|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
30-506 |
0e+00 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 894.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 30 VKLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKL 109
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 110 AESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVA 189
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 190 LATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKR 269
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 270 VQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTAVLVG-EARAWLPELVEKAKNLKVNAGWKPDTDIGPL 348
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 349 ISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEII 428
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71986308 429 NNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIPVPLPMFSFTGSRGSFLGDLNFYGKAGIQFYTQWKTVTQYW 506
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
30-506 |
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: 722.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 30 VKLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKL 109
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 110 AESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVA 189
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 190 LATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKR 269
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 270 VQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTAVLVGEARAWLPELVEKAKNLKVNAGWKPDTDIGPLI 349
Cdd:TIGR01722 241 VQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 350 SKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIIN 429
Cdd:TIGR01722 321 TPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALIN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71986308 430 NNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIPVPLPMFSFTGSRGSFLGDLNFYGKAGIQFYTQWKTVTQYW 506
Cdd:TIGR01722 401 ASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
28-517 |
0e+00 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 661.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 28 PTVKLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMK 107
Cdd:PLN02419 112 PRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 108 KLAESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFP 187
Cdd:PLN02419 192 KLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 188 VALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNG 267
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 268 KRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTAVLVGEARAWLPELVEKAKNLKVNAGWKPDTDIGP 347
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 348 LISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEI 427
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 428 INNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIPVPLPMFSFTGSRGSFLGDLNFYGKAGIQFYTQWKTVTQYWN 507
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQK 591
|
490
....*....|
gi 71986308 508 ESLTELKPQM 517
Cdd:PLN02419 592 DIHSPFSLAI 601
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
27-506 |
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: 548.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 27 APTVKLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDM 106
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 107 KKLAESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMF 186
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 187 PVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAK 265
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVgAALVAHPDVDKISFTGSTAVGRRIAAAAAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 266 NGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLV--GEARAWLPELVEKAKNLKVNAGWKPDT 343
Cdd:COG1012 243 NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTA-ASRLLVheSIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 344 DIGPLISKQSKARVLRLIESAKKEGAQVPLDGsniTVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNE 423
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGG---RRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 424 AIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIPVPLPMFSFTGSRGSFLGDLNfyGKAGIQFYTQWKTVT 503
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREG--GREGLEEYTETKTVT 476
|
...
gi 71986308 504 QYW 506
Cdd:COG1012 477 IRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
33-502 |
4.56e-178 |
|
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: 508.61 E-value: 4.56e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 33 WIDGQavesktTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAES 112
Cdd:pfam00171 1 WVDSE------SETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 113 ITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNvSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALAT 192
Cdd:pfam00171 75 ETLENGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 193 GNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQ-HSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQ 271
Cdd:pfam00171 154 GNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 272 SNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGPLI 349
Cdd:pfam00171 234 LELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTA-TSRLLVHEsiYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 350 SKQSKARVLRLIESAKKEGAQVPLDGSnitvPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIIN 429
Cdd:pfam00171 313 SKAQLERVLKYVEDAKEEGAKLLTGGE----AGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIAN 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71986308 430 NNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIPVPLPMFSFTGSRGSFLGDlnFYGKAGIQFYTQWKTV 502
Cdd:pfam00171 389 DTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGR--EGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
70-503 |
1.35e-137 |
|
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: 404.67 E-value: 1.35e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 70 QAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGET 149
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 150 LPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIH 229
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 230 G-QHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCM 308
Cdd:cd07078 161 GdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 309 AlTTAVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSnitVPGFENG 386
Cdd:cd07078 241 A-ASRLLVHEsiYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGK---RLEGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 387 NFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIP 466
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 71986308 467 VPLPMFSFTGSRGSFLGdlNFYGKAGIQFYTQWKTVT 503
Cdd:cd07078 397 GAEPSAPFGGVKQSGIG--REGGPYGLEEYTEPKTVT 431
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
33-502 |
1.20e-127 |
|
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: 380.83 E-value: 1.20e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 33 WIDGQAVESKTTDfvELTNPA-TNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAE 111
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 112 SITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALA 191
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 192 TGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRV 270
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 271 QSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEA--RAWLPELVEKAKNLKVNAGWKPDTDIGPL 348
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTA-SSRLIVTEGihDRFVEALVERTKALKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 349 ISKQSKARVLRLIESAKKEGAQVpLDGSNiTVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEII 428
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGAKL-VYGGE-RLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71986308 429 NNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVP-----IPVPlpmfsFTGSRGSFLGdLNFYGKAGIQFYTQWKTV 502
Cdd:cd07097 399 NDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPtagvdYHVP-----FGGRKGSSYG-PREQGEAALEFYTTIKTV 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
34-509 |
1.29e-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: 373.22 E-value: 1.29e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 34 IDGQAVESKTTDFVELTNPA-TNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAES 112
Cdd:cd07131 3 IGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 113 ITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALAT 192
Cdd:cd07131 83 VTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 193 GNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQ 271
Cdd:cd07131 163 GNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 272 SNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTAVL-VGEARAWLPELVEKAKNLKVNAGWKPDTDIGPLIS 350
Cdd:cd07131 243 LEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVhESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLIN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 351 KQSKARVLRLIESAKKEGAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINN 430
Cdd:cd07131 323 EAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAND 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 431 NPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPI---PVPLPmfsFTGSRGSFLGdLNFYGKAGIQFYTQWKTVtqYWN 507
Cdd:cd07131 403 TEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTigaEVHLP---FGGVKKSGNG-HREAGTTALDAFTEWKAV--YVD 476
|
..
gi 71986308 508 ES 509
Cdd:cd07131 477 YS 478
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
50-504 |
2.48e-114 |
|
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: 345.57 E-value: 2.48e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 50 TNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVS 129
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 130 RGLQVV----EHACSVpslmMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFP-AMIPLWMFPvALATGNTMVIKPSEQD 204
Cdd:cd07103 82 YAASFLewfaEEARRI----YGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPaAMITRKIAP-ALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 205 PGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAknHG--V 281
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG--NApfI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 282 IMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEARA--WLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLR 359
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVC-ANRIYVHESIYdeFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 360 LIESAKKEGAQVPLDGSNITvpgfENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAI 439
Cdd:cd07103 314 LVEDAVAKGAKVLTGGKRLG----LGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986308 440 FTSNGATARKFTNEVDVGQIGINVPIPvPLPMFSFTGSRGSFLGDLNfyGKAGIQFYTQWKTVTQ 504
Cdd:cd07103 390 FTRDLARAWRVAEALEAGMVGINTGLI-SDAEAPFGGVKESGLGREG--GKEGLEEYLETKYVSL 451
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
51-503 |
3.16e-112 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 340.31 E-value: 3.16e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 51 NPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAE-GDVS 129
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRDIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 130 RGLQVVEHACSVPSLMMGETLPnVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQ 209
Cdd:cd07093 83 RAAANFRFFADYILQLDGESYP-QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 210 LLVELAKEAGVPDGCVNIIHGQ-HSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANK 288
Cdd:cd07093 162 LLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 289 EQTLNQLTAAAFGAAGQRCMAlTTAVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKK 366
Cdd:cd07093 242 DRAVDAAVRSSFSNNGEVCLA-GSRILVQRsiYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 367 EGAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGAT 446
Cdd:cd07093 321 EGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 71986308 447 ARKFTNEVDVGQIGINVPIPVPLPMfSFTGSRGSFLGDLNfyGKAGIQFYTQWKTVT 503
Cdd:cd07093 401 AHRVARRLEAGTVWVNCWLVRDLRT-PFGGVKASGIGREG--GDYSLEFYTELKNVC 454
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
29-506 |
1.29e-108 |
|
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: 333.04 E-value: 1.29e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 29 TVKLWIDGQAVEskTTDFVELTNPA-TNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMK 107
Cdd:cd07124 32 EYPLVIGGKEVR--TEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 108 KLAESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVsRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFP 187
Cdd:cd07124 110 ELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMV-PGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 188 VALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYER---- 262
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERaakv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 263 --GAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTAVLVGEARAWLPE-LVEKAKNLKVNAGW 339
Cdd:cd07124 269 qpGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLErLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 340 KPDTDIGPLISKQSKARVLRLIESAKKEGaQVPLDGSniTVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAE 419
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGE--VLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 420 NLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIPVPLPMF-SFTGSRGSFLGdlnfyGKAG-----I 493
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRqPFGGFKMSGTG-----SKAGgpdylL 500
|
490
....*....|...
gi 71986308 494 QFyTQWKTVTQYW 506
Cdd:cd07124 501 QF-MQPKTVTENF 512
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
34-502 |
2.90e-105 |
|
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: 323.06 E-value: 2.90e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 34 IDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESI 113
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 114 TIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFP-AMIPLWMFPvALAT 192
Cdd:cd07088 82 VEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPfFLIARKLAP-ALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 193 GNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQ 271
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 272 SNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGPLI 349
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTC-AERVYVHEdiYDEFMEKLVEKMKAVKVGDPFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 350 SKQSKARVLRLIESAKKEGAQVPLDGSnitVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIIN 429
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGATLLTGGK---RPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986308 430 NNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIPVPLPMFSfTGSRGSFLG--DlnfyGKAGIQFYTQWKTV 502
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH-AGWKKSGLGgaD----GKHGLEEYLQTKVV 466
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
51-502 |
3.54e-104 |
|
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: 319.88 E-value: 3.54e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 51 NPATNEVIAMVPNATQAEMQAAVDSAKNAFNT--WKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDV 128
Cdd:cd07114 3 NPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 129 SRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAA 208
Cdd:cd07114 83 RYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPAST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 209 QLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADAN 287
Cdd:cd07114 163 LELAKLAEEAGFPPGVVNVVTGFGPETgEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 288 KEQTLNQLTAAAFGAAGQRCMAlTTAVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAK 365
Cdd:cd07114 243 LDAAVNGVVAGIFAAAGQTCVA-GSRLLVQRsiYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 366 KEGAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGA 445
Cdd:cd07114 322 EEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 71986308 446 TARKFTNEVDVGQIGINVPIPVPlPMFSFTGSRGSFLGDLNfyGKAGIQFYTQWKTV 502
Cdd:cd07114 402 RAHRVARAIEAGTVWVNTYRALS-PSSPFGGFKDSGIGREN--GIEAIREYTQTKSV 455
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
33-462 |
3.63e-104 |
|
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: 320.80 E-value: 3.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 33 WIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNT--WKNTSPLTRQQCMFKLQALIKRDMKKLA 110
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 111 ESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPnVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVAL 190
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYD-VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 191 ATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKR 269
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 270 VQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGP 347
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSA-GSRLLVEEsiHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 348 LISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEI 427
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430
....*....|....*....|....*....|....*
gi 71986308 428 INNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN 433
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
50-503 |
1.30e-102 |
|
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: 315.81 E-value: 1.30e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 50 TNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVS 129
Cdd:cd07150 4 LNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 130 RGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQ 209
Cdd:cd07150 84 FTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 210 LLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANK 288
Cdd:cd07150 164 KIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 289 EQTLNqltAAAFGA---AGQRCMAlTTAVLVGEA--RAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIES 363
Cdd:cd07150 244 DYAVR---AAAFGAfmhQGQICMS-ASRIIVEEPvyDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 364 AKKEGAqvpldgsNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSN 443
Cdd:cd07150 320 AVAKGA-------KLLTGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 444 GATARKFTNEVDVGQIGINVPIPVPLPMFSFTGSRGSFLGdlNFYGKAGIQFYTQWKTVT 503
Cdd:cd07150 393 LQRAFKLAERLESGMVHINDPTILDEAHVPFGGVKASGFG--REGGEWSMEEFTELKWIT 450
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
34-464 |
3.36e-101 |
|
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: 312.96 E-value: 3.36e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 34 IDGQAVESKTTDFvELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESI 113
Cdd:cd07086 3 IGGEWVGSGGETF-TSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 114 TIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATG 193
Cdd:cd07086 82 SLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 194 NTMVIKPSEQDPGAA----QLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKR 269
Cdd:cd07086 162 NTVVWKPSETTPLTAiavtKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 270 VQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCmalTTA--VLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDI 345
Cdd:cd07086 242 VLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRC---TTTrrLIVHEsvYDEFLERLVKAYKQVRIGDPLDEGTLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 346 GPLISKQSKARVLRLIESAKKEGAQVPLDGSNITvpGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAI 425
Cdd:cd07086 319 GPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRID--GGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAI 396
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 71986308 426 EIINNNPYGNGTAIFTSNGATARKFT--NEVDVGQIGINVP 464
Cdd:cd07086 397 AINNDVPQGLSSSIFTEDLREAFRWLgpKGSDCGIVNVNIP 437
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
71-503 |
6.61e-100 |
|
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: 307.92 E-value: 6.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 71 AAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETL 150
Cdd:cd07104 4 RAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 151 PNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLV-ELAKEAGVPDGCVNIIH 229
Cdd:cd07104 84 PSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGVLNVVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 230 GQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNqltAAAFGA---AGQ 305
Cdd:cd07104 164 GGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVS---AAAFGAflhQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 306 RCMAlTTAVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSnitvpgf 383
Cdd:cd07104 241 ICMA-AGRILVHEsvYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 384 ENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINV 463
Cdd:cd07104 313 YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 71986308 464 PIPVPLPMFSFTGSRGSFLGDLNfyGKAGIQFYTQWKTVT 503
Cdd:cd07104 393 QTVNDEPHVPFGGVKASGGGRFG--GPASLEEFTEWQWIT 430
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
50-502 |
7.15e-100 |
|
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: 308.30 E-value: 7.15e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 50 TNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVS 129
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 130 RGLQVVEHACSVpslmmgETLPNVSRDMDTHS---YRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPG 206
Cdd:cd07106 82 GAVAWLRYTASL------DLPDEVIEDDDTRRvelRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 207 AAQLLVELAKEAgVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADA 286
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 287 NKEQTLNQLTAAAFGAAGQRCMALTtavlvgeaRAWLPE---------LVEKAKNLKVNAGWKPDTDIGPLISKQSKARV 357
Cdd:cd07106 235 DIDAVAPKLFWGAFINSGQVCAAIK--------RLYVHEsiydefceaLVALAKAAVVGDGLDPGTTLGPVQNKMQYDKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 358 LRLIESAKKEGAQVPLDGSNITVPGFengnFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGT 437
Cdd:cd07106 307 KELVEDAKAKGAKVLAGGEPLDGPGY----FIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986308 438 AIFTSNGATARKFTNEVDVGQIGINvPIPVPLPMFSFTGSRGSFLGdLNFyGKAGIQFYTQWKTV 502
Cdd:cd07106 383 SVWSSDLERAEAVARRLEAGTVWIN-THGALDPDAPFGGHKQSGIG-VEF-GIEGLKEYTQTQVI 444
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
32-503 |
4.70e-99 |
|
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: 307.12 E-value: 4.70e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 32 LWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAE 111
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 112 SITIEQGktlpdAEGDVSRGLQVvehacSVPSLMMGETLpNVSRDMD-------THSYRIPLGVTAGICPFNFPA-MIPL 183
Cdd:cd07138 81 AITLEMG-----APITLARAAQV-----GLGIGHLRAAA-DALKDFEfeerrgnSLVVREPIGVCGLITPWNWPLnQIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 184 WMFPvALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYER 262
Cdd:cd07138 150 KVAP-ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 263 GAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTaVLVGEARawLPE----LVEKAKNLKVNAG 338
Cdd:cd07138 229 AADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTR-MLVPRSR--YAEaeeiAAAAAEAYVVGDP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 339 WKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNiTVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEA 418
Cdd:cd07138 306 RDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 419 ENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIPVPL-PmfsFTGSRGSFLGdlNFYGKAGIQFYT 497
Cdd:cd07138 385 DDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGaP---FGGYKQSGNG--REWGRYGLEEFL 459
|
....*.
