVAVGDETADRLIERLKPLIAAlrIGPGELrgkdeneMGPVVSRAHQQ 334
Cdd:cd07129 234 GA-LAERGEAIAQGFVGSltlgAGQFCTNPGLVLVPAGPAGDAFIAALAEALAA--APAQTM-------LTPGIAEAYRQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 335 kvlgyidkGVSE-----GATLVMDGrnysvAGYPEGFYVGGTLF-----DNVTPEmtIWREEIFGPVLGIVRVPDYATAI 404
Cdd:cd07129 304 --------GVEAlaaapGVRVLAGG-----AAAEGGNQAAPTLFkvdaaAFLADP--ALQEEVFGPASLVVRYDDAAELL 368
|
....*..
gi 446372874 405 STVNSHE 411
Cdd:cd07129 369 AVAEALE 375
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
138-484 |
1.98e-21 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 97.04 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 138 QPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAASLLtsDPR 217
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETTALL--EQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 218 VQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFG-SAGERCMAlPVVVAVGDETAD 296
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACIS-PDYILTTKEYAP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 297 RLIERLKPLIAALrIGPGELRGKDeneMGPVVSRAHQQKVLGYIDKgvsegaTLVMDGRNYSVAGYPEGFYVGGTLFDNV 376
Cdd:PLN02174 268 KVIDAMKKELETF-YGKNPMESKD---MSRIVNSTHFDRLSKLLDE------KEVSDKIVYGGEKDRENLKIAPTILLDV 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 377 TPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINiPVPVPMAFHS--FG 454
Cdd:PLN02174 338 PLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVN-DIAVHLALHTlpFG 416
|
330 340 350
....*....|....*....|....*....|
gi 446372874 455 GWKRSVFGALnvHGPDGVRFYTRMKTVTSR 484
Cdd:PLN02174 417 GVGESGMGAY--HGKFSFDAFSHKKAVLYR 444
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
137-411 |
5.33e-21 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 95.37 E-value: 5.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 137 MQPLGVVAGITPFNFP---AMVPMwmfpV-ALACGNTFVLKPPALVPSASLRMAQLL-----QEAglpdgvFNVVHCG-N 206
Cdd:cd07132 98 KEPLGVVLIIGAWNYPlqlTLVPL----VgAIAAGNCVVIKPSEVSPATAKLLAELIpkyldKEC------YPVVLGGvE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 207 EAASLLtsDPRVQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFGSAGERCMAlPV 286
Cdd:cd07132 168 ETTELL--KQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIA-PD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 287 VVAVGDETADRLIERLKpliAALRigpgELRGKDENE---MGPVVSRAHQQKVLGYIdkgvsEGATLVMDGRnysvaGYP 363
Cdd:cd07132 245 YVLCTPEVQEKFVEALK---KTLK----EFYGEDPKEspdYGRIINDRHFQRLKKLL-----SGGKVAIGGQ-----TDE 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446372874 364 EGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHE 411
Cdd:cd07132 308 KERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSRE 355
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
1-430 |
1.55e-18 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 88.22 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 1 METVGNFIHGKTtLSSSGETLPVTNPATGKVIRQVTqSTREEMLAAIQSAHE-AFPAWSKMTPLRRARILFEFKVLLEKH 79
Cdd:PRK11903 2 TELLANYVAGRW-QAGSGAGTPLFDPVTGEELVRVS-ATGLDLAAAFAFAREqGGAALRALTYAQRAALLAAIVKVLQAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 80 RDELAALIVSEHGKVWSDALGELTRGIEVVEF------ACG-IPHLSKGEysfNVGSGVD-SFSLMQPL----GVVAGIT 147
Cdd:PRK11903 80 RDAYYDIATANSGTTRNDSAVDIDGGIFTLGYyaklgaALGdARLLRDGE---AVQLGKDpAFQGQHVLvptrGVALFIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 148 PFNFPAMvPMW-MFPVALACGNTFVLKPPALVPSASLRMAQLLQEAG-LPDGVFNVVhCGNeAASLLTSDPRVQAVSFVG 225
Cdd:PRK11903 157 AFNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVV-CGS-SAGLLDHLQPFDVVSFTG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 226 SSAVAEHIYTTAS--AHGKRVQAFGAAKNHAIVMPDAD-----LDATVNAIMGGAFGSAGERCMALPVVVaVGDETADRL 298
Cdd:PRK11903 234 SAETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIF-VPEALYDAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 299 IERLKPLIAALRIG-PGElrgkDENEMGPVVSRAHQQKVLGYIDKgVSEGATLVMDGRNYSVAGYPE--GFYVGGTLF-- 373
