|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
5-481 |
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: 825.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 5 IPQLIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDEL 84
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 85 GELLARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLA 164
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 165 IACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKR 244
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 245 VQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAAVFVG-AAREWIPELAERMAVLRPGHWQDPDAAYGPL 323
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 324 ISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALV 403
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595944 404 NANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPLPFFSFTGWKGSFYGDLHAYGKQAVRFYTETKTVTSRW 481
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
8-481 |
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: 742.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGEL 87
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 88 LARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLAIAC 167
Cdd:TIGR01722 84 ITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIAC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 168 GNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQA 247
Cdd:TIGR01722 164 GNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 248 FAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAAVFVGAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQ 327
Cdd:TIGR01722 244 LGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 328 ARQRVLRLIAEGKAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANP 407
Cdd:TIGR01722 324 AKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASP 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595944 408 YGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPLPFFSFTGWKGSFYGDLHAYGKQAVRFYTETKTVTSRW 481
Cdd:TIGR01722 404 YGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
5-481 |
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: 568.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 5 IPQLIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDEL 84
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 85 GELLARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLA 164
Cdd:COG1012 86 AALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 165 IACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLK 243
Cdd:COG1012 166 LAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGdGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 244 RVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISaAVFV--GAAREWIPELAERMAVLRPGHWQDPDAAYG 321
Cdd:COG1012 246 RVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAAS-RLLVheSIYDEFVERLVAAAKALKVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 322 PLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGypnGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIA 401
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEG---GYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 402 LVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPLPFFSFTGWKGSFYGDLHayGKQAVRFYTETKTVTSRW 481
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREG--GREGLEEYTETKTVTIRL 479
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
1-488 |
0e+00 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 556.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 1 MAKAIPQLIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEH 80
Cdd:PLN02419 110 MPPRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKN 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 81 HDELGELLARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFPAMIPLWM 160
Cdd:PLN02419 190 MDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWM 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 161 FPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTA 240
Cdd:PLN02419 270 FPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 241 HLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAAVFVGAAREWIPELAERMAVLRPGHWQDPDAAY 320
Cdd:PLN02419 350 KGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADL 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 321 GPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAI 400
Cdd:PLN02419 430 GPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAI 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 401 ALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPLPFFSFTGWKGSFYGDLHAYGKQAVRFYTETKTVTSR 480
Cdd:PLN02419 510 SIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQK 589
|
....*...
gi 15595944 481 WfDDEPTT 488
Cdd:PLN02419 590 Q-KDIHSP 596
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
13-477 |
3.61e-177 |
|
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: 505.53 E-value: 3.61e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 13 WRGSRSRElVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARET 92
Cdd:pfam00171 1 WVDSESET-IEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 93 GKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIDTASWiQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFV 172
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRR-EPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 173 LKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGA 251
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 252 KNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISaAVFV--GAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQAR 329
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATS-RLLVheSIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 330 QRVLRLIAEGKAEGAECLLDGSqcqvEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYG 409
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGE----AGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595944 410 NGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPLPFFSFTGWKGSFYGDlhAYGKQAVRFYTETKTV 477
Cdd:pfam00171 394 LAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGR--EGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
45-478 |
1.03e-142 |
|
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: 416.99 E-value: 1.03e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 45 EQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVWRGIEVVEHAANVASLMMGET 124
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 125 VENVAReiDTASWI--QPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQV 202
Cdd:cd07078 81 IPSPDP--GELAIVrrEPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 203 IHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQR 281
Cdd:cd07078 159 VTGDGDEVgAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 282 CMAISaAVFV--GAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSqcqVEGYP 359
Cdd:cd07078 239 CTAAS-RLLVheSIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGK---RLEGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 360 NGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVP 439
Cdd:cd07078 315 KGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*....
gi 15595944 440 IPVPLPFFSFTGWKGSFYGDLHayGKQAVRFYTETKTVT 478
Cdd:cd07078 395 SVGAEPSAPFGGVKQSGIGREG--GPYGLEEYTEPKTVT 431
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
8-478 |
1.69e-135 |
|
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: 400.18 E-value: 1.69e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSRSRELVEVTDPA-TQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGE 86
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 87 LLARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLAIA 166
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 167 CGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRV 245
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 246 QAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAA-VFVGAAREWIPELAERMAVLRPGHWQDPDAAYGPLI 324
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLiVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 325 SPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVN 404
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595944 405 ANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPI---PVPLPffsFTGWKGSFYGDLHAyGKQAVRFYTETKTVT 478
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTigaEVHLP---FGGVKKSGNGHREA-GTTALDAFTEWKAVY 474
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
8-477 |
2.28e-125 |
|
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: 373.89 E-value: 2.28e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSRSRElvEVTDPA-TQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGE 86
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 87 LLARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLAIA 166
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 167 CGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRV 245
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 246 QAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAAVFV-GAAREWIPELAERMAVLRPGHWQDPDAAYGPLI 324
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTeGIHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 325 SPQARQRVLRLIAEGKAEGAEcLLDGSQcQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVN 404
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAK-LVYGGE-RLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595944 405 ANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVP-----IPVPlpffsFTGWKGSFYGdLHAYGKQAVRFYTETKTV 477
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPtagvdYHVP-----FGGRKGSSYG-PREQGEAALEFYTTIKTV 471
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
8-478 |
1.16e-117 |
|
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: 354.56 E-value: 1.16e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSrSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGEL 87
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 88 LARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETV-----ENVAREIdtasWiQPLGVCAGITPFNFPAMIPLWMFP 162
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIpserpGHRLMEQ----W-NPLGVVGVITAFNFPVAVPGWNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 163 LAIACGNTFVLKPSEQDPLTPNRLAELFLEA----GAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTG 238
Cdd:cd07086 156 IALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 239 TAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAA-VFVGAAREWIPELAERMAVLRPGHWQDPD 317
Cdd:cd07086 236 ARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLiVHESVYDEFLERLVKAYKQVRIGDPLDEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 318 AAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSqcQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLE 397
Cdd:cd07086 316 TLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGK--RIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 398 EAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVgQVGI-NVPIP-----VPLPffsFTGWKGSfyGDLHAYGKQAVRFY 471
Cdd:cd07086 394 EAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGS-DCGIvNVNIPtsgaeIGGA---FGGEKET--GGGRESGSDAWKQY 467
|
....*..
gi 15595944 472 TETKTVT 478
Cdd:cd07086 468 MRRSTCT 474
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
24-478 |
1.02e-116 |
|
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: 350.96 E-value: 1.02e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 24 VTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDV 103
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 104 WRGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFP-AMIPLWMFPlAIACGNTFVLKPSEQDPLT 182
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPaAMITRKIAP-ALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 183 PNRLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDA 261
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 262 NKAQVLGNLVGASCGAAGQRCmaISA-AVFV--GAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAE 338
Cdd:cd07103 240 DLDKAVDGAIASKFRNAGQTC--VCAnRIYVheSIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 339 GKAEGAECLLDGSQCQvegyPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRS 418
Cdd:cd07103 318 AVAKGAKVLTGGKRLG----LGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 419 GGAARRYQHAVQVGQVGINVPIPvPLPFFSFTGWKGSFYGdlHAYGKQAVRFYTETKTVT 478
Cdd:cd07103 394 LARAWRVAEALEAGMVGINTGLI-SDAEAPFGGVKESGLG--REGGKEGLEEYLETKYVS 450
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
24-478 |
2.18e-109 |
|
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: 332.61 E-value: 2.18e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 24 VTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAK-GD 102
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 103 VWRGIEVVEHAANVASLMMGETVENVAREIDTASWiQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLT 182
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALNYVLR-QPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 183 PNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDA 261
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 262 NKAQVLGNLVGASCGAAGQRCMAISAaVFV--GAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEG 339
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSR-ILVqrSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 340 KAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSG 419
Cdd:cd07093 319 RAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595944 420 GAARRYQHAVQVGQVGINVPI----PVPlpffsFTGWKGSfyGDLHAYGKQAVRFYTETKTVT 478
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLvrdlRTP-----FGGVKAS--GIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
49-478 |
2.25e-104 |
|
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: 316.48 E-value: 2.25e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 49 ASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENV 128
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 129 AReiDTASWI--QPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG- 205
Cdd:cd06534 81 DP--GGEAYVrrEPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 206 GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAI 285
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 286 SAAVFVGAAREwipELAERMAvlrpghwqdpdaaygplispqarqrvlrliaegkaegaeclldgsqcqvegypngnwlg 365
Cdd:cd06534 239 SRLLVHESIYD---EFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 366 pTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPLP 445
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGP 335
|
410 420 430
....*....|....*....|....*....|...
gi 15595944 446 FFSFTGWKGSFYGDLHayGKQAVRFYTETKTVT 478
Cdd:cd06534 336 EAPFGGVKNSGIGREG--GPYGLEEYTRTKTVV 366
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
24-477 |
2.13e-103 |
|
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: 317.19 E-value: 2.13e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 24 VTDPATQDVLALAPKATADEIEQAIASAQRAFET--WREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKG 101
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 102 DVWRGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPL 181
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 182 TPNRLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPD 260
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETgEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 261 ANKAQVLGNLVGASCGAAGQRCMAISAaVFV--GAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAE 338
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSR-LLVqrSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 339 GKAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRS 418
Cdd:cd07114 320 AREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595944 419 GGAARRYQHAVQVGQVGIN----VPIPVPlpffsFTGWKGSFYGdlHAYGKQAVRFYTETKTV 477
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNtyraLSPSSP-----FGGFKDSGIG--RENGIEAIREYTQTKSV 455
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
9-477 |
2.66e-101 |
|
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: 312.28 E-value: 2.66e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELL 88
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 89 ARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENvAREIDTASWI-QPLGVCAGITPFNFP-AMIPLWMFPlAIA 166
Cdd:cd07088 82 VEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPS-DRPNENIFIFkVPIGVVAGILPWNFPfFLIARKLAP-ALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 167 CGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRV 245
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 246 QAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISaAVFVGA--AREWIPELAERMAVLRPGHWQDPDAAYGPL 323
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAE-RVYVHEdiYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 324 ISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGypnGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALV 403
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGGKRPEGEK---GYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595944 404 NANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPLPFFSfTGWKGSFYGDlhAYGKQAVRFYTETKTV 477
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH-AGWKKSGLGG--ADGKHGLEEYLQTKVV 466
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
9-477 |
7.53e-101 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 311.43 E-value: 7.53e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELL 88
Cdd:PRK13252 11 IDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 89 ARETGKNLADAK-GDVWRGIEVVEHAANVASLMMGETVEnvareIDTASWI----QPLGVCAGITPFNFPAMIPLWMFPL 163
Cdd:PRK13252 91 TLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIP-----LRGGSFVytrrEPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 164 AIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLK 243
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 244 RVQAFAGAKNHMVILPDAN-----KAQVLGNLVgascgAAGQRCMAiSAAVFVGAA--REWIPELAERMAVLRPGHWQDP 316
Cdd:PRK13252 246 EVTMELGGKSPLIVFDDADldraaDIAMLANFY-----SSGQVCTN-GTRVFVQKSikAAFEARLLERVERIRIGDPMDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 317 DAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESL 396
Cdd:PRK13252 320 ATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 397 EEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINV--PIPVPLPffsFTGWKGSFYGdlHAYGKQAVRFYTET 474
Cdd:PRK13252 400 DEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPAEMP---VGGYKQSGIG--RENGIATLEHYTQI 474
|
...