gi 71986308 498 QWKTVT 503
Cdd:cd07138 460 EVKSIQ 465
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
74-503 |
5.48e-99 |
|
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: 303.38 E-value: 5.48e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 74 DSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNV 153
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 154 SRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHG-QH 232
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGgGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 233 SAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTT 312
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTA-AS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 313 AVLVGEARAwlPELVEKAKnlkvnagwkpdtdigpliskqskarvlrliesakkegaqvpldgsnitvpgfengnfvgpT 392
Cdd:cd06534 240 RLLVHESIY--DEFVEKLV------------------------------------------------------------T 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 393 ILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIPVPLPMF 472
Cdd:cd06534 258 VLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEA 337
|
410 420 430
....*....|....*....|....*....|.
gi 71986308 473 SFTGSRGSFLGDLNfyGKAGIQFYTQWKTVT 503
Cdd:cd06534 338 PFGGVKNSGIGREG--GPYGLEEYTRTKTVV 366
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
28-503 |
7.03e-99 |
|
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: 306.83 E-value: 7.03e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 28 PTvKLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNT--WKNTSPLTRQQCMFKLQALIKRD 105
Cdd:cd07091 3 PT-GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 106 MKKLAESITIEQGKTLPD-AEGDVSRGLQVVEHACSVPSLMMGETLPNvsrDMDTHSY--RIPLGVTAGICPFNFPAMIP 182
Cdd:cd07091 82 RDELAALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGKTIPI---DGNFLAYtrREPIGVCGQIIPWNFPLLML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 183 LWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQ-HSAVNFICDNPDIKAISFVGGDAAGKHIYE 261
Cdd:cd07091 159 AWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFgPTAGAAISSHMDVDKIAFTGSTAVGRTIME 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 262 RGAK-NGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEA--RAWLPELVEKAKNLKVNAG 338
Cdd:cd07091 239 AAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCA-GSRIFVQESiyDEFVEKFKARAEKRVVGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 339 WKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFengnFVGPTILAGVKPNMTCYREEIFGPVLVVMEA 418
Cdd:cd07091 318 FDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGY----FIQPTVFTDVKDDMKIAKEEIFGPVVTILKF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 419 ENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVpIPVPLPMFSFTGSRGSFLG-DLnfyGKAGIQFYT 497
Cdd:cd07091 394 KTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNT-YNVFDAAVPFGGFKQSGFGrEL---GEEGLEEYT 469
|
....*.
gi 71986308 498 QWKTVT 503
Cdd:cd07091 470 QVKAVT 475
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
32-462 |
7.98e-96 |
|
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: 298.72 E-value: 7.98e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 32 LWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFN--TWKNTSPLTRQQCMFKLQALIKRDMKKL 109
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDngPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 110 AESITIEQGKTLP--------------DAEGDVSRGLQVVEHacsVPSLMMGETLpnVSRDmdthsyriPLGVTAGICPF 175
Cdd:cd07139 81 ARLWTAENGMPISwsrraqgpgpaallRYYAALARDFPFEER---RPGSGGGHVL--VRRE--------PVGVVAAIVPW 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 176 NFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAA 255
Cdd:cd07139 148 NAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 256 GKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTaVLVGEAR--AWLPELVEKAKNL 333
Cdd:cd07139 228 GRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTR-ILVPRSRydEVVEALAAAVAAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 334 KVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSniTVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVL 413
Cdd:cd07139 307 KVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGG--RPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVL 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 71986308 414 VVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:cd07139 385 SVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN 433
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
51-502 |
2.32e-95 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 297.29 E-value: 2.32e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 51 NPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSR 130
Cdd:cd07090 3 EPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 131 GLQVVEHACSVPSLMMGETLPnvsrdMDTHSY----RIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPG 206
Cdd:cd07090 83 SADCLEYYAGLAPTLSGEHVP-----LPGGSFaytrREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 207 AAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADA 286
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 287 NKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEAR--AWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESA 364
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSN-GTRVFVQRSIkdEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 365 KKEGAQVPLDGSNITV-PGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSN 443
Cdd:cd07090 317 KQEGAKVLCGGERVVPeDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71986308 444 GATARKFTNEVDVGQIGIN----VPIPVPlpmfsFTGSRGSFLGDLNfyGKAGIQFYTQWKTV 502
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
31-462 |
1.78e-93 |
|
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: 292.94 E-value: 1.78e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 31 KLWIDGQAVESKTtDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLT-RQQCMFKLQALIKRDMKKL 109
Cdd:cd07082 3 KYLINGEWKESSG-KTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLEeRIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 110 AESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLP----NVSRDMDTHSYRIPLGVTAGICPFNFP------A 179
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPgdwfPGTKGKIAQVRREPLGVVLAIGPFNYPlnltvsK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 180 MIPlwmfpvALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKH 258
Cdd:cd07082 162 LIP------ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIgDPLVTHGRIDVISFTGSTEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 259 IyergAKNGKRVQSNM--GAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTaVLVGE--ARAWLPELVEKAKNLK 334
Cdd:cd07082 236 L----KKQHPMKRLVLelGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-VLVHEsvADELVELLKEEVAKLK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 335 VNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGsnitvpGFENGNFVGPTILAGVKPNMTCYREEIFGPVLV 414
Cdd:cd07082 311 VGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLP 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 71986308 415 VMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:cd07082 385 IIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN 432
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
48-462 |
5.05e-93 |
|
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: 291.04 E-value: 5.05e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 48 ELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGD 127
Cdd:cd07149 2 EVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 128 VSRGLQVVEHACSVPSLMMGETLPnvsrdMDTH---------SYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVI 198
Cdd:cd07149 82 VDRAIETLRLSAEEAKRLAGETIP-----FDASpggegrigfTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 199 KPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKngKRVQSNMGAk 277
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKAGL--KKVTLELGS- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 278 NHGVI-MADANKEQTLNQLTAAAFGAAGQRCMALTTaVLVGEAR--AWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSK 354
Cdd:cd07149 234 NAAVIvDADADLEKAVERCVSGAFANAGQVCISVQR-IFVHEDIydEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 355 ARVLRLIESAKKEGAQVPLDGSNitvpgfeNGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYG 434
Cdd:cd07149 313 ERIEEWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYG 385
|
410 420
....*....|....*....|....*...
gi 71986308 435 NGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:cd07149 386 LQAGVFTNDLQKALKAARELEVGGVMIN 413
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
32-503 |
5.54e-92 |
|
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: 288.96 E-value: 5.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 32 LWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAF-NTWKNTSPLTRQQCMFKLQALIKRDMKKLA 110
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 111 ESITIEQGKTLpdaegDVSRGLQVvehACSVPSL---------MMGETLPNVSRDMDTHSY-----RIPLGVTAGICPFN 176
Cdd:cd07113 82 QLETLCSGKSI-----HLSRAFEV---GQSANFLryfagwatkINGETLAPSIPSMQGERYtaftrREPVGVVAGIVPWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 177 FPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAG 256
Cdd:cd07113 154 FSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 257 KHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCmALTTAVLVGEARawLPELVEKAK----N 332
Cdd:cd07113 234 KKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVC-AAPERFYVHRSK--FDELVTKLKqalsS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 333 LKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFengnFVGPTILAGVKPNMTCYREEIFGPV 412
Cdd:cd07113 311 FQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGY----FVQPTLVLARSADSRLMREETFGPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 413 LVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIPVPlPMFSFTGSRGSFLGdlNFYGKAG 492
Cdd:cd07113 387 VSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLD-PAVPFGGMKQSGIG--REFGSAF 463
|
490
....*....|.
gi 71986308 493 IQFYTQWKTVT 503
Cdd:cd07113 464 IDDYTELKSVM 474
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
28-502 |
1.65e-91 |
|
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: 288.15 E-value: 1.65e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 28 PTvKLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAF-NTWKNTSPLTRQQCMFKLQALIKRDM 106
Cdd:cd07144 7 PT-GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFeSWWSKVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 107 KKLAESITIEQGKTL-PDAEGDVSRGLQVVEHACSVPSLMMGETLPNvsrDMDTHSY--RIPLGVTAGICPFNFPAMIPL 183
Cdd:cd07144 86 DLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPT---SPNKLAYtlHEPYGVCGQIIPWNYPLAMAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 184 WMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYER 262
Cdd:cd07144 163 WKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAgSALAEHPDVDKIAFTGSTATGRLVMKA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 263 GAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEA--RAWLPELVEKAK-NLKVNAGW 339
Cdd:cd07144 243 AAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTA-TSRIYVQESiyDKFVEKFVEHVKqNYKVGSPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 340 KPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSnITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAE 419
Cdd:cd07144 322 DDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGE-KAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 420 NLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVP----IPVPlpmfsFTGSRGSFLGdlNFYGKAGIQF 495
Cdd:cd07144 401 TYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMSGIG--RELGEYGLET 473
|
....*..
gi 71986308 496 YTQWKTV 502
Cdd:cd07144 474 YTQTKAV 480
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
51-502 |
2.15e-90 |
|
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: 284.52 E-value: 2.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 51 NPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWK-NTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAE---- 125
Cdd:cd07089 3 NPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARamqv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 126 ----GDVSRGLQVV-----EHACSVPSLMMGETLPNVSRDmdthsyriPLGVTAGICPFNFPAMIPLWMFPVALATGNTM 196
Cdd:cd07089 83 dgpiGHLRYFADLAdsfpwEFDLPVPALRGGPGRRVVRRE--------PVGVVAAITPWNFPFFLNLAKLAPALAAGNTV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 197 VIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQ-HSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMG 275
Cdd:cd07089 155 VLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSdNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 276 AKNHGVIMADANkeqtLNQLTAAAFG----AAGQRCmALTTAVLVGEARawLPELVEKAKN----LKVNAGWKPDTDIGP 347
Cdd:cd07089 235 GKSANIVLDDAD----LAAAAPAAVGvcmhNAGQGC-ALTTRLLVPRSR--YDEVVEALAAafeaLPVGDPADPGTVMGP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 348 LISKQSKARVLRLIESAKKEGAQVPLDGSniTVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEI 427
Cdd:cd07089 308 LISAAQRDRVEGYIARGRDEGARLVTGGG--RPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRI 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71986308 428 INNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN----VPIPVPlpmfsFTGSRGSFLGdlNFYGKAGIQFYTQWKTV 502
Cdd:cd07089 386 ANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINggggYGPDAP-----FGGYKQSGLG--RENGIEGLEEFLETKSI 457
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
51-462 |
3.63e-89 |
|
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: 281.04 E-value: 3.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 51 NPATNEVIAMVPNATQAEMQAAVDSAKNAFNT-WKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVS 129
Cdd:cd07109 3 DPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 130 RGLQVVEHACSVPSLMMGETLPnVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQ 209
Cdd:cd07109 83 AAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 210 LLVELAKEAGVPDGCVNIIHGQ-HSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANK 288
Cdd:cd07109 162 RLAELAEEAGLPAGALNVVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 289 EQTLNQLTAAAFGAAGQRCMAlTTAVLVGEA--RAWLPELVEKAKNLKVNAGwKPDTDIGPLISKQSKARVLRLIESAKK 366
Cdd:cd07109 242 EAALPVVVNAIIQNAGQTCSA-GSRLLVHRSiyDEVLERLVERFRALRVGPG-LEDPDLGPLISAKQLDRVEGFVARARA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 367 EGAQVpLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGAT 446
Cdd:cd07109 320 RGARI-VAGGRIAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410
....*....|....*.
gi 71986308 447 ARKFTNEVDVGQIGIN 462
Cdd:cd07109 399 ALRVARRLRAGQVFVN 414
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
47-462 |
2.26e-88 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 278.85 E-value: 2.26e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 47 VELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEG 126
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 127 DVSRGLQVVEHACSVPSLMMGETLPnvsrdMDTHSY---------RIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMV 197
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIP-----VDAYEYnerriaftvREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 198 IKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGA 276
Cdd:cd07145 156 VKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 277 KNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSK 354
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNA-VKRILVEEevYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 355 ARVLRLIESAKKEGAQVPLDGSNItvpgfeNGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYG 434
Cdd:cd07145 315 ERMENLVNDAVEKGGKILYGGKRD------EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYG 388
|
410 420
....*....|....*....|....*...
gi 71986308 435 NGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:cd07145 389 LQASVFTNDINRALKVARELEAGGVVIN 416
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
33-503 |
8.38e-88 |
|
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: 277.65 E-value: 8.38e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 33 WIDGQAVESkttdfVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAES 112
Cdd:cd07151 3 WRDGTSERT-----IDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 113 ITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALAT 192
Cdd:cd07151 78 LIRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 193 GNTMVIKPSEQDPGAAQLLV-ELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRV 270
Cdd:cd07151 158 GNAVVLKPASDTPITGGLLLaKIFEEAGLPKGVLNVVVGAGSEIgDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 271 QSNMGAKNHGVIMADANKEQTLNqltAAAFGA---AGQRCMALTTaVLVGEARA--WLPELVEKAKNLKVNAGWKPDTDI 345
Cdd:cd07151 238 ALELGGNNPFVVLEDADIDAAVN---AAVFGKflhQGQICMAINR-IIVHEDVYdeFVEKFVERVKALPYGDPSDPDTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 346 GPLISKQSKARVLRLIESAKKEGAQVPLDGSnitvpgfENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAI 425
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGE-------AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEAL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 426 EIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINvPIPV-PLPMFSFTGSRGSFLGDLNfyGKAGIQFYT--QWKTV 502
Cdd:cd07151 387 ELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVnDEPHVPFGGEKNSGLGRFN--GEWALEEFTtdKWISV 463
|
.