Cdd:PRK11903 313 AEALAARLAKTTVGnPRN----DGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGFALVDADPavAACVGPTLLga 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446372874 374 ---DNVTpemTIWREEIFGPVLGIVRVPDYATAISTVNShefGNGSV---IFTTNGHYAREFA 430
Cdd:PRK11903 388 sdpDAAT---AVHDVEVFGPVATLLPYRDAAHALALARR---GQGSLvasVYSDDAAFLAAAA 444
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
138-484 |
2.86e-18 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 87.47 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 138 QPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLqEAGLPDGVFNVVHCGNEAASLLTsDPR 217
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANI-PKYLDSKAVKVIEGGPAVGEQLL-QHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 218 VQAVSFVGSSAVAEHIYTTASAHGKRVQAFGAAKNHAIV---MPDADLDATVNAIMGGAFGS-AGERCMALPVVVaVGDE 293
Cdd:PLN02203 185 WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVL-VEER 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 294 TADRLIERLKPLIAALRigpGElRGKDENEMGPVVSRAHQQKVLGYI-DKGVSegATLVMDGrnySVAgyPEGFYVGGTL 372
Cdd:PLN02203 264 FAPILIELLKSTIKKFF---GE-NPRESKSMARILNKKHFQRLSNLLkDPRVA--ASIVHGG---SID--EKKLFIEPTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 373 FDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGNGSVIFTTNGHYAREFAQSVEAGMVGINIPVpVPMAFHS 452
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAI-IQYACDS 411
|
330 340 350
....*....|....*....|....*....|....
gi 446372874 453 --FGGWKRSVFGalNVHGPDGVRFYTRMKTVTSR 484
Cdd:PLN02203 412 lpFGGVGESGFG--RYHGKYSFDTFSHEKAVLRR 443
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
6-313 |
1.85e-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: 72.53 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 6 NFIHGKTTLSSSGETLPvtNPATGKVIRQVTQSTREEMLAAIQSAhEAFPAWSKMTPLRR-----------ARILFEFKv 74
Cdd:cd07126 1 NLVAGKWKGASNYTTLL--DPLNGDKFISVPDTDEDEINEFVDSL-RQCPKSGLHNPLKNperyllygdvsHRVAHELR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 75 lLEKHRDELAALIVSEHGKVWSDALGELTRGIEVVEFACG--IPHLSKgeySFNVGS---GVDSFSLMQPLGVVAGITPF 149
Cdd:cd07126 77 -KPEVEDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGdqVRFLAR---SFNVPGdhqGQQSSGYRWPYGPVAIITPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 150 NFPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEAGLPDGVFNVVHCGNEAAS--LLTSDPRVqaVSFVGSS 227
Cdd:cd07126 153 NFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNkiLLEANPRM--TLFTGSS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 228 AVAEHIytTASAHGKrVQAFGAAKNHAIVMPD-ADLDATVNAIMGGAFGSAGERCMALPVVVAVGDETADRLIERLKPLI 306
Cdd:cd07126 231 KVAERL--ALELHGK-VKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAGILDKLKALA 307
|
330
....*....|..
gi 446372874 307 AA-----LRIGP 313
Cdd:cd07126 308 EQrkledLTIGP 319
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
61-303 |
3.49e-13 |
|
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: 71.10 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 61 TPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALGELTRGIEVVEFACGIPHLSKgEYSFNVGSGV------DSF 134
Cdd:cd07077 14 HDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTE-RGITASVGHIqdvllpDNG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 135 SLMQ---PLGVVAGITPFNFPAMVPMWMFpVALACGNTFVLKPPALVPSASLRMAQLLQEA----GLPDGVFNVVHCGNE 207
Cdd:cd07077 93 ETYVrafPIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPFTNRALALLFQAAdaahGPKILVLYVPHPSDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 208 AASLLTSDPRVQAVSFVGSSAVAEHIYTtaSAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMGGAFgSAGERCMALPVV 287
Cdd:cd07077 172 LAEELLSHPKIDLIVATGGRDAVDAAVK--HSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNL 248
|
250
....*....|....*.