gi 15595944 475 KTV 477
Cdd:PRK13252 475 KSV 477
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
24-477 |
4.22e-100 |
|
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: 308.85 E-value: 4.22e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 24 VTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDV 103
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 104 WRGIEVVEHAANVASLMMGETVEnvareIDTASWI----QPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQD 179
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVP-----LPGGSFAytrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 180 PLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILP 259
Cdd:cd07090 156 PLTALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 260 DANKAQVLGNLVGASCGAAGQRCmAISAAVFVGAAR--EWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIA 337
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVC-SNGTRVFVQRSIkdEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 338 EGKAEGAECLLDGSQCQVE-GYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFT 416
Cdd:cd07090 315 SAKQEGAKVLCGGERVVPEdGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595944 417 RSGGAARRYQHAVQVGQVGIN----VPIPVPlpffsFTGWKGSFYGdlHAYGKQAVRFYTETKTV 477
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFG--RENGTAALEHYTQLKTV 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
8-477 |
6.34e-100 |
|
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: 308.73 E-value: 6.34e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSrSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFE-TWREVPAPERARLMLRYQHLLKEHHDELGE 86
Cdd:cd07082 5 LINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRgWWPTMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 87 LLARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETV----ENVAREidTASWIQ--PLGVCAGITPFNFP------A 154
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLpgdwFPGTKG--KIAQVRrePLGVVLAIGPFNYPlnltvsK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 155 MIPlwmfplAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQH 233
Cdd:cd07082 162 LIP------ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 234 VYRTGtaHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAaVFV--GAAREWIPELAERMAVLRPG 311
Cdd:cd07082 236 LKKQH--PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-VLVheSVADELVELLKEEVAKLKVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 312 HWQDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGsqcqveGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACL 391
Cdd:cd07082 313 MPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPII 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 392 EVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINV-----PipvplPFFSFTGWKGSfygdlhAYGKQ 466
Cdd:cd07082 387 RVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSkcqrgP-----DHFPFLGRKDS------GIGTQ 455
|
490
....*....|....*
gi 15595944 467 ----AVRFYTETKTV 477
Cdd:cd07082 456 gigdALRSMTRRKGI 470
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
24-478 |
1.73e-98 |
|
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: 304.54 E-value: 1.73e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 24 VTDPATQDVLALAPKATADEIEQAIASAQRAFET-WREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGD 102
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 103 VWRGIEVVEHAANVASLMMGETVeNVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLT 182
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETI-PLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 183 PNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDA 261
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 262 NKAQVLGNLVGASCGAAGQRCMAISAAVFVGAAR-EWIPELAERMAVLRPGHWQ-DPDaaYGPLISPQARQRVLRLIAEG 339
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYdEVLERLVERFRALRVGPGLeDPD--LGPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 340 KAEGAECLLDGSQcqVEGYPNGNW-LGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRS 418
Cdd:cd07109 318 RARGARIVAGGRI--AEGAPAGGYfVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595944 419 GGAARRYQHAVQVGQVGINVPIP---VPLPffsFTGWKGSFYGdlHAYGKQAVRFYTETKTVT 478
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNNYGAgggIELP---FGGVKKSGHG--REKGLEALYNYTQTKTVA 453
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
9-475 |
1.76e-98 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 304.81 E-value: 1.76e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELL 88
Cdd:TIGR01804 2 IDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 89 ARETGKNLADA-KGDVWRGIEVVEHAANVASLMMGETVEnvAREIDTASWI-QPLGVCAGITPFNFPAMIPLWMFPLAIA 166
Cdd:TIGR01804 82 TLDTGKTLQETiVADMDSGADVFEFFAGLAPALNGEIIP--LGGPSFAYTIrEPLGVCVGIGAWNYPLQIASWKIAPALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 167 CGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRV 245
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGdGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 246 QAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAiSAAVFVGAA--REWIPELAERMAVLRPGHWQDPDAAYGPL 323
Cdd:TIGR01804 240 TMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSN-GTRVFVHKKikERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 324 ISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALV 403
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595944 404 NANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINV--PIPVPLPffsFTGWKGSFYGdlHAYGKQAVRFYTETK 475
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTynLYPAEAP---FGGYKQSGIG--RENGKAALAHYTEVK 467
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
9-477 |
4.25e-98 |
|
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: 304.23 E-value: 4.25e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFET--WREVPAPERARLMLRYQHLLKEHHDELGE 86
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 87 LLARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVEnVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLAIA 166
Cdd:cd07119 82 LETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYD-VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 167 CGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRV 245
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 246 QAFAGAKNHMVILPDAN-KAQVLGNLVGASCGAaGQRCMAISA-AVFVGAAREWIPELAERMAVLRPGHWQDPDAAYGPL 323
Cdd:cd07119 241 ALELGGKNPNIVFADADfETAVDQALNGVFFNA-GQVCSAGSRlLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 324 ISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALV 403
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595944 404 NANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVpLPFFSFTGWKGSFYGdlHAYGKQAVRFYTETKTV 477
Cdd:cd07119 400 NDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPY-FAEAPWGGYKQSGIG--RELGPTGLEEYQETKHI 470
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
23-478 |
1.43e-97 |
|
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: 301.82 E-value: 1.43e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 23 EVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGD 102
Cdd:cd07149 2 EVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 103 VWRGIEVVEHAANVASLMMGETV--ENVAREIDTASWI--QPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQ 178
Cdd:cd07149 82 VDRAIETLRLSAEEAKRLAGETIpfDASPGGEGRIGFTirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 179 DPLTPNRLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRtgTAHLKRVQAFAGAKNHMVI 257
Cdd:cd07149 162 TPLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIAR--KAGLKKVTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 258 LPDANKAQVLGNLVGASCGAAGQRCmaISAA-VFVGAAR--EWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLR 334
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQVC--ISVQrIFVHEDIydEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 335 LIAEGKAEGAEcLLDGsqcqveGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSL 414
Cdd:cd07149 318 WVEEAVEGGAR-LLTG------GKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595944 415 FTRSGGAARRYQHAVQVGQVGINVPIPVPLPFFSFTGWKGSfygdlhAYGKQAVRF----YTETKTVT 478
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMINDSSTFRVDHMPYGGVKES------GTGREGPRYaieeMTEIKLVC 452
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
43-478 |
1.40e-96 |
|
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: 298.68 E-value: 1.40e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 43 EIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVWRGIEVVEHAANVASLMMG 122
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 123 ETVENVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPN-RLAELFLEAGAPKGVLQ 201
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGlLIAEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 202 VIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQ 280
Cdd:cd07104 161 VVPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 281 RCMAIS-----AAVfvgaAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLldgsqcqV 355
Cdd:cd07104 241 ICMAAGrilvhESV----YDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLL-------T 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 356 EGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVG 435
Cdd:cd07104 310 GGTYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVH 389
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15595944 436 INVPIPVPLPFFSFTGWKGSFYGDLHayGKQAVRFYTETKTVT 478
Cdd:cd07104 390 INDQTVNDEPHVPFGGVKASGGGRFG--GPASLEEFTEWQWIT 430
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
8-478 |
1.80e-95 |
|
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: 297.20 E-value: 1.80e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFET--WREVPAPERARLMLRYQHLLKEHHDELG 85
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 86 ELLARETGKNL-ADAKGDVWRGIEVVEHAANVASLMMGETVEnVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLA 164
Cdd:cd07091 87 ALESLDNGKPLeESAKGDVALSIKCLRYYAGWADKIQGKTIP-IDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 165 IACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRT-GTAHL 242
Cdd:cd07091 166 LAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAaAKSNL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 243 KRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISaAVFV--GAAREWIPELAERMAVLRPGHWQDPDAAY 320
Cdd:cd07091 246 KKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGS-RIFVqeSIYDEFVEKFKARAEKRVVGDPFDPDTFQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 321 GPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAI 400
Cdd:cd07091 325 GPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGY----FIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 401 ALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGIN--------VPipvplpffsFTGWKGSFYG-DLHAYGKQAvrfY 471
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNtynvfdaaVP---------FGGFKQSGFGrELGEEGLEE---Y 468
|
....*..
gi 15595944 472 TETKTVT 478
Cdd:cd07091 469 TQVKAVT 475
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
24-480 |
4.11e-95 |
|
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: 295.82 E-value: 4.11e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 24 VTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDV 103
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 104 WRGIEVVEHAANVASLMMGETVENVAREIDTaSWIQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTP 183
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNLHY-TLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 184 NRLAELFLEAgAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDAN 262
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 263 -KAQVLGNLVGASCGAAGQRCMAISAAvFVGAA--REWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEG 339
Cdd:cd07107 239 pEAAADAAVAGMNFTWCGQSCGSTSRL-FVHESiyDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 340 KAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSG 419
Cdd:cd07107 318 KREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595944 420 GAARRYQHAVQVGQVGIN--------VPipvplpffsFTGWKGSFYGDLHayGKQAVRFYTETKTVTSR 480
Cdd:cd07107 398 SQAHRTARRVEAGYVWINgssrhflgAP---------FGGVKNSGIGREE--CLEELLSYTQEKNVNVR 455
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
7-481 |
4.81e-95 |
|
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: 296.28 E-value: 4.81e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 7 QLIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFET-WREVPAPERARLMLRYQHLLKEHHDELG 85
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 86 ELLARETGKNLAdakgdVWRGIEVVEHA------ANVASLMMGETVE----NVAREIDTA-SWIQPLGVCAGITPFNFPA 154
Cdd:cd07113 82 QLETLCSGKSIH-----LSRAFEVGQSAnflryfAGWATKINGETLApsipSMQGERYTAfTRREPVGVVAGIVPWNFSV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 155 MIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHV 234
Cdd:cd07113 157 MIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 235 YRTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCmAISAAVFVGAAR--EWIPELAERMAVLRPGH 312
Cdd:cd07113 237 GRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVC-AAPERFYVHRSKfdELVTKLKQALSSFQVGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 313 WQDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLE 392
Cdd:cd07113 316 PMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGY----FVQPTLVLARSADSRLMREETFGPVVSFVP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 393 VESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPlPFFSFTGWKGSFYGdlHAYGKQAVRFYT 472
Cdd:cd07113 392 YEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLD-PAVPFGGMKQSGIG--REFGSAFIDDYT 468
|
....*....
gi 15595944 473 ETKTVTSRW 481
Cdd:cd07113 469 ELKSVMIRY 477
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
24-477 |
7.55e-95 |
|
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: 294.82 E-value: 7.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 24 VTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDV 103
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 104 WRGIEVVEHAANvaslmMGETVEnVAREIDTASWI---QPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDP 180
Cdd:cd07106 81 GGAVAWLRYTAS-----LDLPDE-VIEDDDTRRVElrrKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 181 LTPNRLAELFLEAgAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPD 260
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 261 ANKAQVLGNLVGASCGAAGQRCMAISaAVFVGAA-----REWIPELAERMAVlrpGHWQDPDAAYGPLISPQARQRVLRL 335
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIK-RLYVHESiydefCEALVALAKAAVV---GDGLDPGTTLGPVQNKMQYDKVKEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 336 IAEGKAEGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLF 415
Cdd:cd07106 310 VEDAKAKGAKVLAGGEPLDGPGY----FIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVW 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595944 416 TRSGGAARRYQHAVQVGQVGINvPIPVPLPFFSFTGWKGSFYGdlHAYGKQAVRFYTETKTV 477
Cdd:cd07106 386 SSDLERAEAVARRLEAGTVWIN-THGALDPDAPFGGHKQSGIG--VEFGIEGLKEYTQTQVI 444
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
9-478 |
9.77e-95 |
|
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: 295.25 E-value: 9.77e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFE--TWREVPAPERARLMLRYQHLLKEHHDELGE 86
Cdd:cd07139 3 IGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDngPWPRLSPAERAAVLRRLADALEARADELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 87 LLARETGKNLADAK-GDVWRGIEVVEHAANVA----------SLMMGETVenVAREidtaswiqPLGVCAGITPFNFPAM 155
Cdd:cd07139 83 LWTAENGMPISWSRrAQGPGPAALLRYYAALArdfpfeerrpGSGGGHVL--VRRE--------PVGVVAAIVPWNAPLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 156 IPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVY 235
Cdd:cd07139 153 LAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 236 RTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAaVFVGAAR--EWIPELAERMAVLRPGHW 313
Cdd:cd07139 233 AVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTR-ILVPRSRydEVVEALAAAVAALKVGDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 314 QDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCqvEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEV 393
Cdd:cd07139 312 LDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRP--AGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 394 ESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVP-LPffsFTGWKGSFYGdlHAYGKQAVRFYT 472
Cdd:cd07139 390 DDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFgAP---FGGFKQSGIG--REGGPEGLDAYL 464
|
....*.