gi 71986308 503 T 503
Cdd:cd07151 464 Q 464
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
52-503 |
1.42e-87 |
|
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: 276.91 E-value: 1.42e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 52 PATNEVIAMVPNATQAEMQAAVDSAKNAFNT--WKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVS 129
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 130 RGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQ 209
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 210 LLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANK 288
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 289 EQTLNqltAAAFGA---AGQRCMAlTTAVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIES 363
Cdd:cd07118 244 DAAAD---AVVFGVyfnAGECCNS-GSRLLVHEsiADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 364 AKKEGAQVPLDGSNItvpGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSN 443
Cdd:cd07118 320 GRAEGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71986308 444 GATARKFTNEVDVGQIGINVPIP--VPLPmfsFTGSRGSFLGDLNfyGKAGIQFYTQWKTVT 503
Cdd:cd07118 397 IDTALTVARRIRAGTVWVNTFLDgsPELP---FGGFKQSGIGREL--GRYGVEEYTELKTVH 453
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
32-462 |
1.82e-87 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 278.36 E-value: 1.82e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 32 LWIDGQAVEskTTDFVELTNPA-TNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLA 110
Cdd:PRK03137 39 LIIGGERIT--TEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 111 ESITIEQGKTLPDAEGDVSRGLQVVE-HACSVPSLMMGEtlPNVSR-DMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPV 188
Cdd:PRK03137 117 AWLVKEAGKPWAEADADTAEAIDFLEyYARQMLKLADGK--PVESRpGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 189 ALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAK-- 265
Cdd:PRK03137 195 AIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFITFTGSREVGLRIYERAAKvq 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 266 NG----KRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTAVLVGEARAWLPE-LVEKAKNLKVNAGWK 340
Cdd:PRK03137 275 PGqiwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEkVVELTKELTVGNPED 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 341 PDtDIGPLISKQSKARVLRLIESAKKEGaQVPLDGSNitvpGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAEN 420
Cdd:PRK03137 355 NA-YMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEG----DDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKD 428
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 71986308 421 LNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN 470
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
51-502 |
1.51e-86 |
|
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: 274.32 E-value: 1.51e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 51 NPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEG-DVS 129
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 130 RGLQVVEHACSVPSLMMGETLPnVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQ 209
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 210 LLVELAKEAGVPDGCVNIIHGQ-HSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANK 288
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 289 EQTLNQLTAAAFGAAGQRCMAlTTAVLVGEARA--WLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKK 366
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTA-GSRLLVHESIYdeFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 367 EGAQVPLDGSNITVPGFengnFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGAT 446
Cdd:cd07115 321 EGARLLTGGKRPGARGF----FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 71986308 447 ARKFTNEVDVGQIGINV--PIPVPLPmfsFTGSRGSFLGDLNfyGKAGIQFYTQWKTV 502
Cdd:cd07115 397 AHRVAAALKAGTVWINTynRFDPGSP---FGGYKQSGFGREM--GREALDEYTEVKSV 449
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
51-503 |
3.87e-86 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 273.05 E-value: 3.87e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 51 NPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPD-AEGDVS 129
Cdd:cd07092 3 DPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 130 RGLQVVEH----ACSVPSLMMGETLPNVSrdmdTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDP 205
Cdd:cd07092 83 GAVDNFRFfagaARTLEGPAAGEYLPGHT----SMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 206 GAAQLLVELAKEaGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMA 284
Cdd:cd07092 159 LTTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 285 DANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEA--RAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIE 362
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTA-ACRVYVHESvyDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 363 SAKKeGAQVPLDGSNITVPGFengnFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTS 442
Cdd:cd07092 317 RAPA-HARVLTGGRRAEGPGY----FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71986308 443 NGATARKFTNEVDVGQIGINVPIPVPLPMfSFTGSRGSFLG-DLNFYgkaGIQFYTQWKTVT 503
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEM-PHGGFKQSGYGkDLSIY---ALEDYTRIKHVM 449
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
31-503 |
7.57e-86 |
|
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: 273.45 E-value: 7.57e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 31 KLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAF---NTWKNTSPLTRQQCMFKLQALIKRDMK 107
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 108 KLAESITIEQGKTLPDA-EGDVSRGLQVVEHACSVPSLMMGETLPnvsRDMDTHSY-RI-PLGVTAGICPFNFPAMIPLW 184
Cdd:cd07141 88 YLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIP---MDGDFFTYtRHePVGVCGQIIPWNFPLLMAAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 185 MFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHG-QHSAVNFICDNPDIKAISFVGGDAAGKHIYERG 263
Cdd:cd07141 165 KLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 264 AK-NGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEA--RAWLPELVEKAKNLKVNAGWK 340
Cdd:cd07141 245 GKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCA-GSRTFVQESiyDEFVKRSVERAKKRVVGNPFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 341 PDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFengnFVGPTILAGVKPNMTCYREEIFGPVLVVMEAEN 420
Cdd:cd07141 324 PKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 421 LNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIPVPlPMFSFTGSRGSFLGDLNfyGKAGIQFYTQWK 500
Cdd:cd07141 400 IDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGREL--GEYGLQEYTEVK 476
|
...
gi 71986308 501 TVT 503
Cdd:cd07141 477 TVT 479
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
34-502 |
1.03e-84 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 270.79 E-value: 1.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 34 IDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESI 113
Cdd:PLN02278 29 IGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 114 TIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFP-AMIPLWMFPvALAT 192
Cdd:PLN02278 109 TLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITRKVGP-ALAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 193 GNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQ 271
Cdd:PLN02278 188 GCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 272 SNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEA--RAWLPELVEKAKNLKVNAGWKPDTDIGPLI 349
Cdd:PLN02278 268 LELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVC-ANRILVQEGiyDKFAEAFSKAVQKLVVGDGFEEGVTQGPLI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 350 SKQSKARVLRLIESAKKEGAQVPLDGSnitvPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIIN 429
Cdd:PLN02278 347 NEAAVQKVESHVQDAVSKGAKVLLGGK----RHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAN 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71986308 430 NNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIpVPLPMFSFTGSRGSFLGDLNfyGKAGIQFYTQWKTV 502
Cdd:PLN02278 423 DTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLGREG--SKYGIDEYLEIKYV 492
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
51-504 |
2.99e-84 |
|
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: 268.45 E-value: 2.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 51 NPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSR 130
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 131 GLQVVEH---ACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGA 207
Cdd:cd07110 83 VAGCFEYyadLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 208 AQLLVELAKEAGVPDGCVNIIHGQHSAVNF-ICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADA 286
Cdd:cd07110 163 ELELAEIAAEAGLPPGVLNVVTGTGDEAGApLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 287 NKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESA 364
Cdd:cd07110 243 DLEKAVEWAMFGCFWNNGQICSA-TSRLLVHEsiADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 365 KKEGAQVPLDGSnitVP-GFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSN 443
Cdd:cd07110 322 KEEGARLLCGGR---RPaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71986308 444 GATARKFTNEVDVGQIGINVPIPVpLPMFSFTGSRGSFLG-DLnfyGKAGIQFYTQWKTVTQ 504
Cdd:cd07110 399 AERCDRVAEALEAGIVWINCSQPC-FPQAPWGGYKRSGIGrEL---GEWGLDNYLEVKQITR 456
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
51-502 |
7.05e-83 |
|
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: 264.85 E-value: 7.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 51 NPATNEVIAMVPNATQAEMQAAVDSAKNAFN--TWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDA-EGD 127
Cdd:cd07112 8 NPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAlAVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 128 VSRGLQVVEHACSVPSLMMGETLPnVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGA 207
Cdd:cd07112 88 VPSAANTFRWYAEAIDKVYGEVAP-TGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 208 AQLLVELAKEAGVPDGCVNIIHG-QHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAK-NGKRVQSNMGAKNHGVIMAD 285
Cdd:cd07112 167 ALRLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 286 A-NKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEARA--WLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIE 362
Cdd:cd07112 247 ApDLDAAAEAAAAGIFWNQGEVCSA-GSRLLVHESIKdeFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 363 SAKKEGAQVPLDGSNITVPGfeNGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTS 442
Cdd:cd07112 326 SGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTS 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986308 443 NGATARKFTNEVDVGQIGIN----VPIPVPlpmfsFTGSRGSFLG-DLNFYgkaGIQFYTQWKTV 502
Cdd:cd07112 404 DLSRAHRVARRLRAGTVWVNcfdeGDITTP-----FGGFKQSGNGrDKSLH---ALDKYTELKTT 460
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
25-502 |
1.29e-82 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 265.21 E-value: 1.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 25 AAAPTVKLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKR 104
Cdd:PRK13252 2 SRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 105 DMKKLAESITIEQGKTLPDAE-GDVSRGLQVVEH-ACSVPSLMmGETLPnvSRDMD-THSYRIPLGVTAGICPFNFPAMI 181
Cdd:PRK13252 82 RNDELAALETLDTGKPIQETSvVDIVTGADVLEYyAGLAPALE-GEQIP--LRGGSfVYTRREPLGVCAGIGAWNYPIQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 182 PLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYE 261
Cdd:PRK13252 159 ACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 262 RGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCmalT--TAVLVGEA--RAWLPELVEKAKNLKVNA 337
Cdd:PRK13252 239 AAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVC---TngTRVFVQKSikAAFEARLLERVERIRIGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 338 GWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVME 417
Cdd:PRK13252 316 PMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 418 AENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINV--PIPVPLPmfsFTGSRGSFLGDLNfyGKAGIQF 495
Cdd:PRK13252 396 FDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPAEMP---VGGYKQSGIGREN--GIATLEH 470
|
....*..
gi 71986308 496 YTQWKTV 502
Cdd:PRK13252 471 YTQIKSV 477
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
30-502 |
3.89e-82 |
|
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: 263.62 E-value: 3.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 30 VKLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNT-W-KNTSPLTRQQCMFKLQALIKRDMK 107
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWgLKVSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 108 KLAESITIEQGKTLPDAEG-DVSRGLQVVEHACSVPSLMMGETLPNVSRDMdTHSYRIPLGVTAGICPFNFPAMIPLWMF 186
Cdd:cd07143 87 YLASIEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVIETDIKKL-TYTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 187 PVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAK 265
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 266 -NGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEA--RAWLPELVEKAKNLKVNAGWKPD 342
Cdd:cd07143 246 sNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCA-GSRIYVQEGiyDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 343 TDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFengnFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLN 422
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY----FIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 423 EAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIPVPlPMFSFTGSRGSFLGdlNFYGKAGIQFYTQWKTV 502
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLH-HQVPFGGYKQSGIG--RELGEYALENYTQIKAV 477
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
50-503 |
1.85e-79 |
|
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: 255.75 E-value: 1.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 50 TNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTL-PDAEGDV 128
Cdd:cd07108 2 INPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 129 SRGLQVVEHACSVPSLMMGETLPnVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAA 208
Cdd:cd07108 82 AVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 209 QLLVELAKEAgVPDGCVNIIHGQHSAVNF-ICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADAN 287
Cdd:cd07108 161 LLLAEILAQV-LPAGVLNVITGYGEECGAaLVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 288 KEQTLNQLTAAA-FGAAGQRCMAlTTAVLVGEA--RAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESA 364
Cdd:cd07108 240 LDDAVDGAIAGMrFTRQGQSCTA-GSRLFVHEDiyDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 365 KKE-GAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSN 443
Cdd:cd07108 319 LSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 444 GATARKFTNEVDVGQIGINVPIpVPLPMFSFTGSRGSFLGDlNFYGKAGIQFYTQWKTVT 503
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLGR-EASLEGMLEHFTQKKTVN 456
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
31-462 |
3.87e-78 |
|
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: 253.04 E-value: 3.87e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 31 KLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLA 110
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 111 ESITIEQGKTLPDAEG-DVSrglQVVEHACSVPSLMMGETLPNVSRDMDTHSY--RIPLGVTAGICPFNFPAMIPLWMFP 187
Cdd:cd07559 82 VAETLDNGKPIRETLAaDIP---LAIDHFRYFAGVIRAQEGSLSEIDEDTLSYhfHEPLGVVGQIIPWNFPLLMAAWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 188 VALATGNTMVIKPSEQDPGAAQLLVELAKEAgVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKN 266
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAgKPLASHPRIAKLAFTGSTTVGRLIMQYAAEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 267 GKRVQSNMGAKNHGVIMADANKEQT--LNQLTAAAFGAA---GQRCMALTTAvLVGEA--RAWLPELVEKAKNLKVNAGW 339
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDAMDADDdfDDKAEEGQLGFAfnqGEVCTCPSRA-LVQESiyDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 340 KPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAE 419
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 71986308 420 NLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN 439
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
70-503 |
4.16e-78 |
|
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: 251.73 E-value: 4.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 70 QAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGET 149
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 150 LPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIH 229
Cdd:cd07105 83 IPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 230 gqHSA------VNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAA 303
Cdd:cd07105 163 --HSPedapevVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 304 GQRCMAlTTAVLVGE--ARAWLPELVEKAKNLKvnagwKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVP 381
Cdd:cd07105 241 GQICMS-TERIIVHEsiADEFVEKLKAAAEKLF-----AGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 382 GfenGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGI 461
Cdd:cd07105 315 S---GTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHI 391
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 71986308 462 NVPIPVPLPMFSFTGSRGSFLGdlNFYGKAGIQFYTQWKTVT 503
Cdd:cd07105 392 NGMTVHDEPTLPHGGVKSSGYG--RFNGKWGIDEFTETKWIT 431
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
49-462 |
5.83e-78 |
|
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: 251.91 E-value: 5.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 49 LTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDV 128
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 129 SRGLQVVEHACSVPSLMMGETLPNVSRDMDtHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAA 208
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLH-YTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 209 QLLVELAKEAgVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADAN 287
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 288 KEQTLNQLTAAA-FGAAGQRCMAlTTAVLVGEA--RAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESA 364
Cdd:cd07107 239 PEAAADAAVAGMnFTWCGQSCGS-TSRLFVHESiyDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 365 KKEGAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNG 444
Cdd:cd07107 318 KREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410
....*....|....*...
gi 71986308 445 ATARKFTNEVDVGQIGIN 462
Cdd:cd07107 398 SQAHRTARRVEAGYVWIN 415
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
56-503 |
9.62e-78 |
|
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: 251.06 E-value: 9.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 56 EVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSRGLQVV 135
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 136 EHACSVPSLMMGETLPNVSRDMdTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLV-EL 214
Cdd:cd07152 82 HEAAGLPTQPQGEILPSAPGRL-SLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIaRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 215 AKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQ 294
Cdd:cd07152 161 FEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 295 LTAAAFGAAGQRCMAlTTAVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVP 372
Cdd:cd07152 241 GAWGAFLHQGQICMA-AGRHLVHEsvADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 373 LDGSNitvpgfeNGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTN 452
Cdd:cd07152 320 AGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 71986308 453 EVDVGQIGINVPIPVPLPMFSFTGSRGSFLGDlNFYGKAGIQFYTQWKTVT 503
Cdd:cd07152 393 RLRTGMLHINDQTVNDEPHNPFGGMGASGNGS-RFGGPANWEEFTQWQWVT 442
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
31-502 |
1.09e-77 |
|
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: 251.99 E-value: 1.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 31 KLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLA 110
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 111 ESITIEQGKTLPDaegdvSRGLQV---VEHACSVPSLMMGETLPNVSRDMDTHS--YRIPLGVTAGICPFNFPAMIPLWM 185
Cdd:cd07117 82 MVETLDNGKPIRE-----TRAVDIplaADHFRYFAGVIRAEEGSANMIDEDTLSivLREPIGVVGQIIPWNFPFLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 186 FPVALATGNTMVIKPSEQDPGAaqlLVELAK--EAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYER 262
Cdd:cd07117 157 LAPALAAGNTVVIKPSSTTSLS---LLELAKiiQDVLPKGVVNIVTGKGSKSgEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 263 GAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEA--RAWLPELVEKAKNLKVNAGWK 340
Cdd:cd07117 234 AAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCA-GSRIFVQEGiyDEFVAKLKEKFENVKVGNPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 341 PDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAEN 420
Cdd:cd07117 313 PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 421 LNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINV--PIPVPLPmfsFTGSRGSFLGDLNFygKAGIQFYTQ 498
Cdd:cd07117 393 EDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTynQIPAGAP---FGGYKKSGIGRETH--KSMLDAYTQ 467
|
....