gi 446372874 288 VAVGDeTADRLIERLK 303
Cdd:cd07077 249 YVVDD-VLDPLYEEFK 263
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
41-484 |
6.56e-13 |
|
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: 70.37 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 41 EEMLAAIQSAHEAFPAWSKMtplRRARILFEFKVLLEKHRDELAALIVSEHGkvwsdaLGELTRGIEVVEFAC-GIPHLS 119
Cdd:cd07081 2 DDAVAAAKVAQQGLSCKSQE---MVDLIFRAAAEAAEDARIDLAKLAVSETG------MGRVEDKVIKNHFAAeYIYNVY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 120 KGEYSFNVGSGVDSFSLM---QPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPALVPSASLRMAQLLQEA---- 192
Cdd:cd07081 73 KDEKTCGVLTGDENGGTLiiaEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 193 GLPDGVFNVVHCGN-EAASLLTSDPRVQAVSFVGSSAVAEhiytTASAHGKRVQAFGAAKNHAIVMPDADLDATVNAIMG 271
Cdd:cd07081 153 GAPENLIGWIDNPSiELAQRLMKFPGIGLLLATGGPAVVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 272 GAFGSAGERCMALPVVVAVgDETADRLIERLKpliaalrigpgelrgkdenEMGPVVSRAHQ-QKVLGYIDKGVSEGATL 350
Cdd:cd07081 229 SKTFDNGVICASEQSVIVV-DSVYDEVMRLFE-------------------GQGAYKLTAEElQQVQPVILKNGDVNRDI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 351 VmdGRNYSVAGYPEGFYVGGT---LFDNVTP--EMTIWREEIFGPVLGIVRVPDYAT----AISTVNSHEFGNGSVIFTT 421
Cdd:cd07081 289 V--GQDAYKIAAAAGLKVPQEtriLIGEVTSlaEHEPFAHEKLSPVLAMYRAANFADadakALALKLEGGCGHTSAMYSD 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446372874 422 NGHyARE----FAQSVEAGMVGINIPVPVPMA--FHSFGGWKR-----SVFGALNVHGPDGVRFYTRMKTVTSR 484
Cdd:cd07081 367 NIK-AIEnmnqFANAMKTSRFVKNGPCSQGGLgdLYNFRGWPSmtlgcGTWGGNSVSENVGPKHLVNLKTVALR 439
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
41-428 |
6.13e-12 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 67.26 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 41 EEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHG------KVWSDAL-GELTRGIEVVEfac 113
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGmgrvedKIAKNHLaAEKTPGTEDLT--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 114 giphlskgeysFNVGSGVDSFSLMQ--PLGVVAGITPFNFPA------MVPMwmfpvaLACGNTFVLKPPalvPSA---S 182
Cdd:cd07121 81 -----------TTAWSGDNGLTLVEyaPFGVIGAITPSTNPTetiinnSISM------LAAGNAVVFNPH---PGAkkvS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 183 LRMAQLLQEA----GLPDGVFNVVHCGN-EAASLLTSDPRVQAVSFVGSSAVAEhiytTASAHGKRVQAFGAAKNHAIVM 257
Cdd:cd07121 141 AYAVELINKAiaeaGGPDNLVVTVEEPTiETTNELMAHPDINLLVVTGGPAVVK----AALSSGKKAIGAGAGNPPVVVD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 258 PDADLDATVNAIMGGAFGSAGERCMALPVVVAVgDETADRLIERLKpliaalRIGPGELRGKDENEM---------GPVV 328
Cdd:cd07121 217 ETADIEKAARDIVQGASFDNNLPCIAEKEVIAV-DSVADYLIAAMQ------RNGAYVLNDEQAEQLlevvlltnkGATP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 329 SRAHQQKVLGYIDK--GVSEGATLVMdgrnysvagypegfyvggtLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAIST 406
Cdd:cd07121 290 NKKWVGKDASKILKaaGIEVPADIRL-------------------IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIEL 350
|
410 420
....*....|....*....|....*...
gi 446372874 407 VNSHEFGN--GSVIFTTN----GHYARE 428
Cdd:cd07121 351 AVELEHGNrhTAIIHSKNvenlTKMARA 378
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
41-422 |
9.09e-12 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 66.85 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 41 EEMLAAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHG------KVWSD-ALGELTRGIEvvefaC 113
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedKIAKNvAAAEKTPGVE-----D 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 114 GIPhlskgeysfNVGSGVDSFSL--MQPLGVVAGITPFNFPA------MVPMwmfpvaLACGNTFVLKPPalvPSA---S 182
Cdd:PRK15398 111 LTT---------EALTGDNGLTLieYAPFGVIGAVTPSTNPTetiinnAISM------LAAGNSVVFSPH---PGAkkvS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 183 LRMAQLLQEAGLPD-GVFNVVHCGN----EAASLLTSDPRVQAVSFVGSSAVAEhiytTASAHGKRVQAFGAAKNHAIVM 257
Cdd:PRK15398 173 LRAIELLNEAIVAAgGPENLVVTVAeptiETAQRLMKHPGIALLVVTGGPAVVK----AAMKSGKKAIGAGAGNPPVVVD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 258 PDADLDATVNAIMGGAFGSAGERCMALPVVVAVgDETADRLIERLKpliaalRIGPGELRGKDENEMGPVV--SRAHQQK 335
Cdd:PRK15398 249 ETADIEKAARDIVKGASFDNNLPCIAEKEVIVV-DSVADELMRLME------KNGAVLLTAEQAEKLQKVVlkNGGTVNK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 336 vlgyidKGVSEGATLVMDGRNYSVAGYPEgfyvggTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAISTVNSHEFGN- 414
Cdd:PRK15398 322 ------KWVGKDAAKILEAAGINVPKDTR------LLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNr 389
|
....*....