gi 15595944 473 ETKTVT 478
Cdd:cd07139 465 ETKSIY 470
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
24-477 |
1.86e-94 |
|
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: 294.15 E-value: 1.86e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 24 VTDPATQDVLALAPKATADEIEQAIASAQRAFETW-REVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKG- 101
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 102 DVWRGIEVVEHAANVASLMMGET--VENVAREIDTASWI--QPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSE 177
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFdlPVPALRGGPGRRVVrrEPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 178 QDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLT-HPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMV 256
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTtDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 257 ILPDANKAQVLGNLVGASCGAAGQRCmAISAAVFVGAAR--EWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLR 334
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGC-ALTTRLLVPRSRydEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 335 LIAEGKAEGAECLLDGSqcQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSL 414
Cdd:cd07089 320 YIARGRDEGARLVTGGG--RPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595944 415 FTRSGGAARRYQHAVQVGQVGINvpipvPLPFFS----FTGWKGSFYGdlHAYGKQAVRFYTETKTV 477
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGIN-----GGGGYGpdapFGGYKQSGLG--RENGIEGLEEFLETKSI 457
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
23-478 |
2.48e-94 |
|
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: 293.47 E-value: 2.48e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 23 EVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGD 102
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 103 VWRGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLT 182
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 183 PNRLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDA 261
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 262 NKAQVLGnlvGASCGA---AGQRCMA-----ISAAVFvgaaREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVL 333
Cdd:cd07150 242 DLDYAVR---AAAFGAfmhQGQICMSasriiVEEPVY----DEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 334 RLIAEGKAEGAEcLLDGsqcqveGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTS 413
Cdd:cd07150 315 RQVEDAVAKGAK-LLTG------GKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595944 414 LFTRSGGAARRYQHAVQVGQVGINVPIPVPLPFFSFTGWKGSFYGdlHAYGKQAVRFYTETKTVT 478
Cdd:cd07150 388 ILTNDLQRAFKLAERLESGMVHINDPTILDEAHVPFGGVKASGFG--REGGEWSMEEFTELKWIT 450
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
3-481 |
3.95e-94 |
|
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: 294.90 E-value: 3.95e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 3 KAIPQLIDGEWRgsRSRELVEVTDPA-TQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHH 81
Cdd:cd07124 31 REYPLVIGGKEV--RTEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 82 DELGELLARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREiDTASWIQPLGVCAGITPFNFPAMIPLWMF 161
Cdd:cd07124 109 FELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGE-DNRYVYRPLGVGAVISPWNFPLAILAGMT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 162 PLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYR---- 236
Cdd:cd07124 188 TAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYEraak 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 237 --TGTAHLKRVQAFAGAKNHMVILPDAN-KAQVLGNLVGAScGAAGQRCMAISAAVFVGAA-REWIPELAERMAVLRPGH 312
Cdd:cd07124 268 vqPGQKWLKRVIAEMGGKNAIIVDEDADlDEAAEGIVRSAF-GFQGQKCSACSRVIVHESVyDEFLERLVERTKALKVGD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 313 WQDPDAAYGPLISPQARQRVLRLIAEGKAEGaECLLDGSqcQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLE 392
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGE--VLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 393 VESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPLP-FFSFTGWKGSfyG-DLHAYGKQAVRF 470
Cdd:cd07124 424 AKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVgRQPFGGFKMS--GtGSKAGGPDYLLQ 501
|
490
....*....|.
gi 15595944 471 YTETKTVTSRW 481
Cdd:cd07124 502 FMQPKTVTENF 512
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
23-477 |
6.88e-94 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 292.97 E-value: 6.88e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 23 EVTDPATQDVLALAPKATADEIEQAIASAQRAFE--TWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADA- 99
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 100 KGDVWRGIEVVEHAANVASLMMGE---TVEN----VAREidtaswiqPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFV 172
Cdd:cd07112 85 AVDVPSAANTFRWYAEAIDKVYGEvapTGPDalalITRE--------PLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 173 LKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYR-TGTAHLKRVQAFAG 250
Cdd:cd07112 157 LKPAEQSPLTALRLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLEySGQSNLKRVWLECG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 251 AKNHMVILPDAnkaqvlGNLVGASCGAA-------GQRCMAISAA-VFVGAAREWIPELAERMAVLRPGHWQDPDAAYGP 322
Cdd:cd07112 237 GKSPNIVFADA------PDLDAAAEAAAagifwnqGEVCSAGSRLlVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 323 LISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGypNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIAL 402
Cdd:cd07112 311 LVSEAHFDKVLGYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVAL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 403 VNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGIN----VPIPVPlpffsFTGWKGSFYG---DLHAYGKqavrfYTETK 475
Cdd:cd07112 389 ANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNcfdeGDITTP-----FGGFKQSGNGrdkSLHALDK-----YTELK 458
|
..
gi 15595944 476 TV 477
Cdd:cd07112 459 TT 460
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
26-477 |
8.92e-94 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 292.42 E-value: 8.92e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 26 DPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKG-DVW 104
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 105 RGIEVVEHAANVASLMMGETVENVAREIDTASwIQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPN 184
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRGPFLNYTV-REPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 185 RLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDAN- 262
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 263 KAQVLGNLVGAScGAAGQRCMAISAA-VFVGAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGKA 341
Cdd:cd07115 242 DAAVRAAATGIF-YNQGQMCTAGSRLlVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 342 EGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSGGA 421
Cdd:cd07115 321 EGARLLTGGKRPGARGF----FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15595944 422 ARRYQHAVQVGQVGINV--PIPVPLPffsFTGWKGSFYGDLHayGKQAVRFYTETKTV 477
Cdd:cd07115 397 AHRVAAALKAGTVWINTynRFDPGSP---FGGYKQSGFGREM--GREALDEYTEVKSV 449
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
7-478 |
1.88e-92 |
|
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: 289.02 E-value: 1.88e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 7 QLIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGE 86
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 87 LLARETGKNLADAKGD-VWRGIEVVEHAANVASLM-MGETVEN--VAREidtaswiqPLGVCAGITPFNFPA-MIPLWMF 161
Cdd:cd07138 81 AITLEMGAPITLARAAqVGLGIGHLRAAADALKDFeFEERRGNslVVRE--------PIGVCGLITPWNWPLnQIVLKVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 162 PlAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTA 240
Cdd:cd07138 153 P-ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGdGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 241 HLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISaAVFVGAAR-EWIPELAERMAV-LRPGHWQDPDA 318
Cdd:cd07138 232 TVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPT-RMLVPRSRyAEAEEIAAAAAEaYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 319 AYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQcQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEE 398
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 399 AIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPL-PffsFTGWKGSfyGDLHAYGKQAVRFYTETKTV 477
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGaP---FGGYKQS--GNGREWGRYGLEEFLEVKSI 464
|
.
gi 15595944 478 T 478
Cdd:cd07138 465 Q 465
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
22-477 |
1.03e-89 |
|
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: 281.93 E-value: 1.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 22 VEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKG 101
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 102 DVWRGIEVVEHAANVASLMMGETVENVAREIDTASWI----QPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSE 177
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERRIAftvrEPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 178 QDPLTPNRLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMV 256
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 257 ILPDANKAQVLGNLVGASCGAAGQRCMAISaAVFV--GAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLR 334
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVK-RILVeeEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 335 LIAEGKAEGAECLLDGSQcqvegyPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSL 414
Cdd:cd07145 320 LVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595944 415 FTRSGGAARRYQHAVQVGQVGINVPIPVPLPFFSFTGWKGSfygdlhAYGKQAVRF----YTETKTV 477
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKS------GIGREGVRYtmleMTEEKTI 454
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
8-458 |
1.59e-89 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 282.73 E-value: 1.59e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGEL 87
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 88 LARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFP-AMIPLWMFPlAIA 166
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITRKVGP-ALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 167 CGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRV 245
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 246 QAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCmaISAAVFV---GAAREWIPELAERMAVLRPGHWQDPDAAYGP 322
Cdd:PLN02278 267 SLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTC--VCANRILvqeGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 323 LISPQARQRVLRLIAEGKAEGAECLLDGSQCQvegyPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIAL 402
Cdd:PLN02278 345 LINEAAVQKVESHVQDAVSKGAKVLLGGKRHS----LGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAI 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595944 403 VNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGIN---VPIPVPlPFFSF----TGWKGSFYG 458
Cdd:PLN02278 421 ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNeglISTEVA-PFGGVkqsgLGREGSKYG 482
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
9-477 |
2.13e-89 |
|
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: 281.99 E-value: 2.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFET-WREVPAPERARLMLRYQHLLKEHHDELGEL 87
Cdd:cd07144 12 INNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 88 LARETGKNL-ADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIdtASWI-QPLGVCAGITPFNFPAMIPLWMFPLAI 165
Cdd:cd07144 92 EALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKL--AYTLhEPYGVCGQIIPWNYPLAMAAWKLAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 166 ACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKR 244
Cdd:cd07144 170 AAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 245 VQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAIS-----AAVFVGAAREWIPELAERMAVlrpGHWQDPDAA 319
Cdd:cd07144 250 VTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSriyvqESIYDKFVEKFVEHVKQNYKV---GSPFDDDTV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 320 YGPLISPQARQRVLRLIAEGKAEGAECLLDGSQcQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEA 399
Cdd:cd07144 327 VGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK-APEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 400 IALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVP----IPVPlpffsFTGWKGSFYG-DLHAYGKQAvrfYTET 474
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMSGIGrELGEYGLET---YTQT 477
|
...