gi 71986308 499 WKTV 502
Cdd:cd07117 468 MKNI 471
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
47-503 |
2.15e-76 |
|
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: 247.73 E-value: 2.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 47 VELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEG 126
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 127 DVSRGLQVVEHACSVPSLMMGETLP-NVSRDMDTH---SYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSE 202
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPlDATQGSDNRlawTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 203 QDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAknGKRVQSNMGAKNHGV 281
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLgDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 282 IMADANKEQTLNQLTAAAFGAAGQRCMALTTAVLVGE-ARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRL 360
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEElYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 361 IESAKKEGAQVPLDGSnitvpgfENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIF 440
Cdd:cd07094 319 VEEAVEAGARLLCGGE-------RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71986308 441 TSNGATARKFTNEVDVGQIGINVPIPVPLPMFSFTGSRGSflgdlnFYGKAGIQF----YTQWKTVT 503
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKES------GVGREGVPYameeMTEEKTVV 452
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
29-466 |
2.72e-76 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 248.29 E-value: 2.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 29 TVKLWIDGQAVESKTTDFvELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKK 108
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQ-PVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 109 LAESITIEQGKTLPDA-EGDVSRGLQVVEH----ACSVPSLMMGETLPN----VSRDmdthsyriPLGVTAGICPFNFPA 179
Cdd:PRK13473 81 FARLESLNCGKPLHLAlNDEIPAIVDVFRFfagaARCLEGKAAGEYLEGhtsmIRRD--------PVGVVASIAPWNYPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 180 MIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAgVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKH 258
Cdd:PRK13473 153 MMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIATGKH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 259 IYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVgeARAWLPELVEK----AKNLK 334
Cdd:PRK13473 232 VLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTA-ACRIYA--QRGIYDDLVAKlaaaVATLK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 335 VNAGWKPDTDIGPLISKQSKARVLRLIESAKKEG-AQVPLDGSNITVPGFengnFVGPTILAGVKPNMTCYREEIFGPVL 413
Cdd:PRK13473 309 VGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGY----YYEPTLLAGARQDDEIVQREVFGPVV 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 71986308 414 VVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIP 466
Cdd:PRK13473 385 SVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM 437
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
48-503 |
8.98e-76 |
|
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: 246.12 E-value: 8.98e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 48 ELTNPATNEVIAMVPNATQAEMQAAVDSAKNafntwkNTSPLTRQQ---CMFKLQALIKRDMKKLAESITIEQGKTLPDA 124
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALAAS------YRSTLTRYQrsaILNKAAALLEARREEFARLITLESGLCLKDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 125 EGDVSRGLQVVEHACSVPSLMMGETLpnvSRDMDTH-------SYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMV 197
Cdd:cd07146 76 RYEVGRAADVLRFAAAEALRDDGESF---SCDLTANgkarkifTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 198 IKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAknGKRVQSNMGA 276
Cdd:cd07146 153 LKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIgDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 277 KNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTaVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSK 354
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKR-ILVHEsvADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 355 ARVLRLIESAKKEGAQVPLDGSnitvpgfENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYG 434
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQ-------RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYG 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71986308 435 NGTAIFTSNGATARKFTNEVDVGQIGINvpiPVP---LPMFSFTGSRGSFLGdlnfyGKAGIQ----FYTQWKTVT 503
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVN---EVPgfrSELSPFGGVKDSGLG-----GKEGVReamkEMTNVKTYS 450
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
51-504 |
1.81e-75 |
|
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: 245.33 E-value: 1.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 51 NPATNEVIAMVPNATQAEMQAAVDSAKNAFN--TWKnTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDV 128
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 129 SRGLQVVEHACSVPSLM---MGETLP-NVSRDMdthsyRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQD 204
Cdd:cd07120 82 SGAISELRYYAGLARTEagrMIEPEPgSFSLVL-----REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 205 PG-AAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVI 282
Cdd:cd07120 157 AQiNAAIIRILAEIPSLPAGVVNLFTESGSEGaAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 283 MADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEARA--WLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRL 360
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMA-GSRVLVQRSIAdeVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 361 IESAKKEGAQVPLDGSNITvPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIF 440
Cdd:cd07120 316 VERAIAAGAEVVLRGGPVT-EGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71986308 441 TSNGATARKFTNEVDVGQIGINVPIPVpLPMFSFTGSRGSFLGDLNfyGKAGIQFYTQWKTVTQ 504
Cdd:cd07120 395 TRDLARAMRVARAIRAGTVWINDWNKL-FAEAEEGGYRQSGLGRLH--GVAALEDFIEYKHIYL 455
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
69-462 |
4.20e-75 |
|
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: 243.52 E-value: 4.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 69 MQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSRGLQVVEH-ACSVPSLMMG 147
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 148 ETLPnvSRDMDTHSYRIPLGVTAGICPFNFPamipLW-MFPVA---LATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDG 223
Cdd:cd07100 81 EPIE--TDAGKAYVRYEPLGVVLGIMPWNFP----FWqVFRFAapnLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 224 CVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAA 303
Cdd:cd07100 155 VFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 304 GQRCMAlttA--VLVGEARA--WLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQV-----PLD 374
Cdd:cd07100 235 GQSCIA---AkrFIVHEDVYdeFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLllggkRPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 375 GsnitvpgfeNGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEV 454
Cdd:cd07100 312 G---------PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRL 382
|
....*...
gi 71986308 455 DVGQIGIN 462
Cdd:cd07100 383 EAGMVFIN 390
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
47-464 |
6.40e-73 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 238.68 E-value: 6.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 47 VELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEG 126
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 127 DVSRGLQVVEHACSVPSLMMGETLPnvsrdMDTHS---------YRIPLGVTAGICPFNFPamIPLWMFPVA--LATGNT 195
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLP-----LDISArgegrqglvRRFPIGPVSAITPFNFP--LNLVAHKVApaIAAGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 196 MVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKngKRVQSNMG 275
Cdd:cd07147 154 FVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 276 AkNHGVIM-ADANKEQTLNQLTAAAFGAAGQRCMALTTaVLVGEAR--AWLPELVEKAKNLKVNAGWKPDTDIGPLISKQ 352
Cdd:cd07147 232 G-NAAVIVdSDADLDFAAQRIIFGAFYQAGQSCISVQR-VLVHRSVydEFKSRLVARVKALKTGDPKDDATDVGPMISES 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 353 SKARVLRLIESAKKEGAqvpldgsNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNP 432
Cdd:cd07147 310 EAERVEGWVNEAVDAGA-------KLLTGGKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSK 382
|
410 420 430
....*....|....*....|....*....|...
gi 71986308 433 YGNGTAIFTSNGATARKFTNEVDVGQIGIN-VP 464
Cdd:cd07147 383 FGLQAGVFTRDLEKALRAWDELEVGGVVINdVP 415
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
31-462 |
7.40e-71 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 234.72 E-value: 7.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 31 KLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFN--TWKNTSPLTRQQCMFKLQALIKRDMKK 108
Cdd:PLN02766 22 KLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 109 LAESITIEQGKTLPDAEG-DVSRGLQVVEHACSVPSLMMGETLpNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFP 187
Cdd:PLN02766 102 LAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETL-KMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 188 VALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHG-QHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAK- 265
Cdd:PLN02766 181 PALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATs 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 266 NGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEA--RAWLPELVEKAKNLKVNAGWKPDT 343
Cdd:PLN02766 261 NLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVA-SSRVYVQEGiyDEFVKKLVEKAKDWVVGDPFDPRA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 344 DIGPLISKQSKARVLRLIESAKKEGAQVPLDGSnitvPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNE 423
Cdd:PLN02766 340 RQGPQVDKQQFEKILSYIEHGKREGATLLTGGK----PCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430
....*....|....*....|....*....|....*....
gi 71986308 424 AIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
50-503 |
1.08e-70 |
|
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: 232.88 E-value: 1.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 50 TNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVS 129
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 130 RGLQVVEHACS-VPSLMMGETLP--NVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPG 206
Cdd:cd07099 81 LALEAIDWAARnAPRVLAPRKVPtgLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 207 AAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPdIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADA 286
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 287 NKEQTLNQLTAAAFGAAGQRCMALTTaVLVGEAR--AWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESA 364
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVER-VYVHESVydEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 365 KKEGAQVPLDGSNITVPGfengNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNG 444
Cdd:cd07099 319 VAKGAKALTGGARSNGGG----PFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 445 ATARKFTNEVDVGQIGIN-VPIPVPLPMFSFTGSRGSFLGdlNFYGKAGIQFYTQWKTVT 503
Cdd:cd07099 395 ARAEAIARRLEAGAVSINdVLLTAGIPALPFGGVKDSGGG--RRHGAEGLREFCRPKAIA 452
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
24-505 |
1.71e-70 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 233.86 E-value: 1.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 24 AAAAPTVKLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNT-----WKNTSPLTRQQCMFKL 98
Cdd:PLN02467 2 AIPVPRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 99 QALIKRDMKKLAESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRI---PLGVTAGICPF 175
Cdd:PLN02467 82 AAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKGYVlkePLGVVGLITPW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 176 NFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQ-HSAVNFICDNPDIKAISFVGGDA 254
Cdd:PLN02467 162 NYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASHPGVDKIAFTGSTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 255 AGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGE--ARAWLPELVEKAKN 332
Cdd:PLN02467 242 TGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSA-TSRLLVHEriASEFLEKLVKWAKN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 333 LKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNitVPGFENGNFVGPTILAGVKPNMTCYREEIFGPV 412
Cdd:PLN02467 321 IKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKR--PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 413 LVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIP--VPLPmfsFTGSRGSFLG-DLnfyG 489
Cdd:PLN02467 399 LCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPcfCQAP---WGGIKRSGFGrEL---G 472
|
490
....*....|....*.
gi 71986308 490 KAGIQFYTQWKTVTQY 505
Cdd:PLN02467 473 EWGLENYLSVKQVTKY 488
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
51-462 |
7.54e-70 |
|
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: 230.60 E-value: 7.54e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 51 NPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSR 130
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 131 GLQVVEHACSV-PSLMMGETLPNVSRdmdTHSY--RIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGA 207
Cdd:cd07102 82 MLERARYMISIaEEALADIRVPEKDG---FERYirREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 208 AQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADAN 287
Cdd:cd07102 159 GERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 288 KEQTLNQLTAAAFGAAGQRCMALTTaVLVGEA--RAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAK 365
Cdd:cd07102 239 LDAAAESLVDGAFFNSGQSCCSIER-IYVHESiyDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 366 KEGAQVPLDGSNITVPGfENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGA 445
Cdd:cd07102 318 AKGARALIDGALFPEDK-AGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410
....*....|....*..
gi 71986308 446 TARKFTNEVDVGQIGIN 462
Cdd:cd07102 397 RAEALGEQLETGTVFMN 413
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
13-465 |
2.77e-69 |
|
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: 230.93 E-value: 2.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 13 QQLAHFsTSKSAAAAPTVklwidgQAVESKTTDFVELTNPA-TNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTR 91
Cdd:cd07125 21 DALKAF-DEKEWEAIPII------NGEETETGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 92 QQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSRGLQVVE-HACSVPSLMMGETLPNVSRDMDTHSYRiPLGVTA 170
Cdd:cd07125 94 AEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRyYAAQARELFSDPELPGPTGELNGLELH-GRGVFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 171 GICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISF 249
Cdd:cd07125 173 CISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 250 VGGDAAGKHIYE-RGAKNGKRVQSN--MGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTAVLVGE-ARAWLPE 325
Cdd:cd07125 253 TGSTETAKLINRaLAERDGPILPLIaeTGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEiAERFIEM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 326 LVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEG---AQVPLDGsnitvpgfENGNFVGPTILAGVKPNmt 402
Cdd:cd07125 333 LKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAwliAPAPLDD--------GNGYFVAPGIIEIVGIF-- 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71986308 403 CYREEIFGPVLVVM--EAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPI 465
Cdd:cd07125 403 DLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNI 467
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
32-462 |
1.67e-66 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 222.66 E-value: 1.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 32 LWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAE 111
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 112 SITIEQGKTLPDA-EGDVSRGLQVVEHACSVPSLMmgetlpnvsrDMDTHSYRiPLGVTAGICPFNFPAMIPLWMFPVAL 190
Cdd:cd07111 104 LESLDNGKPIRESrDCDIPLVARHFYHHAGWAQLL----------DTELAGWK-PVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 191 ATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRV 270
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 271 QSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGPL 348
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCA-GSRLLVQEsvAEELIRKLKERMSHLRVGDPLDKAIDMGAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 349 ISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFengnFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEII 428
Cdd:cd07111 332 VDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGP----FYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALA 407
|
410 420 430
....*....|....*....|....*....|....
gi 71986308 429 NNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWIN 441
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
13-462 |
2.21e-66 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 222.85 E-value: 2.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 13 QQLAHFStSKSAAAAPTVKLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNT--WKNTSPLT 90
Cdd:PRK09847 4 HHLAYWQ-DKALSLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 91 RQQCMFKLQALIKRDMKKLAESITIEQGKTLPDA-EGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMdTHSYRIPLGVT 169
Cdd:PRK09847 83 RKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHEL-AMIVREPVGVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 170 AGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHG-QHSAVNFICDNPDIKAIS 248
Cdd:PRK09847 162 AAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 249 FVGGDAAGKHIY-ERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAA-FGAAGQRCMAlTTAVLVGE--ARAWLP 324
Cdd:PRK09847 242 FTGSTRTGKQLLkDAGDSNMKRVWLEAGGKSANIVFADCPDLQQAASATAAGiFYNQGQVCIA-GTRLLLEEsiADEFLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 325 ELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGaQVPLDGSNITVPGfengnFVGPTILAGVKPNMTCY 404
Cdd:PRK09847 321 LLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-----AIGPTIFVDVDPNASLS 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 71986308 405 REEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:PRK09847 395 REEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVN 452
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
31-502 |
7.62e-64 |
|
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: 215.44 E-value: 7.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 31 KLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFN--TWKNTSPLTRQQCMFKLQALIKRDMKK 108
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 109 LAESITIEQGKTLPDAE-GDVSRGLQVVEHACSVPSLMMGETLPNvsrDMDTHSYRI--PLGVTAGICPFNFPAMIPLWM 185
Cdd:cd07142 85 LAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPA---DGPHHVYTLhePIGVVGQIIPWNFPLLMFAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 186 FPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNF-ICDNPDIKAISFVGGDAAGKHIYERGA 264
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAaIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 265 K-NGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEarAWLPELVEKAKN--LKVNAG--W 339
Cdd:cd07142 242 KsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCA-GSRTFVHE--SIYDEFVEKAKAraLKRVVGdpF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 340 KPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFengnFVGPTILAGVKPNMTCYREEIFGPVLVVMEAE 419
Cdd:cd07142 319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGY----YIQPTIFSDVKDDMKIARDEIFGPVQSILKFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 420 NLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVpIPVPLPMFSFTGSRGSFLGDLNfyGKAGIQFYTQW 499
Cdd:cd07142 395 TVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREK--GIYALNNYLQV 471
|
...