gi 446372874 415 -GSVIFTTN 422
Cdd:PRK15398 390 hTAIMHSRN 398
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
45-404 |
2.44e-10 |
|
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: 62.88 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 45 AAIQSAHEAFPAWSKMTPLRRARILFEFKVLLEKHRDELAALIVSEHGKVWSDALG-----ELTRGIEVVEFA----CGI 115
Cdd:cd07127 88 ALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQaggphAQDRGLEAVAYAwremSRI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 116 PHLSKGEYSFNVGSGV---DSFSLM-QPLGVVAGITPFnfpamvPMW-----MFpVALACGNTFVLK--PPALVPSA-SL 183
Cdd:cd07127 168 PPTAEWEKPQGKHDPLameKTFTVVpRGVALVIGCSTF------PTWngypgLF-ASLATGNPVIVKphPAAILPLAiTV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 184 RMAQ-LLQEAGL-PDGVFNVVHC-GNEAASLLTSDPRVQAVSFVGSSAVAEHIytTASAHGKRVQAFGAAKNHAIVMPDA 260
Cdd:cd07127 241 QVAReVLAEAGFdPNLVTLAADTpEEPIAQTLATRPEVRIIDFTGSNAFGDWL--EANARQAQVYTEKAGVNTVVVDSTD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 261 DLDATVNAImggAFGSA---GERCMAlPVVVAV---GDETADrliERLKP--LIAALRIGPGELRGKDENE---MGPVVS 329
Cdd:cd07127 319 DLKAMLRNL---AFSLSlysGQMCTT-PQNIYVprdGIQTDD---GRKSFdeVAADLAAAIDGLLADPARAaalLGAIQS 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446372874 330 rahqQKVLGYIDKGvSEGATLVMDGRNYSVAGYPEGFYVGGTLFDNVTPEMTIWREEIFGPVLGIVRVPDYATAI 404
Cdd:cd07127 392 ----PDTLARIAEA-RQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSI 461
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
138-455 |
2.78e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 46.33 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 138 QPLGVVAGITPFNFPAMVPMWMFPVALACGNTFVLKPPalvPSA---SLRMAQLLQEA----GLPDGVFNVV-HCGNEAA 209
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPH---PRAkkcSIEAAKIMREAavaaGAPEGLIQWIeEPSIELT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 210 SLLTSDPRVQAVSFVGSSAVAEHIYTTasahGKRVQAFGAAKNHAIVMPDADLDATVNAI-MGGAF--GSAgerCMALPV 286
Cdd:cd07122 171 QELMKHPDVDLILATGGPGMVKAAYSS----GKPAIGVGPGNVPAYIDETADIKRAVKDIiLSKTFdnGTI---CASEQS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 287 VVAVgDETADRLIERLKPLIAALrigpgeLRGKDENEMGPVV---SRAHQQKVLGyidKGVSEGATLvmdgrnysvAGY- 362
Cdd:cd07122 244 VIVD-DEIYDEVRAELKRRGAYF------LNEEEKEKLEKALfddGGTLNPDIVG---KSAQKIAEL---------AGIe 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446372874 363 -PEGFYVGGTLFDNVTPEMTIWREEIFgPVLGIVRVPDYATAISTVNS---HEfGNG--SVIFTTNGHYAREFAQSVEAG 436
Cdd:cd07122 305 vPEDTKVLVAEETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKARElleYG-GAGhtAVIHSNDEEVIEEFALRMPVS 382
|
330
....*....|....*....
gi 446372874 437 MVGINIPvpvpmafHSFGG 455
Cdd:cd07122 383 RILVNTP-------SSLGG 394
|
|
| |