gi 15595944 475 KTV 477
Cdd:cd07144 478 KAV 480
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
27-478 |
2.94e-89 |
|
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: 280.76 E-value: 2.94e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 27 PATQDVLALAPKATADEIEQAIASAQRAFET--WREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVW 104
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 105 RGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPN 184
Cdd:cd07118 84 GAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 185 RLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDAN- 262
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADl 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 263 KAQVLGNLVGAsCGAAGQRCMAiSAAVFV--GAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGK 340
Cdd:cd07118 244 DAAADAVVFGV-YFNAGECCNS-GSRLLVheSIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 341 AEGAECLLDGSQCQVEgypNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSGG 420
Cdd:cd07118 322 AEGATLLLGGERLASA---AGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDID 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595944 421 ----AARRyqhaVQVGQVGINVPIP--VPLPffsFTGWKGSFYGdlHAYGKQAVRFYTETKTVT 478
Cdd:cd07118 399 taltVARR----IRAGTVWVNTFLDgsPELP---FGGFKQSGIG--RELGRYGVEEYTELKTVH 453
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
11-478 |
6.89e-89 |
|
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: 279.96 E-value: 6.89e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 11 GEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLAR 90
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 91 ETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLAIACGNT 170
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 171 FVLKPSEQDPLTPNRL-AELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAF 248
Cdd:cd07151 161 VVLKPASDTPITGGLLlAKIFEEAGLPKGVLNVVVGaGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 249 AGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAaVFVGAA--REWIPELAERMAVLRPGHWQDPDAAYGPLISP 326
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINR-IIVHEDvyDEFVEKFVERVKALPYGDPSDPDTVVGPLINE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 327 QARQRVLRLIAEGKAEGAECLldgsqcqVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNAN 406
Cdd:cd07151 320 SQVDGLLDKIEQAVEEGATLL-------VGGEAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDT 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595944 407 PYGNGTSLFTRSGGAARRYQHAVQVGQVGINvPIPV-PLPFFSFTGWKGSFYGDLHayGKQAVRFYTETKTVT 478
Cdd:cd07151 393 EYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVnDEPHVPFGGEKNSGLGRFN--GEWALEEFTTDKWIS 462
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
24-478 |
1.52e-87 |
|
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: 276.16 E-value: 1.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 24 VTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNL-ADAKGD 102
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 103 VWRGIEVVEHAANVASLMMGETV---ENVAreidTASWIQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQD 179
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLpfgPDVL----TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 180 PLTPNRLAELfLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVIL 258
Cdd:cd07108 157 PLAVLLLAEI-LAQVLPAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 259 PDANKAQVL-GNLVGASCGAAGQRCMAiSAAVFVGAA--REWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRL 335
Cdd:cd07108 236 PDADLDDAVdGAIAGMRFTRQGQSCTA-GSRLFVHEDiyDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 336 IAEGKAE-GAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSL 414
Cdd:cd07108 315 IDLGLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595944 415 FTRSGGAARRYQHAVQVGQVGINVPIpVPLPFFSFTGWKGSfygdlhAYGKQA-----VRFYTETKTVT 478
Cdd:cd07108 395 WTRDLGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQS------GLGREAslegmLEHFTQKKTVN 456
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
22-478 |
1.20e-85 |
|
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: 271.23 E-value: 1.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 22 VEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKG 101
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 102 DVWRGIEVVEHAANVASLMMGETV--ENVAREIDTASWI--QPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSE 177
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIplDATQGSDNRLAWTirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 178 QDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVyrTGTAHLKRVQAFAGAKNHMV 256
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGeREVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 257 ILPDANKAQVLGNLVGASCGAAGQRCMAISaAVFVGA--AREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLR 334
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQ-RIYVHEelYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 335 LIAEGKAEGAEcLLDGsqcqveGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSL 414
Cdd:cd07094 318 WVEEAVEAGAR-LLCG------GERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGI 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595944 415 FTRSGGAARRYQHAVQVGQVGINVPIPVPLPFFSFTGWKGSFYGDLHAygKQAVRFYTETKTVT 478
Cdd:cd07094 391 FTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGVGREGV--PYAMEEMTEEKTVV 452
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
24-479 |
2.24e-85 |
|
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: 270.35 E-value: 2.24e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 24 VTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGD- 102
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 103 VWRGIEVVEHAANVASLM----MGETVEN----VAREidtaswiqPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLK 174
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLegpaAGEYLPGhtsmIRRE--------PIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 175 PSEQDPLTPNRLAELfLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKN 253
Cdd:cd07092 153 PSETTPLTTLLLAEL-AAEVLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 254 HMVILPDANKAQVLGNLVGASCGAAGQRCMAISaAVFVGAA--REWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQR 331
Cdd:cd07092 232 PVIVFDDADLDAAVAGIATAGYYNAGQDCTAAC-RVYVHESvyDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 332 VLRLIAEGKAeGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNG 411
Cdd:cd07092 311 VAGFVERAPA-HARVLTGGRRAEGPGY----FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLA 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595944 412 TSLFTRSGGAARRYQHAVQVGQVGINVPIPVP--LPffsFTGWKGSFYG-DLHAYGkqaVRFYTETKTVTS 479
Cdd:cd07092 386 SSVWTRDVGRAMRLSARLDFGTVWVNTHIPLAaeMP---HGGFKQSGYGkDLSIYA---LEDYTRIKHVMV 450
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
24-478 |
1.34e-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: 1.34e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 24 VTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDV 103
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 104 WRGIEVVEHAANVASLMMGETVENVAREIDTASWI---QPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDP 180
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARvrrEPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 181 LTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLT-HPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILP 259
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAaHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 260 DANKAQVLGNLVGASCGAAGQRCMAISAA-VFVGAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAE 338
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLlVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 339 GKAEGAECLLDGSqcQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRS 418
Cdd:cd07110 321 GKEEGARLLCGGR--RPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595944 419 GGAARRYQHAVQVGQVGINVPIPVpLPFFSFTGWKGSFYG-DLHAYGKQAvrfYTETKTVT 478
Cdd:cd07110 399 AERCDRVAEALEAGIVWINCSQPC-FPQAPWGGYKRSGIGrELGEWGLDN---YLEVKQIT 455
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
43-478 |
1.42e-84 |
|
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: 267.52 E-value: 1.42e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 43 EIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVWRGIEVVEHAANVASLMMG 122
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 123 ETVEnvAREIDTASWI--QPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVL 200
Cdd:cd07105 81 GSIP--SDKPGTLAMVvkEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 201 QVIHGGREQ----VDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDAN-KAQVLGNLVGASC 275
Cdd:cd07105 159 NVVTHSPEDapevVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADlDAAANAALFGAFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 276 gAAGQRCMAiSAAVFV--GAAREWIPELAERMAVLRPGhwqdpDAAYGPLISPQARQRVLRLIAEGKAEGAEcLLDGSQc 353
Cdd:cd07105 239 -NSGQICMS-TERIIVheSIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAK-LVVGGL- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 354 qVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQ 433
Cdd:cd07105 310 -ADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 15595944 434 VGINVPIPVPLPFFSFTGWKGSFYGDLHayGKQAVRFYTETKTVT 478
Cdd:cd07105 389 VHINGMTVHDEPTLPHGGVKSSGYGRFN--GKWGIDEFTETKWIT 431
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
3-437 |
3.28e-81 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 261.41 E-value: 3.28e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 3 KAIPQLIDGEWrgSRSRELVEVTDPA-TQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHH 81
Cdd:PRK03137 35 QDYPLIIGGER--ITTEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 82 DELGELLARETGKNLADAKGDVWRGIEVVEHAANVA-SLMMGETVENVAREIDTASWIqPLGVCAGITPFNFPAMIPLWM 160
Cdd:PRK03137 113 HEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMlKLADGKPVESRPGEHNRYFYI-PLGVGVVISPWNFPFAIMAGM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 161 FPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVY---- 235
Cdd:PRK03137 192 TLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGsGSEVGDYLVDHPKTRFITFTGSREVGLRIYeraa 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 236 --RTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAAVFVGAAR----EWIPELAERMAVLR 309
Cdd:PRK03137 272 kvQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYdevlEKVVELTKELTVGN 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 310 PGHwqdpDAAYGPLISPQARQRVLRLIAEGKAEGaECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLA 389
Cdd:PRK03137 352 PED----NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGY----FIQPTIFADVDPKARIMQEEIFGPVVA 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15595944 390 CLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGIN 437
Cdd:PRK03137 423 FIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN 470
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
7-481 |
7.12e-81 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 259.46 E-value: 7.12e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 7 QLIDGEWRGSrSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGE 86
Cdd:PRK13473 5 LLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 87 LLARETGKNLADAKGD-VWRGIEVVEHAANVASLMMGE-TVENVAreiDTASWIQ--PLGVCAGITPFNFPAMIPLWMFP 162
Cdd:PRK13473 84 LESLNCGKPLHLALNDeIPAIVDVFRFFAGAARCLEGKaAGEYLE---GHTSMIRrdPVGVVASIAPWNYPLMMAAWKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 163 LAIACGNTFVLKPSEQDPLTPNRLAELFLEAgAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAH 241
Cdd:PRK13473 161 PALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGrGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 242 LKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCmaiSAAVFVGAAR----EWIPELAERMAVLRPGHWQDPD 317
Cdd:PRK13473 240 VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDC---TAACRIYAQRgiydDLVAKLAAAVATLKVGDPDDED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 318 AAYGPLISPQARQRVLRLIAEGKAEG-AECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESL 396
Cdd:PRK13473 317 TELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGY----YYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 397 EEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPV--PLPffsFTGWKGSFYG-DLHAYGkqaVRFYTE 473
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLvsEMP---HGGQKQSGYGkDMSLYG---LEDYTV 466
|
....*...
gi 15595944 474 TKTVTSRW 481
Cdd:PRK13473 467 VRHVMVKH 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
8-475 |
7.62e-81 |
|
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: 259.58 E-value: 7.62e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGEL 87
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 88 LARETGKNLADAkgdvwRGIEV---VEHAANVASLMMGEtvENVAREID--TASWI--QPLGVCAGITPFNFPAMIPLWM 160
Cdd:cd07559 84 ETLDNGKPIRET-----LAADIplaIDHFRYFAGVIRAQ--EGSLSEIDedTLSYHfhEPLGVVGQIIPWNFPLLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 161 FPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAgAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGT 239
Cdd:cd07559 157 LAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGfGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 240 AHLKRVQAFAGAKNHMVILPDANKAQ--VLGNLVGASCGAA---GQRCMAISAAvFV--GAAREWIPELAERMAVLRPGH 312
Cdd:cd07559 236 ENLIPVTLELGGKSPNIFFDDAMDADddFDDKAEEGQLGFAfnqGEVCTCPSRA-LVqeSIYDEFIERAVERFEAIKVGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 313 WQDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLE 392
Cdd:cd07559 315 PLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVIT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 393 VESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINV--PIPVPLPffsFTGWKGSFYG-DLHaygKQAVR 469
Cdd:cd07559 395 FKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCyhQYPAHAP---FGGYKKSGIGrETH---KMMLD 468
|
....*.
gi 15595944 470 FYTETK 475
Cdd:cd07559 469 HYQQTK 474
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
9-437 |
6.38e-80 |
|
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: 257.32 E-value: 6.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELL 88
Cdd:cd07111 26 INGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 89 ARETGKNLADAK-GDVWRGIEVVEHAANVASLMmgetvenvarEIDTASWiQPLGVCAGITPFNFPAMIPLWMFPLAIAC 167
Cdd:cd07111 106 SLDNGKPIRESRdCDIPLVARHFYHHAGWAQLL----------DTELAGW-KPVGVVGQIVPWNFPLLMLAWKICPALAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 168 GNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQA 247
Cdd:cd07111 175 GNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 248 FAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISA-AVFVGAAREWIPELAERMAVLRPGHWQDPDAAYGPLISP 326
Cdd:cd07111 255 ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRlLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 327 QARQRVLRLIAEGKAEGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNAN 406
Cdd:cd07111 335 AQLKRIRELVEEGRAEGADVFQPGADLPSKGP----FYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNT 410
|
410 420 430
....*....|....*....|....*....|.
gi 15595944 407 PYGNGTSLFTRSGGAARRYQHAVQVGQVGIN 437
Cdd:cd07111 411 PYGLAASVWSENLSLALEVALSLKAGVVWIN 441
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
44-477 |
3.30e-79 |
|
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: 253.54 E-value: 3.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 44 IEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVWRGIEVVEH-AANVASLMMG 122
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 123 ETVENVAREidtaSWI--QPLGVCAGITPFNFPamipLW-MF----PlAIACGNTFVLKPSEQDPLTPNRLAELFLEAGA 195
Cdd:cd07100 81 EPIETDAGK----AYVryEPLGVVLGIMPWNFP----FWqVFrfaaP-NLMAGNTVLLKHASNVPGCALAIEELFREAGF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 196 PKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASC 275
Cdd:cd07100 152 PEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 276 GAAGQRCmaISAAVFV---GAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQ 352
Cdd:cd07100 232 QNAGQSC--IAAKRFIvheDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 353 cqVEGypNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVG 432
Cdd:cd07100 310 --PDG--PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 15595944 433 QVGINVPIpVPLPFFSFTGWKGSFYG-DLHAYGkqaVRFYTETKTV 477
Cdd:cd07100 386 MVFINGMV-KSDPRLPFGGVKRSGYGrELGRFG---IREFVNIKTV 427
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
9-477 |
6.13e-79 |
|
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: 254.76 E-value: 6.13e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFET-W-REVPAPERARLMLRYQHLLKEHHDELGE 86
Cdd:cd07143 11 INGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWgLKVSGSKRGRCLSKLADLMERNLDYLAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 87 LLARETGKN-LADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIdTASWIQPLGVCAGITPFNFPAMIPLWMFPLAI 165
Cdd:cd07143 91 IEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKL-TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 166 ACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGT-AHLK 243
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGyGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAkSNLK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 244 RVQAFAGAKNHMVILPDANKAQVlgnLVGASCGA---AGQRCMAISaAVFV--GAAREWIPELAERMAVLRPGHWQDPDA 318
Cdd:cd07143 250 KVTLELGGKSPNIVFDDADLESA---VVWTAYGIffnHGQVCCAGS-RIYVqeGIYDKFVKRFKEKAKKLKVGDPFAEDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 319 AYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEE 398
Cdd:cd07143 326 FQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY----FIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 399 AIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGIN----VPIPVPlpffsFTGWKGSFYGdlHAYGKQAVRFYTET 474
Cdd:cd07143 402 AIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcynlLHHQVP-----FGGYKQSGIG--RELGEYALENYTQI 474
|
...