gi 71986308 500 KTV 502
Cdd:cd07142 472 KAV 474
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
33-500 |
7.75e-64 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 215.54 E-value: 7.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 33 WIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAES 112
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 113 ITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFP-AMIPLWMFPvALA 191
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPaAMITRKAGP-ALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 192 TGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRV 270
Cdd:PRK11241 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 271 QSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCM-ALTTAVLVGEARAWLPELVEKAKNLKVNAGWKPDTDIGPLI 349
Cdd:PRK11241 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVcANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 350 SKQSKARVLRLIESAKKEGAQVPLDGSnitvPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIIN 429
Cdd:PRK11241 333 DEKAVAKVEEHIADALEKGARVVCGGK----AHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71986308 430 NNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIpVPLPMFSFTGSRGSFLGDLNfyGKAGIQFYTQWK 500
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLGREG--SKYGIEDYLEIK 476
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
40-462 |
5.70e-61 |
|
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: 208.59 E-value: 5.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 40 ESKTTDFVELTNP-ATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQG 118
Cdd:cd07083 27 WVDTKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 119 KTLPDAEGDVSRGLQVVEHACSVPSLMMG--ETLPNVSRDMDTHSYRiPLGVTAGICPFNFPAMIPLWMFPVALATGNTM 196
Cdd:cd07083 107 KNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 197 VIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKNG------KR 269
Cdd:cd07083 186 IAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLApgqtwfKR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 270 VQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTtaVLVGEARAWLP---ELVEKAKNLKVNAGWKPDTDIG 346
Cdd:cd07083 266 LYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAAS--RLILTQGAYEPvleRLLKRAERLSVGPPEENGTDLG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 347 PLISKQSKARVLRLIESAKKEG---AQVPLDGSnitvpgfeNGNFVGPTILAGVKPNMTCYREEIFGPVL--VVMEAENL 421
Cdd:cd07083 344 PVIDAEQEAKVLSYIEHGKNEGqlvLGGKRLEG--------EGYFVAPTVVEEVPPKARIAQEEIFGPVLsvIRYKDDDF 415
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 71986308 422 NEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:cd07083 416 AEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYIN 456
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
31-503 |
3.53e-59 |
|
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: 203.50 E-value: 3.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 31 KLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNT--WKNTSPLTRQQCMFKLQALIKRDMKK 108
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 109 LAESITIEQGKTLPDA-EGDVSRGLQVVEHACSVPSLMMGETLP-NVSRDMD--THSYRIPLGVTAGICPFNFPAMIPLW 184
Cdd:cd07140 87 LATIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGKTIPiNQARPNRnlTLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 185 MFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERG 263
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 264 AK-NGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEA--RAWLPELVEKAKNLKVNAGWK 340
Cdd:cd07140 247 AVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA-AGRLFVEESihDEFVRRVVEEVKKMKIGDPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 341 PDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFengnFVGPTILAGVKPNMTCYREEIFGPVLVVMEAEN 420
Cdd:cd07140 326 RSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFGPIMIISKFDD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 421 --LNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINV--PIPVPLPMFSFTGSrgSFLGDLnfyGKAGIQFY 496
Cdd:cd07140 402 gdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTynKTDVAAPFGGFKQS--GFGKDL---GEEALNEY 476
|
....*..
gi 71986308 497 TQWKTVT 503
Cdd:cd07140 477 LKTKTVT 483
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
51-462 |
1.35e-58 |
|
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: 201.37 E-value: 1.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 51 NPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAegdvsr 130
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDA------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 131 glqvvehacsvpslMMGETLPN---------------------VSRDMDTHSYRI---PLGVTAGICPFNFP------AM 180
Cdd:cd07098 76 --------------SLGEILVTcekirwtlkhgekalrpesrpGGLLMFYKRARVeyePLGVVGAIVSWNYPfhnllgPI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 181 IPlwmfpvALATGNTMVIKPSEQDPGAAQLLVELAKEA----GVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAG 256
Cdd:cd07098 142 IA------ALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 257 KHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTaVLVGEAR--AWLPELVEKAKNLK 334
Cdd:cd07098 216 KKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIER-VIVHEKIydKLLEILTDRVQALR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 335 VNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLV 414
Cdd:cd07098 295 QGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMV 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 71986308 415 VMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:cd07098 375 VMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIN 422
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
47-464 |
1.85e-58 |
|
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: 200.90 E-value: 1.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 47 VELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEG 126
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 127 DVSRGLQVVEHACSVPSLMMGETLPnvS-----RDMDTHSyriPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPS 201
Cdd:cd07130 94 EVQEMIDICDFAVGLSRQLYGLTIP--SerpghRMMEQWN---PLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 202 EQDPGAA----QLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAK 277
Cdd:cd07130 169 PTTPLTAiavtKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 278 NHGVIMADANKEQTLNQLTAAAFGAAGQRCmalTTA--VLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQS 353
Cdd:cd07130 249 NAIIVMEDADLDLAVRAVLFAAVGTAGQRC---TTTrrLIVHEsiYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 354 KARVLRLIESAKKEGAQVPLDGSNITVPgfenGNFVGPTILAGvKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPY 433
Cdd:cd07130 326 VDNYLAAIEEAKSQGGTVLFGGKVIDGP----GNYVEPTIVEG-LSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQ 400
|
410 420 430
....*....|....*....|....*....|...
gi 71986308 434 GNGTAIFTSNGATARKFTNEV--DVGQIGINVP 464
Cdd:cd07130 401 GLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIG 433
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
31-462 |
3.32e-58 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 200.76 E-value: 3.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 31 KLWIDGQAVESKTTDFvELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNT--WKNTSPLtRQQCMFKLQALIKRDMKK 108
Cdd:TIGR04284 2 RLLIDGKLVAGSAGTF-PTVNPATEEVLGVAADATAADMDAAIAAARRAFDEtdWSRDTAL-RVRCLRQLRDALRAHVEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 109 LAESITIEQG--KTL---PDAEGDVSRGLQVVEHACSVP-SLMMGETLPnvsrdMDTHSYRI----PLGVTAGICPFNFP 178
Cdd:TIGR04284 80 LRELTIAEVGapRMLtagAQLEGPVDDLGFAADLAESYAwTTDLGVASP-----MGIPTRRTlrreAVGVVGAITPWNFP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 179 AMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVEL-AKEAGVPDGCVNII-HGQHSAVNFICDNPDIKAISFVGGDAAG 256
Cdd:TIGR04284 155 HQINLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELiAEHTDFPPGVVNIVtSSDHRLGALLAKDPRVDMVSFTGSTATG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 257 KHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLnqlTAAAFGA---AGQRCmALTTAVLVGEARawLPELVEKAK-- 331
Cdd:TIGR04284 235 RAVMADAAATLKKVFLELGGKSAFIVLDDADLAAAC---SMAAFTVcmhAGQGC-AITTRLVVPRAR--YDEAVAAAAat 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 332 --NLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGsniTVP-GFENGNFVGPTILAGVKPNMTCYREEI 408
Cdd:TIGR04284 309 mgSIKPGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGG---GRPaDRDRGFFVEPTVIAGLDNNARVAREEI 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 71986308 409 FGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:TIGR04284 386 FGPVLTVIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVN 439
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
95-462 |
3.32e-58 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 198.81 E-value: 3.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 95 MFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICP 174
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 175 FNFPA-MIPLWMFPvALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGG 252
Cdd:PRK10090 81 WNFPFfLIARKMAP-ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 253 DAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRC-MALTTAVLVGEARAWLPELVEKAK 331
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCnCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 332 NLKV-NAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFengnFVGPTILAGVKPNMTCYREEIFG 410
Cdd:PRK10090 240 AVQFgNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGY----YYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 71986308 411 PVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
71-466 |
9.60e-58 |
|
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: 197.88 E-value: 9.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 71 AAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSRGLQVVehACSVPSLMmgETL 150
Cdd:cd07095 4 AAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKI--DISIKAYH--ERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 151 PNVSRDMDTHSYRI---PLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNI 227
Cdd:cd07095 80 GERATPMAQGRAVLrhrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 228 IHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKN-GKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQR 306
Cdd:cd07095 160 VQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRpGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 307 CMAlTTAVLV---GEARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITvpgf 383
Cdd:cd07095 240 CTC-ARRLIVpdgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV---- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 384 ENGNFVGPTIL----AGVKPNmtcyrEEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQI 459
Cdd:cd07095 315 AGTAFLSPGIIdvtdAADVPD-----EEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIV 389
|
....*..
gi 71986308 460 GINVPIP 466
Cdd:cd07095 390 NWNRPTT 396
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
52-504 |
1.03e-56 |
|
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: 195.99 E-value: 1.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 52 PATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSRG 131
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 132 LQVVEH-ACSVPSLMMGE----TLPNVSRdmdTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPG 206
Cdd:cd07101 83 AIVARYyARRAERLLKPRrrrgAIPVLTR---TTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 207 AAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIkaISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMAD 285
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGPGSEVgGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 286 ANKEQTLNQLTAAAFGAAGQRCMALTTaVLVGEARA--WLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIES 363
Cdd:cd07101 238 ADLDKAAAGAVRACFSNAGQLCVSIER-IYVHESVYdeFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 364 AKKEGAQVPLDGSniTVPGFenGN-FVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTS 442
Cdd:cd07101 317 AVAKGATVLAGGR--ARPDL--GPyFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71986308 443 NGATARKFTNEVDVGQIGINVPI-----PVPLPMfsfTGSRGSFLGDLNfyGKAGIQFYTQWKTVTQ 504
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNEGYaaawaSIDAPM---GGMKDSGLGRRH--GAEGLLKYTETQTVAV 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
18-502 |
1.60e-55 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 194.64 E-value: 1.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 18 FSTSKSAAAAPTV--------KLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNT--WKNTS 87
Cdd:PLN02466 38 FSTAAAAVEEPITppvqvsytQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 88 PLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEG-DVSRGLQVVEHACSVPSLMMGETLPNvsrDMDTHSYRI-- 164
Cdd:PLN02466 118 AYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPA---DGPHHVQTLhe 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 165 PLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHG-QHSAVNFICDNPD 243
Cdd:PLN02466 195 PIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 244 IKAISFVGGDAAGKHIYERGAK-NGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEaRAW 322
Cdd:PLN02466 275 VDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCA-GSRTFVHE-RVY 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 323 lPELVEKAK--NLKVNAG--WKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFengnFVGPTILAGVK 398
Cdd:PLN02466 353 -DEFVEKAKarALKRVVGdpFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQ 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 399 PNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN------VPIPvplpmf 472
Cdd:PLN02466 428 DDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfdAAIP------ 501
|
490 500 510
....*....|....*....|....*....|
gi 71986308 473 sFTGSRGSFLGDLNfyGKAGIQFYTQWKTV 502
Cdd:PLN02466 502 -FGGYKMSGIGREK--GIYSLNNYLQVKAV 528
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
47-462 |
3.41e-54 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 190.86 E-value: 3.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 47 VELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEG 126
Cdd:PRK09407 34 REVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 127 DVsrgLQVV----EHACSVPSLM----MGETLPNVSRdmdTHSYRIPLGVTAGICPFNFPA------MIPlwmfpvALAT 192
Cdd:PRK09407 114 EV---LDVAltarYYARRAPKLLaprrRAGALPVLTK---TTELRQPKGVVGVISPWNYPLtlavsdAIP------ALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 193 GNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIkaISFVGGDAAGKHIYERGAKNGKRVQ 271
Cdd:PRK09407 182 GNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVgTALVDNADY--LMFTGSTATGRVLAEQAGRRLIGFS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 272 SNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGEARA--WLPELVEKAKNLKVNAGWKPDTDIGPLI 349
Cdd:PRK09407 260 LELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCIS-IERIYVHESIYdeFVRAFVAAVRAMRLGAGYDYSADMGSLI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 350 SKQSKARVLRLIESAKKEGAQV-----------PLdgsnitvpgfengnFVGPTILAGVKPNMTCYREEIFGPVLVVMEA 418
Cdd:PRK09407 339 SEAQLETVSAHVDDAVAKGATVlaggkarpdlgPL--------------FYEPTVLTGVTPDMELAREETFGPVVSVYPV 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 71986308 419 ENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:PRK09407 405 ADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVN 448
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
51-462 |
4.23e-54 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 189.30 E-value: 4.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 51 NPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSR 130
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 131 GLQV----VEHAcsvPSLMMGE-TLpnVSRDMDTHSYRiPLGVTAGICPFNFPamipLWMF-----PVALAtGNTMVIKP 200
Cdd:PRK13968 93 SANLcdwyAEHG---PAMLKAEpTL--VENQQAVIEYR-PLGTILAIMPWNFP----LWQVmrgavPILLA-GNGYLLKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 201 SEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIyerGAKNG---KRVQSNMGAK 277
Cdd:PRK13968 162 APNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAI---GAQAGaalKKCVLELGGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 278 NHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTAVL-VGEARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKAR 356
Cdd:PRK13968 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIeEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 357 VLRLIESAKKEGAQVPLDGSNITvpgfENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNG 436
Cdd:PRK13968 319 LHHQVEATLAEGARLLLGGEKIA----GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLS 394
|
410 420
....*....|....*....|....*.
gi 71986308 437 TAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:PRK13968 395 ATIFTTDETQARQMAARLECGGVFIN 420
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
50-502 |
1.74e-53 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 187.25 E-value: 1.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 50 TNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVS 129
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 130 ---RGLQ-VVEHAcsvPSLMMGET--LPNVSRDMDTHSYRiPLGVTAGICPFNFPamipLWM---FPV-ALATGNTMVIK 199
Cdd:PRK09406 86 kcaKGFRyYAEHA---EALLADEPadAAAVGASRAYVRYQ-PLGVVLAVMPWNFP----LWQvvrFAApALMAGNVGLLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 200 PSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNH 279
Cdd:PRK09406 158 HASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 280 GVIMADANKEQTLNQLTAAAFGAAGQRCMALTTAVLVGE-ARAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVL 358
Cdd:PRK09406 238 FIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADvYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 359 RLIESAKKEGAQVPLDGSNITVPGFengnFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTA 438
Cdd:PRK09406 318 KQVDDAVAAGATILCGGKRPDGPGW----FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSN 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71986308 439 IFTSNGATARKFTNEVDVGQIGINvPIPVPLPMFSFTGSRGSflGdlnfYGK----AGIQFYTQWKTV 502
Cdd:PRK09406 394 AWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPELPFGGVKRS--G----YGRelsaHGIREFCNIKTV 454
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
33-462 |
2.27e-52 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 184.96 E-value: 2.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 33 WIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAES 112
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 113 ITIEQGKTLPDAEG-DVSrglQVVEHACSVPSLMMGETLPNVSRDMDTHSYRI--PLGVTAGICPFNFPAMIPLWMFPVA 189
Cdd:cd07116 84 ETWDNGKPVRETLAaDIP---LAIDHFRYFAGCIRAQEGSISEIDENTVAYHFhePLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 190 LATGNTMVIKPSEQDPGAAQLLVELAKEAgVPDGCVNIIHG-QHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGK 268
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 269 RVQSNMGAKNHGVIMADANKEQ------TLNQLTAAAFGaAGQRCMALTTAvLVGEA--RAWLPELVEKAKNLKVNAGWK 340
Cdd:cd07116 240 PVTLELGGKSPNIFFADVMDADdaffdkALEGFVMFALN-QGEVCTCPSRA-LIQESiyDRFMERALERVKAIKQGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 341 PDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFENGNFVGPTILAGVKpNMTCYREEIFGPVLVVMEAEN 420
Cdd:cd07116 318 TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTTFKD 396
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 71986308 421 LNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN 438
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
31-483 |
1.89e-51 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 182.65 E-value: 1.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 31 KLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLA 110
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 111 ESITIEQGKTLPDAEGDVSRGLQVVEHAC-------SVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPL 183
Cdd:PLN00412 97 ECLVKEIAKPAKDAVTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 184 WMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDaAGKHIyer 262
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIgDFLTMHPGVNCISFTGGD-TGIAI--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 263 gAKNGKRV--QSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALtTAVLVGEARAwlPELVEK--AKNLKVNAG 338
Cdd:PLN00412 253 -SKKAGMVplQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAV-KVVLVMESVA--DALVEKvnAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 339 wKP--DTDIGPLISKQSKARVLRLIESAKKEGAQvpldgsnITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVM 416
Cdd:PLN00412 329 -PPedDCDITPVVSESSANFIEGLVMDAKEKGAT-------FCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVI 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71986308 417 EAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPiPVPLP-MFSFTGSRGSFLG 483
Cdd:PLN00412 401 RINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA-PARGPdHFPFQGLKDSGIG 467
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
13-462 |
9.63e-47 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 175.00 E-value: 9.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 13 QQLAHFsTSKSAAAAPTvklwIDGqaveskTTDFVELTNPA-TNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTR 91
Cdd:PRK11904 541 AAIAAF-LEKQWQAGPI----ING------EGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEER 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 92 QQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVsRglqvvE-------HACSVPSLM-MGETLP------Nvsrdm 157
Cdd:PRK11904 610 AAILERAADLLEANRAELIALCVREAGKTLQDAIAEV-R-----EavdfcryYAAQARRLFgAPEKLPgptgesN----- 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 158 dtHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-N 236
Cdd:PRK11904 679 --ELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgA 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 237 FICDNPDIKAISFVGGDAAGKHIyERG--AKNGKRV--------QSNMgaknhgviMAD--ANKEQTLNQLTAAAFGAAG 304
Cdd:PRK11904 757 ALTADPRIAGVAFTGSTETARII-NRTlaARDGPIVpliaetggQNAM--------IVDstALPEQVVDDVVTSAFRSAG 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 305 QRCMAL------------TTAVLVGEARAwlpelvekaknLKV-NAGWkPDTDIGPLISKQSKARVLRLIESAKKEG--- 368
Cdd:PRK11904 828 QRCSALrvlfvqediadrVIEMLKGAMAE-----------LKVgDPRL-LSTDVGPVIDAEAKANLDAHIERMKREArll 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 369 AQVPLDGsnitvpGFENGNFVGPTILAgvKPNMTCYREEIFGPVLVVM--EAENLNEAIEIINNNPYGNGTAIFTSNGAT 446
Cdd:PRK11904 896 AQLPLPA------GTENGHFVAPTAFE--IDSISQLEREVFGPILHVIryKASDLDKVIDAINATGYGLTLGIHSRIEET 967
|
490
....*....|....*.
gi 71986308 447 ARKFTNEVDVGQIGIN 462
Cdd:PRK11904 968 ADRIADRVRVGNVYVN 983
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
2-462 |
2.50e-45 |
|
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: 166.24 E-value: 2.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 2 LSRLARVQPKCQQLaHFSTSKSAAAAPTvklwIDGQAVESKTTDFVelTNPAT-NEVIAMVPNATQAEMQAAVDSAKNAF 80
Cdd:TIGR01238 15 LDNESELKPLEAQI-HAWADKTWQAAPI----IGHSYKADGEAQPV--TNPADrRDIVGQVFHANLAHVQAAIDSAQQAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 81 NTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSRGLQVvehaCSVPSLMMGETLPNvsrdmDTH 160
Cdd:TIGR01238 88 PTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDF----CRYYAKQVRDVLGE-----FSV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 161 SyriPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVN-FIC 239
Cdd:TIGR01238 159 E---SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGaALT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 240 DNPDIKAISFVGGDAAG----KHIYERGAKNGKRVqSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTAVL 315
Cdd:TIGR01238 236 SDPRIAGVAFTGSTEVAqlinQTLAQREDAPVPLI-AETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 316 VGEARAWLPELVEKA-KNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEG---AQVPLDGSNitvpGFENGNFVGP 391
Cdd:TIGR01238 315 QEDVADRVLTMIQGAmQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSR----ACQHGTFVAP 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71986308 392 TILAgvKPNMTCYREEIFGPVL--VVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:TIGR01238 391 TLFE--LDDIAELSEEVFGPVLhvVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN 461
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
38-462 |
1.61e-43 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 165.81 E-value: 1.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 38 AVESKTTDFVELTNPA-TNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIE 116
Cdd:PRK11905 560 AGGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVRE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 117 QGKTLPDAEGDVsR---------GLQVvehacsvpslmmgetlpnvsRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFP 187
Cdd:PRK11905 640 AGKTLANAIAEV-ReavdflryyAAQA--------------------RRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIA 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 188 VALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGGDAAGKHIYERGAKN 266
Cdd:PRK11905 699 AALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLIQRTLAKR 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 267 GKR---VQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAL------------TTAVLVGEARAwlpelvekak 331
Cdd:PRK11905 779 SGPpvpLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALrvlclqedvadrVLTMLKGAMDE---------- 848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 332 nLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEG---AQVPLDgsnitvPGFENGNFVGPTILAgvKPNMTCYREEI 408
Cdd:PRK11905 849 -LRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGrlvHQLPLP------AETEKGTFVAPTLIE--IDSISDLEREV 919
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 71986308 409 FGPVLVVM--EAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:PRK11905 920 FGPVLHVVrfKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN 975
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
32-434 |
1.90e-43 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 160.89 E-value: 1.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 32 LWIDGQAVESKTTDFVElTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAE 111
Cdd:PRK09457 3 LWINGDWIAGQGEAFES-RNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 112 SITIEQGKTLPDAEGDVSRGLQVVehACSVPSLmmGETLPNVSRDM-DTHS---YRiPLGVTAGICPFNFPAMIPLWMFP 187
Cdd:PRK09457 82 VIARETGKPLWEAATEVTAMINKI--AISIQAY--HERTGEKRSEMaDGAAvlrHR-PHGVVAVFGPYNFPGHLPNGHIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 188 VALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKN- 266
Cdd:PRK09457 157 PALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQp 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 267 GKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCmalTTA--VLV---GEARAWLPELVEKAKNLKVNAgwkP 341
Cdd:PRK09457 237 EKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRC---TCArrLLVpqgAQGDAFLARLVAVAKRLTVGR---W 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 342 DTD----IGPLISKQSKARVL----RLIESakkeGAQVPLDGSNITvpgfENGNFVGPTILagvkpNMTCYR----EEIF 409
Cdd:PRK09457 311 DAEpqpfMGAVISEQAAQGLVaaqaQLLAL----GGKSLLEMTQLQ----AGTGLLTPGII-----DVTGVAelpdEEYF 377
|
410 420
....*....|....*....|....*
gi 71986308 410 GPVLVVMEAENLNEAIEIINNNPYG 434
Cdd:PRK09457 378 GPLLQVVRYDDFDEAIRLANNTRFG 402
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
3-462 |
2.38e-43 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 165.11 E-value: 2.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 3 SRLARVQpkcQQLAHFStSKSAAAAPTvklwIDGQAVESKTTdfvELTNPA-TNEVIAMVPNATQAEMQAAVDSAKNAFN 81
Cdd:COG4230 539 AVLAALS---AALAAAA-EKQWQAAPL----IAGEAASGEAR---PVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFP 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 82 TWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVsR---------GLQVvehacsvpslmmgetlpn 152
Cdd:COG4230 608 AWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEV-ReavdfcryyAAQA------------------ 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 153 vSRDMDTHSYRIPLGVTAGICPFNFPAMIplwmF----PVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNII 228
Cdd:COG4230 669 -RRLFAAPTVLRGRGVFVCISPWNFPLAI----FtgqvAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLL 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 229 HGQHSAV-NFICDNPDIKAISFVGGDAAGKHIyERG--AKNGKRV--------QSNMgaknhgviMAD--ANKEQTLNQL 295
Cdd:COG4230 744 PGDGETVgAALVADPRIAGVAFTGSTETARLI-NRTlaARDGPIVpliaetggQNAM--------IVDssALPEQVVDDV 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 296 TAAAFGAAGQRCMAL------------TTAVLVGEARAwlpelvekaknLKVNAGWKPDTDIGPLISKQSKARVLRLIES 363
Cdd:COG4230 815 LASAFDSAGQRCSALrvlcvqediadrVLEMLKGAMAE-----------LRVGDPADLSTDVGPVIDAEARANLEAHIER 883
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 364 AKKEG---AQVPLDgsnitvPGFENGNFVGPTI--LAGVKPnmtcYREEIFGPVLVVM--EAENLNEAIEIINNNPYGNG 436
Cdd:COG4230 884 MRAEGrlvHQLPLP------EECANGTFVAPTLieIDSISD----LEREVFGPVLHVVryKADELDKVIDAINATGYGLT 953
|
490 500
....*....|....*....|....*.
gi 71986308 437 TAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:COG4230 954 LGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
47-483 |
2.28e-41 |
|
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: 154.50 E-value: 2.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 47 VELTNPATNEVIAMVPNATQAEMQAAVDSAKNAF---NTWknTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPD 123
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFldrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 124 AEGDVSRGLQVVEHACSVPSLMMGETLPnvsrdMD---------THSYRIPLGVTAGICPFNFPA-MIPLWMFPvALATG 193
Cdd:cd07148 79 AKVEVTRAIDGVELAADELGQLGGREIP-----MGltpasagriAFTTREPIGVVVAISAFNHPLnLIVHQVAP-AIAAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 194 NTMVIKPSEQDPGAAQLLVELAKEAGVPDG-CVNIIHGQHSAVNFICDnPDIKAISFVGGDAAGKHIYERGAKnGKRVqs 272
Cdd:cd07148 153 CPVIVKPALATPLSCLAFVDLLHEAGLPEGwCQAVPCENAVAEKLVTD-PRVAFFSFIGSARVGWMLRSKLAP-GTRC-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 273 nmgAKNHG-----VIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLVGE--ARAWLPELVEKAKNLKVNAGWKPDTDI 345
Cdd:cd07148 229 ---ALEHGgaapvIVDRSADLDAMIPPLVKGGFYHAGQVCVS-VQRVFVPAeiADDFAQRLAAAAEKLVVGDPTDPDTEV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 346 GPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGFEngnfvgPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAI 425
Cdd:cd07148 305 GPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTYA------PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAI 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 71986308 426 EIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPIPVPLPMFSFTGSRGSFLG 483
Cdd:cd07148 379 AQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
47-464 |
5.21e-41 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 154.61 E-value: 5.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 47 VELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEG 126
Cdd:PLN02315 36 VSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 127 DVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDP- 205
Cdd:PLN02315 116 EVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPl 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 206 ---GAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYER-GAKNGKRVQSnMGAKNHGV 281
Cdd:PLN02315 196 itiAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTvNARFGKCLLE-LSGNNAII 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 282 IMADANKEQTLNQLTAAAFGAAGQRCmalTTA--VLVGEA--RAWLPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARV 357
Cdd:PLN02315 275 VMDDADIQLAVRSVLFAAVGTAGQRC---TTCrrLLLHESiyDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 358 LRLIESAKKEGAQVPLDGSNITvpgfENGNFVGPTILAgVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGT 437
Cdd:PLN02315 352 EKGIEIIKSQGGKILTGGSAIE----SEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSS 426
|
410 420
....*....|....*....|....*....
gi 71986308 438 AIFTSNGATARKFTNEV--DVGQIGINVP 464
Cdd:PLN02315 427 SIFTRNPETIFKWIGPLgsDCGIVNVNIP 455
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
19-462 |
5.06e-40 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 155.52 E-value: 5.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 19 STSKSAAAAPTvklwIDGQAVESKTTDFVeltNPA-TNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFK 97
Cdd:PRK11809 640 SAHQKWQAAPM----LEDPVAAGEMSPVI---NPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILER 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 98 LQALIKRDMKKLAESITIEQGKTLPDAEGDVSRGLQVVEHACSvpslmmgetlpNVSRDMDTHSYRiPLGVTAGICPFNF 177
Cdd:PRK11809 713 AADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAG-----------QVRDDFDNDTHR-PLGPVVCISPWNF 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 178 PAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIKAISFVGG---- 252
Cdd:PRK11809 781 PLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVgAALVADARVRGVMFTGSteva 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 253 -----------DAAGKH---IYERGAKNGKRVQSNmgaknhgvimadANKEQTLNQLTAAAFGAAGQRCMAL-------- 310
Cdd:PRK11809 861 rllqrnlagrlDPQGRPiplIAETGGQNAMIVDSS------------ALTEQVVADVLASAFDSAGQRCSALrvlclqdd 928
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 311 ----TTAVLVGEARAWlpelvekaknlkvNAGwKPD---TDIGPLISKQSKARVLRLIESAKKEG---AQVPLDGSNitv 380
Cdd:PRK11809 929 vadrTLKMLRGAMAEC-------------RMG-NPDrlsTDIGPVIDAEAKANIERHIQAMRAKGrpvFQAARENSE--- 991
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 381 pGFENGNFVGPTILAgvKPNMTCYREEIFGPVLVVM--EAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQ 458
Cdd:PRK11809 992 -DWQSGTFVPPTLIE--LDSFDELKREVFGPVLHVVryNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGN 1068
|
....