gi 15595944 475 KTV 477
Cdd:cd07143 475 KAV 477
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
31-437 |
1.45e-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: 252.60 E-value: 1.45e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 31 DVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVWRGIEVV 110
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 111 EHAANVASLMMGETVENVAREIDTAsWIQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRL-AEL 189
Cdd:cd07152 82 HEAAGLPTQPQGEILPSAPGRLSLA-RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVViARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 190 FLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAqvlgn 269
Cdd:cd07152 161 FEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLD----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 270 lVGASCGAA------GQRCMAiSAAVFV--GAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGKA 341
Cdd:cd07152 236 -LAASNGAWgaflhqGQICMA-AGRHLVheSVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 342 EGAECLLDGSQcqvegypNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSGGA 421
Cdd:cd07152 314 AGARLEAGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGR 386
|
410
....*....|....*.
gi 15595944 422 ARRYQHAVQVGQVGIN 437
Cdd:cd07152 387 AMALADRLRTGMLHIN 402
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
9-478 |
3.04e-78 |
|
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: 252.65 E-value: 3.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFE---TWREVPAPERARLMLRYQHLLKEHHDELG 85
Cdd:cd07141 11 INNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 86 ELLARETGKNLADAK-GDVWRGIEVVEHAANVASLMMGETVEnVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLA 164
Cdd:cd07141 91 SLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTIP-MDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 165 IACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYR-TGTAHL 242
Cdd:cd07141 170 LACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQaAGKSNL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 243 KRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISaAVFV--GAAREWIPELAERMAVLRPGHWQDPDAAY 320
Cdd:cd07141 250 KRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGS-RTFVqeSIYDEFVKRSVERAKKRVVGNPFDPKTEQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 321 GPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAI 400
Cdd:cd07141 329 GPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595944 401 ALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPlPFFSFTGWKGSFYG-DLHAYGKQAvrfYTETKTVT 478
Cdd:cd07141 405 ERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGrELGEYGLQE---YTEVKTVT 479
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
23-478 |
2.18e-77 |
|
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: 249.58 E-value: 2.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 23 EVTDPATQDVLALAPKATADEIEQAIASA--QRAFETwrevpAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAK 100
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALAasYRSTLT-----RYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 101 GDVWRGIEVVEHAANVASLMMGETVE------NVAREIDTASwiQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLK 174
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFScdltanGKARKIFTLR--EPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 175 PSEQDPLTPNRLAELFLEAGAPKGVLQVIHGG-REQVDALLTHPDIRAISFVGSVAVGQHVyrTGTAHLKRVQAFAGAKN 253
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 254 HMVILPDAN--KAQVLGnlVGASCGAAGQRCMAISAaVFVGA--AREWIPELAERMAVLRPGHWQDPDAAYGPLISPQAR 329
Cdd:cd07146 233 PLIVMDDADleRAATLA--VAGSYANSGQRCTAVKR-ILVHEsvADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 330 QRVLRLIAEGKAEGAECLLDGSQcqvegypNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYG 409
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYG 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595944 410 NGTSLFTRSGGAARRYQHAVQVGQVGINvpiPVP---LPFFSFTGWKGSFYGdlhayGKQ----AVRFYTETKTVT 478
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVN---EVPgfrSELSPFGGVKDSGLG-----GKEgvreAMKEMTNVKTYS 450
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
26-478 |
1.02e-76 |
|
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: 248.03 E-value: 1.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 26 DPATQDVLALAPKATADEIEQAIASAQRAFE--TWREVPApERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDV 103
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 104 WRGIEVVEHAANVASLMMGETVENVAREIDTASWiQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTP 183
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPEPGSFSLVLR-EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 184 NRLAELFLEA-GAPKGVLQVIHGGREQVDALL-THPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDA 261
Cdd:cd07120 161 AAIIRILAEIpSLPAGVVNLFTESGSEGAAHLvASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 262 NKAQVLGNLVGASCGAAGQRCMAISAA-VFVGAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGK 340
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSRVlVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 341 AEGAECLLDGSQCqVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLAcLEVESLE-EAIALVNANPYGNGTSLFTRSG 419
Cdd:cd07120 321 AAGAEVVLRGGPV-TEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLT-LETFDDEaEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15595944 420 GAARRYQHAVQVGQVGINVPIPVpLPFFSFTGWKGSFYGDLHayGKQAVRFYTETKTVT 478
Cdd:cd07120 399 ARAMRVARAIRAGTVWINDWNKL-FAEAEEGGYRQSGLGRLH--GVAALEDFIEYKHIY 454
|
|
| lactal_redase_Meth |
NF040648 |
lactaldehyde dehydrogenase; |
8-477 |
2.38e-76 |
|
lactaldehyde dehydrogenase;
Pssm-ID: 468615 [Multi-domain] Cd Length: 463 Bit Score: 247.21 E-value: 2.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRgsrSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGEL 87
Cdd:NF040648 2 FINGKWI---DREDIDVINPYNLEVIDKIPSLSREEVKEAIEIANEAKEVMKNLSPRKRYNILMDIAEELKKNKEELAKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 88 LARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIDTASwiQPLGVCAGITPFNFPAMIPLWMFPLAIAC 167
Cdd:NF040648 79 ITIDAGKPIKQSIIEVDRSIETFKLAAFYAKEIRGETIPSDAGLIFTKK--EPLGVVGAITPFNYPLNLAAHKIAPAIAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 168 GNTFVLKPSEQDPLTPNRLAEL----FLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVyrTGTAHL 242
Cdd:NF040648 157 GNSVVLHPSSKAPLAAIELAKIiekvLKKMNIPLGVFNLVTGYGEVVgDEIVKNEKVNKISFTGSVEVGESI--SKKAGM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 243 KRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAIsAAVFV--GAAREWIPELAERMAVLRPGHWQDPDAAY 320
Cdd:NF040648 235 KKITLELGGNNPLIVLKDADIEKAVESAVKGSFLNSGQVCISV-GRVIVeeEIADEFIKKLVEETKKLKVGNPLDEKTDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 321 GPLISPQARQRVLRLIAEGKAEGAECLLDGSQcqvegypNGNWLGPTLFRaVTPKMGLYREEIFGPVLACLEVESLEEAI 400
Cdd:NF040648 314 GPLITEEAAIRVENLVNEAIEEGAKLLCGGNR-------EGSLFYPTVLD-VDEDNILVKVETFGPVLPIIRVKDIDEAI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 401 ALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPipvplPFFS-----FTGWKGSfygdlhAYGKQAVRF----Y 471
Cdd:NF040648 386 EIANNTKYGLQAGVFTNDINKALKFADELEYGGVIINKS-----STFRtdnmpFGGFKKS------GLGKEGIKYaveeM 454
|
....*.
gi 15595944 472 TETKTV 477
Cdd:NF040648 455 TEIKTI 460
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
8-477 |
1.63e-74 |
|
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: 242.75 E-value: 1.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGEL 87
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 88 LARETGKNLADAkgdvwRGIEV---VEHAANVASLMMGEtvENVAREID--TASWI--QPLGVCAGITPFNFPAMIPLWM 160
Cdd:cd07117 84 ETLDNGKPIRET-----RAVDIplaADHFRYFAGVIRAE--EGSANMIDedTLSIVlrEPIGVVGQIIPWNFPFLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 161 FPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAgAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGT 239
Cdd:cd07117 157 LAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGkGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 240 AHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAiSAAVFV--GAAREWIPELAERMAVLRPGHWQDPD 317
Cdd:cd07117 236 KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCA-GSRIFVqeGIYDEFVAKLKEKFENVKVGNPLDPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 318 AAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLE 397
Cdd:cd07117 315 TQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTED 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 398 EAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINV--PIPVPLPffsFTGWKGSFYG-DLHaygKQAVRFYTET 474
Cdd:cd07117 395 EVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTynQIPAGAP---FGGYKKSGIGrETH---KSMLDAYTQM 468
|
...
gi 15595944 475 KTV 477
Cdd:cd07117 469 KNI 471
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
25-478 |
3.66e-74 |
|
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: 241.36 E-value: 3.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 25 TDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVW 104
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 105 RGIEVVEHAA-NVASLMMGETVENVAREIDTASWIQ--PLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPL 181
Cdd:cd07099 81 LALEAIDWAArNAPRVLAPRKVPTGLLMPNKKATVEyrPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 182 TPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPdIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDA 261
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 262 N-KAQVLGNLVGASCGaAGQRCMAISaAVFVGAAR--EWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAE 338
Cdd:cd07099 240 DlERAAAAAVWGAMVN-AGQTCISVE-RVYVHESVydEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 339 GKAEGAECLLDGSQCQVegypNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRS 418
Cdd:cd07099 318 AVAKGAKALTGGARSNG----GGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595944 419 GGAARRYQHAVQVGQVGIN-VPIPVPLPFFSFTGWKGSFYGDLHayGKQAVRFYTETKTVT 478
Cdd:cd07099 394 LARAEAIARRLEAGAVSINdVLLTAGIPALPFGGVKDSGGGRRH--GAEGLREFCRPKAIA 452
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
27-455 |
2.60e-73 |
|
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: 239.07 E-value: 2.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 27 PATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVWRG 106
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 107 IEVVEHAANVASLMMGETV--------ENVAREidtaswiqPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQ 178
Cdd:cd07102 83 LERARYMISIAEEALADIRvpekdgfeRYIRRE--------PLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 179 DPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVIL 258
Cdd:cd07102 155 TPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 259 PDANKAQVLGNLVGASCGAAGQRCMAISaAVFVGAA--REWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLI 336
Cdd:cd07102 235 PDADLDAAAESLVDGAFFNSGQSCCSIE-RIYVHESiyDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 337 AEGKAEGAECLLDGSQCQvEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFT 416
Cdd:cd07102 314 ADAIAKGARALIDGALFP-EDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWT 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 15595944 417 RSGGAARRYQHAVQVGQVGINvPIPVPLPFFSFTGWKGS 455
Cdd:cd07102 393 KDIARAEALGEQLETGTVFMN-RCDYLDPALAWTGVKDS 430
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
22-439 |
6.08e-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: 237.91 E-value: 6.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 22 VEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKG 101
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 102 DVWRGIEVVEHAANVASLMMGETV--ENVAREIDTASWIQ--PLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSE 177
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLplDISARGEGRQGLVRrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 178 QDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVyrTGTAHLKRVQAFAGAKNHMVI 257
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDL--KARAGKKKVVLELGGNAAVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 258 LPDANKAQVLGNLVGASCGAAGQRCMAISaAVFVGAAR--EWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRL 335
Cdd:cd07147 239 DSDADLDFAAQRIIFGAFYQAGQSCISVQ-RVLVHRSVydEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 336 IAEGKAEGAECLLDGSQcqvegypNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLF 415
Cdd:cd07147 318 VNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420
....*....|....*....|....*
gi 15595944 416 TRSGGAARRYQHAVQVGQVGIN-VP 439
Cdd:cd07147 391 TRDLEKALRAWDELEVGGVVINdVP 415
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
10-439 |
4.07e-70 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 231.33 E-value: 4.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 10 DGEWRGSRsrELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLA 89
Cdd:cd07130 4 DGEWGGGG--GVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 90 RETGKNLADAKGDVWRGIEVVEHAANVASLMMGETvenVARE------IDTasWiQPLGVCAGITPFNFPAMIPLWMFPL 163
Cdd:cd07130 82 LEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLT---IPSErpghrmMEQ--W-NPLGVVGVITAFNFPVAVWGWNAAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 164 AIACGNTFVLKPSEQDPLTP----NRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGT 239
Cdd:cd07130 156 ALVCGNVVVWKPSPTTPLTAiavtKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 240 AHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMaisaavfvgAAREWI------PELAERM----AVLR 309
Cdd:cd07130 236 ARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCT---------TTRRLIvhesiyDEVLERLkkayKQVR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 310 PGHWQDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSqcQVEGypNGNWLGPTLFRAvTPKMGLYREEIFGPVLA 389
Cdd:cd07130 307 IGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGK--VIDG--PGNYVEPTIVEG-LSDAPIVKEETFAPILY 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15595944 390 CLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAV--QVGQVGINVP 439
Cdd:cd07130 382 VLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIG 433
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
9-477 |
8.79e-69 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 228.63 E-value: 8.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFET--WREVPAPERARLMLRYQHLLKEHHDELGE 86
Cdd:PRK09847 24 INGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 87 LLARETGKNLADA-KGDVWRGIEVVEHAANVASLMMGETVENVAREIDTASWiQPLGVCAGITPFNFPAMIPLWMFPLAI 165
Cdd:PRK09847 104 LETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVR-EPVGVIAAIVPWNFPLLLTCWKLGPAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 166 ACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYR-TGTAHLK 243
Cdd:PRK09847 183 AAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKdAGDSNMK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 244 RVQAFAGAKNHMVIL---PDANKAqvlgnlvgASCGAA------GQRCMAISAAVFVGA-AREWIPELAERMAVLRPGHW 313
Cdd:PRK09847 263 RVWLEAGGKSANIVFadcPDLQQA--------ASATAAgifynqGQVCIAGTRLLLEESiADEFLALLKQQAQNWQPGHP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 314 QDPDAAYGPLISPQARQRVLRLIAEGKAEGaECLLDGSQcqvEGYPNGnwLGPTLFRAVTPKMGLYREEIFGPVLACLEV 393
Cdd:PRK09847 335 LDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRN---AGLAAA--IGPTIFVDVDPNASLSREEIFGPVLVVTRF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 394 ESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINV----PIPVPlpffsFTGWKGSFYG---DLHAYGKq 466
Cdd:PRK09847 409 TSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMTVP-----FGGYKQSGNGrdkSLHALEK- 482
|
490
....*....|.