gi 71986308 459 IGIN 462
Cdd:PRK11809 1069 LYVN 1072
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
70-497 |
9.30e-39 |
|
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: 146.52 E-value: 9.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 70 QAAVDSAKNAFNTWKnTSPL-TRQQCMFKLQALIKRDMKKLAESITIEQGKtlPDAE---GDVSRGLQVVEHACS-VPSL 144
Cdd:cd07087 1 AELVARLRETFLTGK-TRSLeWRKAQLKALKRMLTENEEEIAAALYADLGK--PPAEaylTEIAVVLGEIDHALKhLKKW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 145 MMGETLPNVSRDMDTHSYRI--PLGVTAGICPFNFP---AMIPLwmfpV-ALATGNTMVIKPSEQDPGAAQLLVELAKEA 218
Cdd:cd07087 78 MKPRRVSVPLLLQPAKAYVIpePLGVVLIIGPWNYPlqlALAPL----IgAIAAGNTVVLKPSELAPATSALLAKLIPKY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 219 gVPDGCVNIIHGQHSAVNFICDNP-DIkaISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTA 297
Cdd:cd07087 154 -FDPEAVAVVEGGVEVATALLAEPfDH--IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 298 AAFGAAGQRCMALTTaVLVGEARawLPELVEKAKNlKVNAGWKPDT----DIGPLISKQSKARVLRLiesakkegaqvpL 373
Cdd:cd07087 231 GKFLNAGQTCIAPDY-VLVHESI--KDELIEELKK-AIKEFYGEDPkespDYGRIINERHFDRLASL------------L 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 374 DGSNITVPGF--ENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNP-----YgngtaIFTSNGAT 446
Cdd:cd07087 295 DDGKVVIGGQvdKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPkplalY-----LFSEDKAV 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 71986308 447 ARKFTNEVDVGQIGIN-VPIPVPLPMFSFTGSRGSFLGdlNFYGKAGiqFYT 497
Cdd:cd07087 370 QERVLAETSSGGVCVNdVLLHAAIPNLPFGGVGNSGMG--AYHGKAG--FDT 417
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
67-502 |
3.19e-36 |
|
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: 139.66 E-value: 3.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 67 AEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKL-----------QALIKRDMKKLA-ESITIEQGKTLPDaegdvsrglqV 134
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLywavkdneeaiVEALKKDLGRPPfETLLTEVSGVKND----------I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 135 VEHACSVPSLMMGETLPNVSRDMDTHSYRI---PLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLL 211
Cdd:cd07135 75 LHMLKNLKKWAKDEKVKDGPLAFMFGKPRIrkePLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 212 VELAKEAgVPDGCVNIIHGQHSAVNFICDNPDIKaISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQT 291
Cdd:cd07135 155 AELVPKY-LDPDAFQVVQGGVPETTALLEQKFDK-IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 292 LNQLTAAAFGAAGQRCMAlTTAVLVgeARAWLPELVEKAK---NLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEg 368
Cdd:cd07135 233 AKRILWGKFGNAGQICVA-PDYVLV--DPSVYDEFVEELKkvlDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTKGK- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 369 aqvpldgsnITVPGFENG--NFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGAT 446
Cdd:cd07135 309 ---------VVIGGEMDEatRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSE 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 71986308 447 ARKFTNEVDVGQIGIN-VPIPVPLPMFSFTGSRGSFLGdlNFYGKAGIQFYTQWKTV 502
Cdd:cd07135 380 IDHILTRTRSGGVVINdTLIHVGVDNAPFGGVGDSGYG--AYHGKYGFDTFTHERTV 434
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
34-453 |
3.22e-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: 3.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 34 IDGQAVESKTTDFVEltNPAT-NEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALI--KRDMKKLA 110
Cdd:cd07123 37 IGGKEVRTGNTGKQV--MPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLsgKYRYELNA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 111 eSITIEQGKTLPDAEGDVSRGL-----------------QVVEHAcsvpslmmgetlPNVSRDMDthsYRiPL-GVTAGI 172
Cdd:cd07123 115 -ATMLGQGKNVWQAEIDAACELidflrfnvkyaeelyaqQPLSSP------------AGVWNRLE---YR-PLeGFVYAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 173 CPFNFPAM------IPLWMfpvalatGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAV-NFICDNPDIK 245
Cdd:cd07123 178 SPFNFTAIggnlagAPALM-------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVgDTVLASPHLA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 246 AISFVGGDAAGKHIYERGA------KNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTtavlvgea 319
Cdd:cd07123 251 GLHFTGSTPTFKSLWKQIGenldryRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAAS-------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 320 RAWLPE---------LVEKAKNLKVNAgwkPDTD---IGPLISKQSKARVLRLIESAKKE-GAQVPLDGSNITVPGFeng 386
Cdd:cd07123 323 RAYVPEslwpevkerLLEELKEIKMGD---PDDFsnfMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGY--- 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 387 nFVGPTILAGVKPNMTCYREEIFGPVLV--VMEAENLNEAIEIINN-NPYGNGTAIFtsngATARKFTNE 453
Cdd:cd07123 397 -FVEPTVIETTDPKHKLMTEEIFGPVLTvyVYPDSDFEETLELVDTtSPYALTGAIF----AQDRKAIRE 461
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
77-462 |
1.91e-34 |
|
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: 134.66 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 77 KNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKtlPDAEGDVSRGLQVVE---HACS-VPSLMMGETLPN 152
Cdd:cd07134 8 QAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRK--PAAEVDLTEILPVLSeinHAIKhLKKWMKPKRVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 153 VSRDMDTHSYRI--PLGVTAGICPFNFP---AMIPLwmfPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGcVNI 227
Cdd:cd07134 86 PLLLFGTKSKIRyePKGVCLIISPWNYPfnlAFGPL---VSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDE-VAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 228 IHGQHSAVNFICDNPdIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRC 307
Cdd:cd07134 162 FEGDAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 308 MALTTaVLVGE--ARAWLPELVEK-AKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVpLDGSNITvpgfE 384
Cdd:cd07134 241 IAPDY-VFVHEsvKDAFVEHLKAEiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKV-EFGGQFD----A 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71986308 385 NGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:cd07134 315 AQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN 392
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
165-520 |
2.82e-34 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 135.16 E-value: 2.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 165 PLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAgVPDGCVNIIHGQHSAVNFICDNP-D 243
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTELLKEPfD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 244 IkaISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTaVLVgeARAWL 323
Cdd:PTZ00381 188 H--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDY-VLV--HRSIK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 324 PELVEKAKN-LKVNAGWKPDT--DIGPLISKQSKARVLRLIESakkegaqvplDGSNITVPGF--ENGNFVGPTILAGVK 398
Cdd:PTZ00381 263 DKFIEALKEaIKEFFGEDPKKseDYSRIVNEFHTKRLAELIKD----------HGGKVVYGGEvdIENKYVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 399 PNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGINVPI----PVPLPmfsF 474
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVfhllNPNLP---F 409
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 71986308 475 TGSRGSFLGdlNFYGKAGIQFYTQWKTVTQywNESLTELKPQMSFP 520
Cdd:PTZ00381 410 GGVGNSGMG--AYHGKYGFDTFSHPKPVLN--KSTGNSFDLSLRYP 451
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
165-462 |
1.13e-30 |
|
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: 123.75 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 165 PLGVTAGICPFNFP---AMIPLwmfPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDgcvniihgqHSAVnfICDN 241
Cdd:cd07133 101 PLGVVGIIVPWNYPlylALGPL---IAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED---------EVAV--VTGG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 242 PDI-KAIS--------FVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTT 312
Cdd:cd07133 167 ADVaAAFSslpfdhllFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVA-PD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 313 AVLVGEARawLPELVEKAKnlKVNAGWKPDT----DIGPLISKQSKARVLRLIESAKKEGAQV-PLDGSNitvPGFENGN 387
Cdd:cd07133 246 YVLVPEDK--LEEFVAAAK--AAVAKMYPTLadnpDYTSIINERHYARLQGLLEDARAKGARViELNPAG---EDFAATR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 388 FVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNP-----YgngtaIFTSNGATARKFTNEVDVGQIGIN 462
Cdd:cd07133 319 KLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPrplalY-----YFGEDKAEQDRVLRRTHSGGVTIN 393
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
162-462 |
8.33e-29 |
|
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: 118.76 E-value: 8.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 162 YRIPLGVTAGICPFNFP---AMIPLwmfpV-ALATGNTMVIKPSEQDPGAAQLLVELAKEAgVPDGCVNIIHGQHSAVNF 237
Cdd:cd07136 97 YYEPYGVVLIIAPWNYPfqlALAPL----IgAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 238 ICDNP-DikAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEqtlnqlTAA---AFGA---AGQRCMAl 310
Cdd:cd07136 172 LLDQKfD--YIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLK------LAAkriVWGKflnAGQTCVA- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 311 TTAVLVGEAR--AWLPELVEKAKNLKvnaGWKP--DTDIGPLISKQSKARVLRLIESAKkegaqvpldgsnITVPGF--E 384
Cdd:cd07136 243 PDYVLVHESVkeKFIKELKEEIKKFY---GEDPleSPDYGRIINEKHFDRLAGLLDNGK------------IVFGGNtdR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 385 NGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNP-----YgngtaIFTSNGATARKFTNEVDVGQI 459
Cdd:cd07136 308 ETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPkplalY-----LFSEDKKVEKKVLENLSFGGG 382
|
...
gi 71986308 460 GIN 462
Cdd:cd07136 383 CIN 385
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
70-424 |
8.57e-28 |
|
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: 115.80 E-value: 8.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 70 QAAVDSAKNAFNTWKNtspLTRQQCMFKLQALIKRDMKK---LAESITIEQGKT---LPDAEGDVS--RGLQVVEHACSV 141
Cdd:cd07084 2 ERALLAADISTKAARR---LALPKRADFLARIIQRLAAKsydIAAGAVLVTGKGwmfAENICGDQVqlRARAFVIYSYRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 142 PSLMMGEtlPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAG-V 220
Cdd:cd07084 79 PHEPGNH--LGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 221 PDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERgAKNGkRVQSNMGAKNHGVIMADAN-KEQTLNQLTAAA 299
Cdd:cd07084 157 PPEDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALD-AKQA-RIYLELAGFNWKVLGPDAQaVDYVAWQCVQDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 300 FGAAGQRCMAlTTAVLVGEARAWLPeLVEKAKNLKVNAGWKpDTDIGPLISKQSKARvlrlIESAKKEGAQVPLDGS--- 376
Cdd:cd07084 235 TACSGQKCTA-QSMLFVPENWSKTP-LVEKLKALLARRKLE-DLLLGPVQTFTTLAM----IAHMENLLGSVLLFSGkel 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 71986308 377 -NITVPGFEnGNFVGPTILAGVKPNMTCYR---EEIFGPVLVVMEAENLNEA 424
Cdd:cd07084 308 kNHSIPSIY-GACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYKKDQLA 358
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
165-502 |
2.53e-23 |
|
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: 102.49 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 165 PLGVTAGICPFNFPamIPLWMFPV--ALATGNTMVIKPSEQDPGAAQLLVELAKEAgVPDGCVNIIHGQHSAVNFICDNP 242
Cdd:cd07137 101 PLGVVLVISAWNFP--FLLSLEPVigAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVPETTALLEQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 243 DIKaISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGA-AGQRCMALTTaVLVGEARA 321
Cdd:cd07137 178 WDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDY-VLVEESFA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 322 wlPELVEKAKN-LKVNAGWKP-DTDIGPLISKQSKARVLRLIESAKKEGAQVpLDGSNITvpgfENGNFVGPTILAGVKP 399
Cdd:cd07137 256 --PTLIDALKNtLEKFFGENPkESKDLSRIVNSHHFQRLSRLLDDPSVADKI-VHGGERD----EKNLYIEPTILLDPPL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 400 NMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN-VPIPVPLPMFSFTGSR 478
Cdd:cd07137 329 DSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdTVVQYAIDTLPFGGVG 408
|
330 340
....*....|....*....|....
gi 71986308 479 GSFLGdlNFYGKAGIQFYTQWKTV 502
Cdd:cd07137 409 ESGFG--AYHGKFSFDAFSHKKAV 430
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
70-462 |
3.95e-23 |
|
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: 101.91 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 70 QAAVDSAKNAFNTWKnTSPLT-RQQCMFKLQALIKRDMKKLAESITIEQGKtlPDAEGDVSRGLQVVEHAC----SVPSL 144
Cdd:cd07132 1 AEAVRRAREAFSSGK-TRPLEfRIQQLEALLRMLEENEDEIVEALAKDLRK--PKFEAVLSEILLVKNEIKyaisNLPEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 145 MMGETLP-NVSRDMDT-HSYRIPLGVTAGICPFNFPamIPLWMFPV--ALATGNTMVIKPSEQDPGAAQLLVELAKEAGV 220
Cdd:cd07132 78 MKPEPVKkNLATLLDDvYIYKEPLGVVLIIGAWNYP--LQLTLVPLvgAIAAGNCVVIKPSEVSPATAKLLAELIPKYLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 221 PDgCVNIIHGQHSAVNFICDNpDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAF 300
Cdd:cd07132 156 KE-CYPVVLGGVEETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 301 GAAGQRCMA----LTTAvlvgEARawlPELVEKAKN-LKVNAGWKP--DTDIGPLISKQSKARVLRLIEsakkegaqvpl 373
Cdd:cd07132 234 INAGQTCIApdyvLCTP----EVQ---EKFVEALKKtLKEFYGEDPkeSPDYGRIINDRHFQRLKKLLS----------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 374 dGSNITVPGF--ENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIIN--NNP---YgngtaIFTSNGAT 446
Cdd:cd07132 296 -GGKVAIGGQtdEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINsrEKPlalY-----VFSNNKKV 369
|
410
....*....|....*.