gi 15595944 467 avrfYTETKTV 477
Cdd:PRK09847 483 ----FTELKTI 489
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
8-477 |
4.83e-68 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 225.84 E-value: 4.83e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFE--TWREVPAPERARLMLRYQHLLKEHHDELG 85
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 86 ELLARETGKNLADAK-GDVWRGIEVVEHAANVASLMMGETVE-NVAREIDTASwiQPLGVCAGITPFNFPAMIPLWMFPL 163
Cdd:cd07142 87 ALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPaDGPHHVYTLH--EPIGVVGQIIPWNFPLLMFAWKVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 164 AIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTA-H 241
Cdd:cd07142 165 ALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 242 LKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAiSAAVFV--GAAREWIPELAERMAVLRPGHWQDPDAA 319
Cdd:cd07142 245 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCA-GSRTFVheSIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 320 YGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEA 399
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGY----YIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 400 IALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGIN------VPIPvplpffsFTGWKGSFYGdlHAYGKQAVRFYTE 473
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcydvfdASIP-------FGGYKMSGIG--REKGIYALNNYLQ 470
|
....
gi 15595944 474 TKTV 477
Cdd:cd07142 471 VKAV 474
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
9-477 |
6.35e-68 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 226.24 E-value: 6.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFE--TWREVPAPERARLMLRYQHLLKEHHDELGE 86
Cdd:PLN02766 25 INGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 87 LLARETGKNLADAKG-DVWRGIEVVEHAANVASLMMGETVEnVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLAI 165
Cdd:PLN02766 105 LDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLK-MSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 166 ACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRT-GTAHLK 243
Cdd:PLN02766 184 AAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAaATSNLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 244 RVQAFAGAKNHMVILPDA--NKAQVLGNLvgASCGAAGQRCMAiSAAVFV--GAAREWIPELAERMAVLRPGHWQDPDAA 319
Cdd:PLN02766 264 QVSLELGGKSPLLIFDDAdvDMAVDLALL--GIFYNKGEICVA-SSRVYVqeGIYDEFVKKLVEKAKDWVVGDPFDPRAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 320 YGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEA 399
Cdd:PLN02766 341 QGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGY----YIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595944 400 IALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPlPFFSFTGWKGSFYGdlHAYGKQAVRFYTETKTV 477
Cdd:PLN02766 417 IKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFD-PDCPFGGYKMSGFG--RDQGMDALDKYLQVKSV 491
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
3-440 |
1.08e-66 |
|
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: 223.61 E-value: 1.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 3 KAIPQLIDGEwrgSRSRELVEVTDPATQD-VLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHH 81
Cdd:cd07125 32 EAIPIINGEE---TETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 82 DELGELLARETGKNLADAKGDVWRGIEVVE-HAANVASLMMGETVENVAREIDTASWiQPLGVCAGITPFNFPAMIPLWM 160
Cdd:cd07125 109 GELIALAAAEAGKTLADADAEVREAIDFCRyYAAQARELFSDPELPGPTGELNGLEL-HGRGVFVCISPWNFPLAIFTGQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 161 FPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRT-- 237
Cdd:cd07125 188 IAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAKLINRAla 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 238 ----GTAHLkrvQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAAVFVG-AAREWIPELAERMAVLRPGH 312
Cdd:cd07125 268 erdgPILPL---IAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEeIAERFIEMLKGAMASLKVGD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 313 WQDPDAAYGPLISPQARQRVLRLIAEGKAEG---AECLLDGSqcqvegypNGNWLGPTLFRAVTPkmGLYREEIFGPVL- 388
Cdd:cd07125 345 PWDLSTDVGPLIDKPAGKLLRAHTELMRGEAwliAPAPLDDG--------NGYFVAPGIIEIVGI--FDLTTEVFGPILh 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15595944 389 -ACLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPI 440
Cdd:cd07125 415 vIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNI 467
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
8-440 |
1.42e-66 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 222.47 E-value: 1.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGEL 87
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 88 LARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFP-AMIPLWMFPlAIA 166
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPaAMITRKAGP-ALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 167 CGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLT-HPDIRAISFVGSVAVGQHVYRTGTAHLKRV 245
Cdd:PRK11241 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTsNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 246 QAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCM-AISAAVFVGAAREWIPELAERMAVLRPGHWQDPDAAYGPLI 324
Cdd:PRK11241 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVcANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 325 SPQARQRVLRLIAEGKAEGAECLLDGSQCQVEgypnGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVN 404
Cdd:PRK11241 333 DEKAVAKVEEHIADALEKGARVVCGGKAHELG----GNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430
....*....|....*....|....*....|....*.
gi 15595944 405 ANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPI 440
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI 444
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
43-446 |
5.23e-65 |
|
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: 216.75 E-value: 5.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 43 EIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVWRGIEVVEHAANVASLMMG 122
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 123 EtvenvaREIDTAS-----WIQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPK 197
Cdd:cd07095 81 E------RATPMAQgravlRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 198 GVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFA-GAKNHMVILPDANKAQVLGNLVGASCG 276
Cdd:cd07095 155 GVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEmGGNNPLVVWDVADIDAAAYLIVQSAFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 277 AAGQRCMAISAAVFVG--AAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQ 354
Cdd:cd07095 235 TAGQRCTCARRLIVPDgaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 355 VegypNGNWLGPTLFRaVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQV 434
Cdd:cd07095 315 A----GTAFLSPGIID-VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIV 389
|
410
....*....|....*
gi 15595944 435 GINVPI---PVPLPF 446
Cdd:cd07095 390 NWNRPTtgaSSTAPF 404
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
25-477 |
6.89e-65 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 217.30 E-value: 6.89e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 25 TDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVW 104
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 105 RGIEVVEHAANVASLMMGETVENVAREIDTASWI--QPLGVCAGITPFNFPamipLWMF-----PlAIACGNTFVLKPSE 177
Cdd:PRK09406 86 KCAKGFRYYAEHAEALLADEPADAAAVGASRAYVryQPLGVVLAVMPWNFP----LWQVvrfaaP-ALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 178 QDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVI 257
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 258 LPDANKAQVLGNLVGASCGAAGQRCmaISAAVFVGAA---REWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLR 334
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSC--IAAKRFIVHAdvyDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 335 LIAEGKAEGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSL 414
Cdd:PRK09406 319 QVDDAVAAGATILCGGKRPDGPGW----FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595944 415 FTRSGGAARRYQHAVQVGQVGINvPIPVPLPFFSFTGWKGSFYG-DLHAYGkqaVRFYTETKTV 477
Cdd:PRK09406 395 WTRDEAEQERFIDDLEAGQVFIN-GMTVSYPELPFGGVKRSGYGrELSAHG---IREFCNIKTV 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
3-480 |
8.19e-65 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 218.22 E-value: 8.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 3 KAIPQLIDGEWRGSRSRElVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHD 82
Cdd:cd07083 17 RAYPLVIGGEWVDTKERM-VSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 83 ELGELLARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIDT-ASWIQPLGVCAGITPFNFPAMIPLWMF 161
Cdd:cd07083 96 ELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDnESFYVGLGAGVVISPWNFPVAIFTGMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 162 PLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTA 240
Cdd:cd07083 176 VAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAAR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 241 HLKRVQAF------AGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAAVFV-GAAREWIPELAERMAVLRPGHW 313
Cdd:cd07083 256 LAPGQTWFkrlyveTGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTqGAYEPVLERLLKRAERLSVGPP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 314 QDPDAAYGPLISPQARQRVLRLIAEGKAEGAecLLDGSQCqVEGypNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEV 393
Cdd:cd07083 336 EENGTDLGPVIDAEQEAKVLSYIEHGKNEGQ--LVLGGKR-LEG--EGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 394 ES--LEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPL----PffsFTGWKGSFYGDlHAYGKQA 467
Cdd:cd07083 411 KDddFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALvgvqP---FGGFKLSGTNA-KTGGPHY 486
|
490
....*....|...
gi 15595944 468 VRFYTETKTVTSR 480
Cdd:cd07083 487 LRRFLEMKAVAER 499
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
1-486 |
8.80e-64 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 215.37 E-value: 8.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 1 MAKAIP---QLIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFET-----WREVPAPERARLMLR 72
Cdd:PLN02467 1 MAIPVPrrqLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 73 YQHLLKEHHDELGELLARETGKNLADAKGDVWRGIEVVEHAANVA-----------SLMMGETVENVAREidtaswiqPL 141
Cdd:PLN02467 81 IAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAealdakqkapvSLPMETFKGYVLKE--------PL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 142 GVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIR 220
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGlGTEAGAPLASHPGVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 221 AISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDAN--KAqVLGNLVGASCgAAGQRCMAISaAVFV--GAARE 296
Cdd:PLN02467 233 KIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDldKA-VEWAMFGCFW-TNGQICSATS-RLLVheRIASE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 297 WIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGsqCQVEGYPNGNWLGPTLFRAVTPKM 376
Cdd:PLN02467 310 FLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGG--KRPEHLKKGFFIEPTIITDVTTSM 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 377 GLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVplpfFSFTGWKG-- 454
Cdd:PLN02467 388 QIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPC----FCQAPWGGik 463
|
490 500 510
....*....|....*....|....*....|....
gi 15595944 455 -SFYG-DLHAYGKQAvrfYTETKTVTsRWFDDEP 486
Cdd:PLN02467 464 rSGFGrELGEWGLEN---YLSVKQVT-KYISDEP 493
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
25-479 |
1.58e-63 |
|
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: 213.32 E-value: 1.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 25 TDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVW 104
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 105 RGIEVVEHAANVA-SLM-----------MGETVENVareidtaswiQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFV 172
Cdd:cd07101 81 DVAIVARYYARRAeRLLkprrrrgaipvLTRTTVNR----------RPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 173 LKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIraISFVGSVAVGQHVYRTGTAHLKRVQAFAGA 251
Cdd:cd07101 151 LKPDSQTALTALWAVELLIEAGLPRDLWQVVTGpGSEVGGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 252 KNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAaVFVGAAR--EWIPELAERMAVLRPGHWQDPDAAYGPLISPQAR 329
Cdd:cd07101 229 KNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIER-IYVHESVydEFVRRFVARTRALRLGAALDYGPDMGSLISQAQL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 330 QRVLRLIAEGKAEGAECLLDGSQcqvegYPNgnwLGP-----TLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVN 404
Cdd:cd07101 308 DRVTAHVDDAVAKGATVLAGGRA-----RPD---LGPyfyepTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELAN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 405 ANPYGNGTSLFTRSGGAARRYQHAVQVGQVGIN-------VPIPVPLpffsfTGWKGSFYGDLHayGKQAVRFYTETKTV 477
Cdd:cd07101 380 DTDYGLNASVWTRDGARGRRIAARLRAGTVNVNegyaaawASIDAPM-----GGMKDSGLGRRH--GAEGLLKYTETQTV 452
|
..
gi 15595944 478 TS 479
Cdd:cd07101 453 AV 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
7-478 |
3.94e-63 |
|
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: 213.13 E-value: 3.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 7 QLIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFET--WREVPAPERARLMLRYQHLLKEHHDEL 84
Cdd:cd07140 8 LFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 85 GELLARETGK--NLAdAKGDVWRGIEVVEHAANVASLMMGETVE-NVAREIDTASWI--QPLGVCAGITPFNFPAMIPLW 159
Cdd:cd07140 88 ATIESLDSGAvyTLA-LKTHVGMSIQTFRYFAGWCDKIQGKTIPiNQARPNRNLTLTkrEPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 160 MFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRT- 237
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGsGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSc 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 238 GTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAiSAAVFVGAA--REWIPELAERMAVLRPGHWQD 315
Cdd:cd07140 247 AVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA-AGRLFVEESihDEFVRRVVEEVKKMKIGDPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 316 PDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVES 395
Cdd:cd07140 326 RSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFGPIMIISKFDD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 396 --LEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINV--PIPVPLPffsFTGWKGSFYG-DLhayGKQAVRF 470
Cdd:cd07140 402 gdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTynKTDVAAP---FGGFKQSGFGkDL---GEEALNE 475
|
....*...
gi 15595944 471 YTETKTVT 478
Cdd:cd07140 476 YLKTKTVT 483
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
26-479 |
7.15e-63 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 212.16 E-value: 7.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 26 DPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMlryQHLLK---EHHDELGELLARETGKNLADAK-G 101
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVL---RSLLKyilENQEEICRVACRDTGKTMVDASlG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 102 DVWRGIE----VVEHAANV-------ASLMMGETVENVAREidtaswiqPLGVCAGITPFNFP------AMIPlwmfplA 164
Cdd:cd07098 79 EILVTCEkirwTLKHGEKAlrpesrpGGLLMFYKRARVEYE--------PLGVVGAIVSWNYPfhnllgPIIA------A 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 165 IACGNTFVLKPSEQDPLTpnrlAELFLE--------AGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYR 236
Cdd:cd07098 145 LFAGNAIVVKVSEQVAWS----SGFFLSiireclaaCGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 237 TGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAA-VFVGAAREWIPELAERMAVLRPGHWQD 315
Cdd:cd07098 221 AAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERViVHEKIYDKLLEILTDRVQALRQGPPLD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 316 PDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVES 395
Cdd:cd07098 301 GDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 396 LEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGIN----VPIPVPLPffsFTGWKGSFYGDLHayGKQAVRFY 471
Cdd:cd07098 381 DEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfgvNYYVQQLP---FGGVKGSGFGRFA--GEEGLRGL 455
|
....*...
gi 15595944 472 TETKTVTS 479
Cdd:cd07098 456 CNPKSVTE 463
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
8-458 |
1.07e-60 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 206.92 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGEL 87
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 88 LARETGKNLADAKGDVWRGIEVVEHAANVASLMMGET--------VENVAREIDTASWIqPLGVCAGITPFNFPAMIPLW 159
Cdd:PLN00412 99 LVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEGkflvsdsfPGNERNKYCLTSKI-PLGVVLAIPPFNYPVNLAVS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 160 MFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSvavgqhvyRTG 238
Cdd:PLN00412 178 KIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGkGSEIGDFLTMHPGVNCISFTGG--------DTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 239 TAHLKR-----VQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISA-AVFVGAAREWIPELAERMAVLRPGH 312
Cdd:PLN00412 250 IAISKKagmvpLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVvLVMESVADALVEKVNAKVAKLTVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 313 WQDpDAAYGPLISPQARQRVLRLIAEGKAEGAeclldgSQCQvEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLE 392
Cdd:PLN00412 330 PED-DCDITPVVSESSANFIEGLVMDAKEKGA------TFCQ-EWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIR 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595944 393 VESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPiPVPLP-FFSFTGWKGSFYG 458
Cdd:PLN00412 402 INSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA-PARGPdHFPFQGLKDSGIG 467
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
16-482 |
2.73e-60 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 206.65 E-value: 2.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 16 SRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKN 95
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 96 LADAkgdvwrgIEVVEHAANVASL-------------------MMGETVENVareidtaswiQPLGVCAGITPFNFPA-- 154
Cdd:PRK09407 108 RRHA-------FEEVLDVALTARYyarrapkllaprrragalpVLTKTTELR----------QPKGVVGVISPWNYPLtl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 155 ----MIPlwmfplAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIraISFVGSVA 229
Cdd:PRK09407 171 avsdAIP------ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGpGPVVGTALVDNADY--LMFTGSTA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 230 VGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAaVFVGAAR--EWIPELAERMAV 307
Cdd:PRK09407 243 TGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIER-IYVHESIydEFVRAFVAAVRA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 308 LRPGHWQDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSqcqveGYPNgnwLG-----PTLFRAVTPKMGLYREE 382
Cdd:PRK09407 322 MRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGK-----ARPD---LGplfyePTVLTGVTPDMELAREE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 383 IFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVP-------IPVPLpffsfTGWKGS 455
Cdd:PRK09407 394 TFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGyaaawgsVDAPM-----GGMKDS 468
|
490 500
....*....|....*....|....*...
gi 15595944 456 FYGDLHayGKQAVRFYTETKTV-TSRWF 482
Cdd:PRK09407 469 GLGRRH--GAEGLLKYTESQTIaTQRVL 494
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
8-479 |
2.10e-57 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 199.26 E-value: 2.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFET--WREVPAPERARLMLRYQHLLKEHHDELG 85
Cdd:PLN02466 61 LINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 86 ELLARETGKNLAD-AKGDVWRGIEVVEHAANVASLMMGETVENvareiDTASWIQ----PLGVCAGITPFNFPAMIPLWM 160
Cdd:PLN02466 141 ALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHGLTVPA-----DGPHHVQtlhePIGVAGQIIPWNFPLLMFAWK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 161 FPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGT 239
Cdd:PLN02466 216 VGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 240 -AHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAAVFVGAAREWIPELAERMAVLRPghWQDP-- 316
Cdd:PLN02466 296 kSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRV--VGDPfk 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 317 -DAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVES 395
Cdd:PLN02466 374 kGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 396 LEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGIN------VPIPvplpffsFTGWKGSFYGdlHAYGKQAVR 469
Cdd:PLN02466 450 LDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfdAAIP-------FGGYKMSGIG--REKGIYSLN 520
|
490
....*....|
gi 15595944 470 FYTETKTVTS 479
Cdd:PLN02466 521 NYLQVKAVVT 530
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
7-480 |
6.64e-56 |
|
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: 193.83 E-value: 6.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 7 QLIDGEWRGSRSRELvEVTDPATQDVLALAPKATADEIEQAIASAQRAFET--W-REVPApeRARLMLRYQHLLKEHHDE 83
Cdd:TIGR04284 3 LLIDGKLVAGSAGTF-PTVNPATEEVLGVAADATAADMDAAIAAARRAFDEtdWsRDTAL--RVRCLRQLRDALRAHVEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 84 LGELLARETGKNLADAKGDVWRG-IEVVEHAAN------------VASLMMGETVENVAREidtaswiqPLGVCAGITPF 150
Cdd:TIGR04284 80 LRELTIAEVGAPRMLTAGAQLEGpVDDLGFAADlaesyawttdlgVASPMGIPTRRTLRRE--------AVGVVGAITPW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 151 NFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLE-AGAPKGVLQVIHGGREQVDALL-THPDIRAISFVGSV 228
Cdd:TIGR04284 152 NFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIAEhTDFPPGVVNIVTSSDHRLGALLaKDPRVDMVSFTGST 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 229 AVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCmAISAAVFVGAAR--EWIPELAERMA 306
Cdd:TIGR04284 232 ATGRAVMADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGC-AITTRLVVPRARydEAVAAAAATMG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 307 VLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQcqVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGP 386
Cdd:TIGR04284 311 SIKPGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGR--PADRDRGFFVEPTVIAGLDNNARVAREEIFGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 387 VLACLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIpvplpFFS----FTGWKGSFYGdlHA 462
Cdd:TIGR04284 389 VLTVIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGV-----WYSadapFGGYKQSGIG--RE 461
|
490
....*....|....*...
gi 15595944 463 YGKQAVRFYTETKTVTSR 480
Cdd:TIGR04284 462 MGVAGFEEYLETKLIATA 479
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
9-437 |
4.78e-55 |
|
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: 191.51 E-value: 4.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSRSRELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELL 88
Cdd:cd07116 5 IGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 89 ARETGKNLADAKG-DVwrgIEVVEHAANVASLMMGEtvENVAREIDTAS----WIQPLGVCAGITPFNFPAMIPLWMFPL 163
Cdd:cd07116 85 TWDNGKPVRETLAaDI---PLAIDHFRYFAGCIRAQ--EGSISEIDENTvayhFHEPLGVVGQIIPWNFPLLMATWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 164 AIACGNTFVLKPSEQDPLTPNRLAELFLEAgAPKGVLQVIHG-GREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHL 242
Cdd:cd07116 160 ALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 243 KRVQAFAGAKNHMVILPD---ANKAQVLGNLVGASCGA--AGQRCMAISAAVFVGAAREWIPELA-ERMAVLRPGHWQDP 316
Cdd:cd07116 239 IPVTLELGGKSPNIFFADvmdADDAFFDKALEGFVMFAlnQGEVCTCPSRALIQESIYDRFMERAlERVKAIKQGNPLDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 317 DAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAvTPKMGLYREEIFGPVLACLEVESL 396
Cdd:cd07116 319 ETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDE 397
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15595944 397 EEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGIN 437
Cdd:cd07116 398 EEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN 438
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
7-436 |
1.18e-52 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 185.16 E-value: 1.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 7 QLIDGEWRGSRSrELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGE 86
Cdd:PRK09457 3 LWINGDWIAGQG-EAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 87 LLARETGKNLADAKGDVWRGIEVV--------EHAANVASLMMGETVenVAREidtaswiQPLGVCAGITPFNFPAMIPL 158
Cdd:PRK09457 82 VIARETGKPLWEAATEVTAMINKIaisiqayhERTGEKRSEMADGAA--VLRH-------RPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 159 WMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTG 238
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 239 TAHLKRVQAFA-GAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAiSAAVFV--GA-AREWIPELAERMAVLRPGHW- 313
Cdd:PRK09457 233 AGQPEKILALEmGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTC-ARRLLVpqGAqGDAFLARLVAVAKRLTVGRWd 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 314 QDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQvegyPNGNWLGPTLFRaVTPKMGLYREEIFGPVLACLEV 393
Cdd:PRK09457 312 AEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQ----AGTGLLTPGIID-VTGVAELPDEEYFGPLLQVVRY 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15595944 394 ESLEEAIALVNANPYGNGTSLFtrsGGAARRYQHAVQVGQVGI 436
Cdd:PRK09457 387 DDFDEAIRLANNTRFGLSAGLL---SDDREDYDQFLLEIRAGI 426
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
26-437 |
1.12e-47 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 171.20 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 26 DPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVWR 105
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 106 GIEVVEHAANVASLMMGET---VENVAREIDtaswIQPLGVCAGITPFNFpamiPLWMF-----PLAIAcGNTFVLKPSE 177
Cdd:PRK13968 93 SANLCDWYAEHGPAMLKAEptlVENQQAVIE----YRPLGTILAIMPWNF----PLWQVmrgavPILLA-GNGYLLKHAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 178 QDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVI 257
Cdd:PRK13968 164 NVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 258 LPDANKAQVLGNLVGASCGAAGQRCMAisAAVFV---GAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLR 334
Cdd:PRK13968 244 LNDADLELAVKAAVAGRYQNTGQVCAA--AKRFIieeGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 335 LIAEGKAEGAECLLDGSqcQVEGypNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSL 414
Cdd:PRK13968 322 QVEATLAEGARLLLGGE--KIAG--AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATI 397
|
410 420
....*....|....*....|...