gi 71986308 447 ARKFTNEVDVGQIGIN 462
Cdd:cd07132 370 INKILSNTSSGGVCVN 385
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
33-450 |
1.72e-17 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 85.40 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 33 WIDGQavesktTDFVELTNPATNEVIAMVPNATqAEMQAAVDSAKNAFNtwKNTSPLTRQQCMFKLQALIKRDMKKLAE- 111
Cdd:cd07128 9 WHAGT------GDGRTLHDAVTGEVVARVSSEG-LDFAAAVAYAREKGG--PALRALTFHERAAMLKALAKYLMERKEDl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 112 -SITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMM--------GETLPnVSRD---MDTHSYrIPL-GVTAGICPFNFP 178
Cdd:cd07128 80 yALSAATGATRRDSWIDIDGGIGTLFAYASLGRRELpnahflveGDVEP-LSKDgtfVGQHIL-TPRrGVAVHINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 179 AMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGV-PDGCVNIIHGQhsaVNFICDNPDIK-AISFVGGDAAG 256
Cdd:cd07128 158 VWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHLGEQdVVAFTGSAATA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 257 KHIYERGAKNGKRVQSNMGAK--NHGVIMADAN----------KEqTLNQLTAAAfgaaGQRCMAlTTAVLVGEAR--AW 322
Cdd:cd07128 235 AKLRAHPNIVARSIRFNAEADslNAAILGPDATpgtpefdlfvKE-VAREMTVKA----GQKCTA-IRRAFVPEARvdAV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 323 LPELVEKAKNLKVNAGWKPDTDIGPLISKQSKARVLRLIESAKKEGAQVPLDGSNITVPGF--ENGNFVGPTILAGVKP- 399
Cdd:cd07128 309 IEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVGAdaEKGAFFPPTLLLCDDPd 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 71986308 400 NMTCYRE-EIFGPVLVVMEAENLNEAIEIINNnpyGNG---TAIFTSNGATARKF 450
Cdd:cd07128 389 AATAVHDvEAFGPVATLMPYDSLAEAIELAAR---GRGslvASVVTNDPAFAREL 440
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
165-502 |
4.99e-17 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 83.56 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 165 PLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDgCVNIIHGQHSAVNFICDNPDI 244
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVVEGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 245 KaISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAA-GQRCMA----LTTavlvgea 319
Cdd:PLN02174 191 K-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCNnGQACISpdyiLTT------- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 320 RAWLPELVEKAK-NLKVNAGWKP--DTDIGPLISKQSKARVLRLIEsaKKEGAQVPLDGSNITVPGFEngnfVGPTILAG 396
Cdd:PLN02174 263 KEYAPKVIDAMKkELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLD--EKEVSDKIVYGGEKDRENLK----IAPTILLD 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 397 VKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN-VPIPVPLPMFSFT 475
Cdd:PLN02174 337 VPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFG 416
|
330 340
....*....|....*....|....*..
gi 71986308 476 GSRGSFLGdlNFYGKAGIQFYTQWKTV 502
Cdd:PLN02174 417 GVGESGMG--AYHGKFSFDAFSHKKAV 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
165-520 |
1.27e-15 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 79.39 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 165 PLGVTAGICPFNFPamIPLWMFPV--ALATGNTMVIKPSEQDPGAAQLLVelakeAGVPDgcvniiHGQHSAVNFICDNP 242
Cdd:PLN02203 108 PLGVVLIFSSWNFP--IGLSLEPLigAIAAGNAVVLKPSELAPATSAFLA-----ANIPK------YLDSKAVKVIEGGP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 243 DI---------KAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGV---IMADANKEQTLNQLTAAAFGA-AGQRCMA 309
Cdd:PLN02203 175 AVgeqllqhkwDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 310 LTTaVLVGEARAwlPELVEKAKN-LKVNAGWKPD--TDIGPLISKQSKARVLRLIESakkegaqvPLDGSNITVPGF--E 384
Cdd:PLN02203 255 IDY-VLVEERFA--PILIELLKStIKKFFGENPResKSMARILNKKHFQRLSNLLKD--------PRVAASIVHGGSidE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 385 NGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAIEIINNNPYGNGTAIFTSNGATARKFTNEVDVGQIGIN-V 463
Cdd:PLN02203 324 KKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNdA 403
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 71986308 464 PIPVPLPMFSFTGSRGSFLGdlNFYGKAGIQFYTQWKTVTQywNESLTELKPQmsFP 520
Cdd:PLN02203 404 IIQYACDSLPFGGVGESGFG--RYHGKYSFDTFSHEKAVLR--RSLLTEFEFR--YP 454
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
71-429 |
3.90e-13 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 71.42 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 71 AAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGktLPDA--EGDVSR--------------G--L 132
Cdd:cd07129 3 AAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEArlQGELGRttgqlrlfadlvreGswL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 133 QV-VEHAcsvpsLMMGETLPNvsrdMDTHSYRIPLGVTAGICPFNFP-AmiplwmFPV-------ALATGNTMVIKPSEQ 203
Cdd:cd07129 81 DArIDPA-----DPDRQPLPR----PDLRRMLVPLGPVAVFGASNFPlA------FSVaggdtasALAAGCPVVVKAHPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 204 DPGAAQLLVELA----KEAGVPDGCVNIIHGQHSAVNF-ICDNPDIKAISFVGGDAAGKHIYERGAK--NGKRVQSNMGA 276
Cdd:cd07129 146 HPGTSELVARAIraalRATGLPAGVFSLLQGGGREVGVaLVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 277 KNHGVIMADANKEQ--TLNQLTAAAF-GAAGQRCmaltTA--VLVGEARAWLPELVEKAKNlKVNAgWKPDTDIGPLISK 351
Cdd:cd07129 226 VNPVFILPGALAERgeAIAQGFVGSLtLGAGQFC----TNpgLVLVPAGPAGDAFIAALAE-ALAA-APAQTMLTPGIAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 352 QSKARVLRLIESAkkeGAQVPLDGsnitvPGFENGNFVGPTILA------GVKPNMtcyREEIFGPVLVVMEAENLNEAI 425
Cdd:cd07129 300 AYRQGVEALAAAP---GVRVLAGG-----AAAEGGNQAAPTLFKvdaaafLADPAL---QEEVFGPASLVVRYDDAAELL 368
|
....
gi 71986308 426 EIIN 429
Cdd:cd07129 369 AVAE 372
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
66-427 |
3.36e-12 |
|
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: 68.66 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 66 QAEMQAAVDSAKNAFNTWKNTSPLTRQQ-CMFKLQALIKRDMKkLAESI--TIEQGKTL------PDAEgdvSRGLQVVE 136
Cdd:cd07127 83 QCDPDALLAAARAAMPGWRDAGARARAGvCLEILQRLNARSFE-MAHAVmhTTGQAFMMafqaggPHAQ---DRGLEAVA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 137 HACSVPSLMMGETL---PNVSRD---MDTHSYRIPLGVTAGICPFNFPAmiplW-----MFpVALATGNTMVIKPSeqdP 205
Cdd:cd07127 159 YAWREMSRIPPTAEwekPQGKHDplaMEKTFTVVPRGVALVIGCSTFPT----WngypgLF-ASLATGNPVIVKPH---P 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 206 GA---AQLLVELAK----EAGVPDGCVNII--HGQHSAVNFICDNPDIKAISFVGGDAAGKHIyERGAKnGKRVQSNMGA 276
Cdd:cd07127 231 AAilpLAITVQVARevlaEAGFDPNLVTLAadTPEEPIAQTLATRPEVRIIDFTGSNAFGDWL-EANAR-QAQVYTEKAG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 277 KNHGVIMADANKEQTLNQLTAAAFGAAGQRCMAlTTAVLV-------GEARAWLPE----LVEKAKNLKVNagwkPDTDI 345
Cdd:cd07127 309 VNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTT-PQNIYVprdgiqtDDGRKSFDEvaadLAAAIDGLLAD----PARAA 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 346 GPLISKQSKARVLRLIESAKkeGAQVPLDGSNITVPGFENGNFVGPTILAGVKPNMTCYREEIFGPVLVVMEAENLNEAI 425
Cdd:cd07127 384 ALLGAIQSPDTLARIAEARQ--LGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSI 461
|
..
gi 71986308 426 EI 427
Cdd:cd07127 462 EL 463
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
43-454 |
2.02e-10 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 62.90 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 43 TTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAK--------NAF------NTWKNTSplTRQQCMFKLQA-------L 101
Cdd:cd07126 10 ASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRqcpksglhNPLknperyLLYGDVS--HRVAHELRKPEvedffarL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 102 IKRDMKK-----LAEsITIEQgKTLPDAEGDVSRGLQvveHACSVPSLMMGETlpnvsrdmdTHSYRIPLGVTAGICPFN 176
Cdd:cd07126 88 IQRVAPKsdaqaLGE-VVVTR-KFLENFAGDQVRFLA---RSFNVPGDHQGQQ---------SSGYRWPYGPVAIITPFN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 177 FPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGgdaaG 256
Cdd:cd07126 154 FPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTG----S 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 257 KHIYERGAKNGK-RVQSNMGAKNHGVIMAD-ANKEQTLNQLTAAAFGAAGQRCMAltTAVLVGEARAWLPELVEKAKNLk 334
Cdd:cd07126 230 SKVAERLALELHgKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSA--QSILFAHENWVQAGILDKLKAL- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 335 vnAGWK--PDTDIGPLISKQSKARVLRLIESAKKEGAQV-----PL-DGSNITVPG-FENGNFVGPTILAGVKPNMTCYR 405
Cdd:cd07126 307 --AEQRklEDLTIGPVLTWTTERILDHVDKLLAIPGAKVlfggkPLtNHSIPSIYGaYEPTAVFVPLEEIAIEENFELVT 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 71986308 406 EEIFGPVLVVMEAEN--LNEAIEIINNNPYgNGTAIFTSNGAtarKFTNEV 454
Cdd:cd07126 385 TEVFGPFQVVTEYKDeqLPLVLEALERMHA-HLTAAVVSNDI---RFLQEV 431
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
167-454 |
1.45e-09 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 60.49 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 167 GVTAGICPFNFPAMiPLW-MFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGV-PDGCVNIIHGqhSAVNFICDNPDI 244
Cdd:PRK11903 150 GVALFINAFNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCG--SSAGLLDHLQPF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 245 KAISFVGGDAAGKHIYERGAKNGKRVQSNMGAK--NHGVIMADAnkeqtlnQLTAAAFGA------------AGQRCMAL 310
Cdd:PRK11903 227 DVVSFTGSAETAAVLRSHPAVVQRSVRVNVEADslNSALLGPDA-------APGSEAFDLfvkevvremtvkSGQKCTAI 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 311 TTaVLVGEARAWLPELVEKAKNLKVNAGwKPDTD---IGPLISKQSKARVLRLIEsAKKEGAQVPLDGSNITVPGFEN-- 385
Cdd:PRK11903 300 RR-IFVPEALYDAVAEALAARLAKTTVG-NPRNDgvrMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDADPav 376
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71986308 386 GNFVGPTILAGVKPN--MTCYREEIFGPVLVVMEAENLNEAIEIINNnpyGNG---TAIFTSNGATARKFTNEV 454
Cdd:PRK11903 377 AACVGPTLLGASDPDaaTAVHDVEVFGPVATLLPYRDAAHALALARR---GQGslvASVYSDDAAFLAAAALEL 447
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
134-341 |
2.73e-05 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 46.45 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 134 VVEHACSVPSLMMGETLpnvsrdmdthSYRIPLGVTAGICPFNFPAMIPLWMFpVALATGNTMVIKPSEQDPGAAQLLVE 213
Cdd:cd07077 79 SVGHIQDVLLPDNGETY----------VRAFPIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPFTNRALAL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 214 LAKEA----GVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGakNGKRVQSnMGAKNHGVIM---ADA 286
Cdd:cd07077 148 LFQAAdaahGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHS--PHIPVIG-FGAGNSPVVVdetADE 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 71986308 287 NKEQTLNQLTAAAFGAAgqrCMALTTAVLVGEARAWLPELVE---KAKNLKVNAGWKP 341
Cdd:cd07077 225 ERASGSVHDSKFFDQNA---CASEQNLYVVDDVLDPLYEEFKlklVVEGLKVPQETKP 279
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
165-464 |
1.39e-03 |
|
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: 41.32 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 165 PLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSeqdPGA-------AQLLVELAKEAGVPDGCVNII-HGQHSAVN 236
Cdd:cd07122 95 PVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPH---PRAkkcsieaAKIMREAAVAAGAPEGLIQWIeEPSIELTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 237 FICDNPDIKAISFVGG----DAA---GKHIYERGAKNG-----KRVQSNMGAKN--------HGVIMAdanKEQTL--NQ 294
Cdd:cd07122 172 ELMKHPDVDLILATGGpgmvKAAyssGKPAIGVGPGNVpayidETADIKRAVKDiilsktfdNGTICA---SEQSVivDD 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 295 LTAAAFGAAGQRCMA--LTtavlvgearawlPELVEKAKNLKVNAGWKPDTDIgplISKqsKARVLrliesAKKEGAQVP 372
Cdd:cd07122 249 EIYDEVRAELKRRGAyfLN------------EEEKEKLEKALFDDGGTLNPDI---VGK--SAQKI-----AELAGIEVP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 373 LDgsnITVPGFENgNFVGPT-ILAGvkpnmtcyreEIFGPVLVVMEAENLNEAIE----IINNNPYGNGTAIFTSNGATA 447
Cdd:cd07122 307 ED---TKVLVAEE-TGVGPEePLSR----------EKLSPVLAFYRAEDFEEALEkareLLEYGGAGHTAVIHSNDEEVI 372
|
330
....*....|....*..
gi 71986308 448 RKFTNEVDVGQIGINVP 464
Cdd:cd07122 373 EEFALRMPVSRILVNTP 389
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
419-455 |
5.97e-03 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 39.28 E-value: 5.97e-03
10 20 30
....*....|....*....|....*....|....*....
gi 71986308 419 ENLNEAIEIINNnpYGNG-T-AIFTSNGATARKFTNEVD 455
Cdd:PRK00197 324 DSLDEAIAHINR--YGSGhTeAIVTEDYAAAERFLNEVD 360
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
165-464 |
9.00e-03 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 39.01 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 165 PLGVTAGICPF-N------FPAMIplwmfpvALATGNTMVIKPSeqdPGA-------AQLLVELAKEAGVPDGCVNII-H 229
Cdd:PRK13805 108 PVGVIAGITPTtNptstaiFKALI-------ALKTRNPIIFSFH---PRAqkssiaaAKIVLDAAVAAGAPKDIIQWIeE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 230 GQHSAVNFICDNPDIKAISFVGGDAAGKHIYER-------GAKNG----------KR-VQSNMGAKN--HGVIMAdanKE 289
Cdd:PRK13805 178 PSVELTNALMNHPGIALILATGGPGMVKAAYSSgkpalgvGAGNVpayidktadiKRaVNDILLSKTfdNGMICA---SE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 290 QTLnQLTAAAFGAAGQRCMALTTAVLVGEARAWLPELVEKAKNLKVNAGwkpdtdigplISKQSKARVlrliesAKKEGA 369
Cdd:PRK13805 255 QAV-IVDDEIYDEVKEEFASHGAYFLNKKELKKLEKFIFGKENGALNAD----------IVGQSAYKI------AEMAGF 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71986308 370 QVPlDGSNITVpgFEngnfvgptiLAGVKPNMTCYREEIFgPVLVVMEAENLNEAIEI----INNNPYGNGTAIFTSNGA 445
Cdd:PRK13805 318 KVP-EDTKILI--AE---------VKGVGESEPLSHEKLS-PVLAMYKAKDFEDAVEKaeklVEFGGLGHTAVIYTNDDE 384
|
330
....*....|....*....
gi 71986308 446 TARKFTNEVDVGQIGINVP 464
Cdd:PRK13805 385 LIKEFGLRMKACRILVNTP 403
|
|
| |