gi 15595944 415 FTRSGGAARRYQHAVQVGQVGIN 437
Cdd:PRK13968 398 FTTDETQARQMAARLECGGVFIN 420
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
77-477 |
5.73e-47 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 167.99 E-value: 5.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 77 LKEHHDELGELLARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVENVAREIDTASWIQPLGVCAGITPFNFPA-M 155
Cdd:PRK10090 8 IRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFfL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 156 IPLWMFPlAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHV 234
Cdd:PRK10090 88 IARKMAP-ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGSVSAGEKI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 235 YRTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRC-MAISAAVFVGAAREWIPELAERMAVLRPGH- 312
Cdd:PRK10090 167 MAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCnCAERVYVQKGIYDQFVNRLGEAMQAVQFGNp 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 313 WQDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLE 392
Cdd:PRK10090 247 AERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGY----YYPPTLLLDVRQEMSIMHEETFGPVLPVVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 393 VESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPLPFFSfTGWKGSFYGDlhAYGKQAVRFYT 472
Cdd:PRK10090 323 FDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH-AGWRKSGIGG--ADGKHGLHEYL 399
|
....*
gi 15595944 473 ETKTV 477
Cdd:PRK10090 400 QTQVV 404
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
9-439 |
1.51e-46 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 169.24 E-value: 1.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSRSreLVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELL 88
Cdd:PLN02315 25 VGGEWRANGP--LVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 89 ARETGKNLADAKGDVWRGIEVVEHAANVA-----SLMMGETVENVAREIdtasWiQPLGVCAGITPFNFPAMIPLWMFPL 163
Cdd:PLN02315 103 SLEMGKILAEGIGEVQEIIDMCDFAVGLSrqlngSIIPSERPNHMMMEV----W-NPLGIVGVITAFNFPCAVLGWNACI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 164 AIACGNTFVLKPSEQDPL----TPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGT 239
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLitiaMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 240 AHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAAGQRC-----MAISAAVFvgaaREWIPELAERMAVLRPGHWQ 314
Cdd:PLN02315 258 ARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCttcrrLLLHESIY----DDVLEQLLTVYKQVKIGDPL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 315 DPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQvegyPNGNWLGPTLFRaVTPKMGLYREEIFGPVLACLEVE 394
Cdd:PLN02315 334 EKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE----SEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFK 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15595944 395 SLEEAIALVNANPYGNGTSLFTRSGGAARRY--QHAVQVGQVGINVP 439
Cdd:PLN02315 409 TLEEAIEINNSVPQGLSSSIFTRNPETIFKWigPLGSDCGIVNVNIP 455
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1-437 |
2.98e-45 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 170.38 E-value: 2.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 1 MAKAIPQLIDGEWRG----SRSRELVEVTDPA-TQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQH 75
Cdd:PRK11904 539 LAAAIAAFLEKQWQAgpiiNGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAAD 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 76 LLKEHHDELGELLARETGKNLADAKGDVWRGIEVVEHAANVASLMMGETVE--------NVAReidtaswIQPLGVCAGI 147
Cdd:PRK11904 619 LLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKlpgptgesNELR-------LHGRGVFVCI 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 148 TPfnfpamiplWMFPLAI---------ACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHP 217
Cdd:PRK11904 692 SP---------WNFPLAIflgqvaaalAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGdGATVGAALTADP 762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 218 DIRAISFVGSVAVGQHVYRTGTAhlkRVQAFA------GAKNHMVI----LPDankaQVLGNLVGASCGAAGQRCmaiSA 287
Cdd:PRK11904 763 RIAGVAFTGSTETARIINRTLAA---RDGPIVpliaetGGQNAMIVdstaLPE----QVVDDVVTSAFRSAGQRC---SA 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 288 A--VFV--GAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGKAEG---AECLLDgsqcqvEGYPN 360
Cdd:PRK11904 833 LrvLFVqeDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREArllAQLPLP------AGTEN 906
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595944 361 GNWLGPTLFRavTPKMGLYREEIFGPVLACL--EVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGIN 437
Cdd:PRK11904 907 GHFVAPTAFE--IDSISQLEREVFGPILHVIryKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
24-437 |
3.25e-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: 165.47 E-value: 3.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 24 VTDPAT-QDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGD 102
Cdd:TIGR01238 55 VTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 103 VWRGIEVVEHAANVASLMMGEtvenvareiDTAswiQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLT 182
Cdd:TIGR01238 135 VREAVDFCRYYAKQVRDVLGE---------FSV---ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 183 PNRLAELFLEAGAPKGVLQVIHGGREQVDALLT-HPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAF---AGAKNHMVIL 258
Cdd:TIGR01238 203 AYRAVELMQEAGFPAGTIQLLPGRGADVGAALTsDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaeTGGQNAMIVD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 259 PDANKAQVLGNLVGASCGAAGQRCMAISA-AVFVGAAREWIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIA 337
Cdd:TIGR01238 283 STALPEQVVRDVLRSAFDSAGQRCSALRVlCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 338 EGKAEG---AECLLDGS-QCQvegypNGNWLGPTLFRavTPKMGLYREEIFGPVLACL--EVESLEEAIALVNANPYGNG 411
Cdd:TIGR01238 363 HMSQTQkkiAQLTLDDSrACQ-----HGTFVAPTLFE--LDDIAELSEEVFGPVLHVVryKARELDQIVDQINQTGYGLT 435
|
410 420
....*....|....*....|....*.
gi 15595944 412 TSLFTRSGGAARRYQHAVQVGQVGIN 437
Cdd:TIGR01238 436 MGVHSRIETTYRWIEKHARVGNCYVN 461
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
22-458 |
7.09e-45 |
|
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: 163.74 E-value: 7.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 22 VEVTDPATQDVLALAPKATADEIEQAIASAQRAFET---WreVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLAD 98
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDrnnW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 99 AKGDVWRGIEVVEHAANVASLM------MGETVENVAREIDTASwiQPLGVCAGITPFNFPA-MIPLWMFPlAIACGNTF 171
Cdd:cd07148 79 AKVEVTRAIDGVELAADELGQLggreipMGLTPASAGRIAFTTR--EPIGVVVAISAFNHPLnLIVHQVAP-AIAAGCPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 172 VLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVyRTGTAHLKRVQAFAGA 251
Cdd:cd07148 156 IVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWML-RSKLAPGTRCALEHGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 252 KNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISaAVFVGA--AREWIPELAERMAVLRPGHWQDPDAAYGPLISPQAR 329
Cdd:cd07148 235 AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQ-RVFVPAeiADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 330 QRVLRLIAEGKAEGAECLLDGSQCQVEGYpngnwlGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYG 409
Cdd:cd07148 314 DRVEEWVNEAVAAGARLLCGGKRLSDTTY------APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 15595944 410 NGTSLFTRSGGAARRYQHAVQVGQVGINVPIPVPLPFFSFTGWKGSFYG 458
Cdd:cd07148 388 FQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
8-437 |
1.74e-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: 1.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSRSRElveVTDPA-TQDVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGE 86
Cdd:COG4230 561 LIAGEAASGEARP---VRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMA 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 87 LLARETGKNLADAKGDVwRgiEVVE----HAANVASLMMGETVenvareidtaswIQPLGVCAGITPfnfpamiplWMFP 162
Cdd:COG4230 638 LLVREAGKTLPDAIAEV-R--EAVDfcryYAAQARRLFAAPTV------------LRGRGVFVCISP---------WNFP 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 163 LAI---------ACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQ 232
Cdd:COG4230 694 LAIftgqvaaalAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVgAALVADPRIAGVAFTGSTETAR 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 233 HVYRTGTAHLKRVQAF---AGAKNHMVI----LPDankaQVLGNLVGASCGAAGQRCmaiSAA--VFVGAarewipELAE 303
Cdd:COG4230 774 LINRTLAARDGPIVPLiaeTGGQNAMIVdssaLPE----QVVDDVLASAFDSAGQRC---SALrvLCVQE------DIAD 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 304 R--------MAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGKAEGAEClldgSQCQV-EGYPNGNWLGPTLFRAvtP 374
Cdd:COG4230 841 RvlemlkgaMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLV----HQLPLpEECANGTFVAPTLIEI--D 914
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595944 375 KMGLYREEIFGPVLACL--EVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGIN 437
Cdd:COG4230 915 SISDLEREVFGPVLHVVryKADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
3-409 |
1.38e-42 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 162.34 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 3 KAIPQLIDGEWRGSRsrelVEVTDPATQ-DVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHH 81
Cdd:PRK11905 554 HAAPLLAGGDVDGGT----RPVLNPADHdDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHM 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 82 DELGELLARETGKNLADAKGDVwRgiEVVE----HAANvaslmmgetvenvAREIDTASWIQPLGVCAGITPFNFPAMIP 157
Cdd:PRK11905 630 PELFALAVREAGKTLANAIAEV-R--EAVDflryYAAQ-------------ARRLLNGPGHKPLGPVVCISPWNFPLAIF 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 158 LWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLT-HPDIRAISFVGSVAVGQHVYR 236
Cdd:PRK11905 694 TGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVaDPRIAGVMFTGSTEVARLIQR 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 237 TGTAHLKR---VQAFAGAKNHMVI----LPDankaQVLGNLVGASCGAAGQRCMA---------ISAAV---FVGAarew 297
Cdd:PRK11905 774 TLAKRSGPpvpLIAETGGQNAMIVdssaLPE----QVVADVIASAFDSAGQRCSAlrvlclqedVADRVltmLKGA---- 845
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 298 ipelaerMAVLRPGhwqDPDAA---YGPLISPQARQRVLRLIAEGKAEGaeCLLdgSQCQV-EGYPNGNWLGPTLFRavT 373
Cdd:PRK11905 846 -------MDELRIG---DPWRLstdVGPVIDAEAQANIEAHIEAMRAAG--RLV--HQLPLpAETEKGTFVAPTLIE--I 909
|
410 420 430
....*....|....*....|....*....|....*...
gi 15595944 374 PKMGLYREEIFGPVL--ACLEVESLEEAIALVNANPYG 409
Cdd:PRK11905 910 DSISDLEREVFGPVLhvVRFKADELDRVIDDINATGYG 947
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
46-446 |
2.29e-40 |
|
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: 150.37 E-value: 2.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 46 QAIASAQRA-FETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAK----GDVwrgIEVVEHA-ANVASL 119
Cdd:cd07087 1 AELVARLREtFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlteiAVV---LGEIDHAlKHLKKW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 120 MMGETVENVAREIDTASWIQ--PLGVCAGITPFNFPAMipLWMFPL--AIACGNTFVLKPSEQDPLTPNRLAELFLEAgA 195
Cdd:cd07087 78 MKPRRVSVPLLLQPAKAYVIpePLGVVLIIGPWNYPLQ--LALAPLigAIAAGNTVVLKPSELAPATSALLAKLIPKY-F 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 196 PKGVLQVIHGGREQVDALLTHP-DIraISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGAS 274
Cdd:cd07087 155 DPEAVAVVEGGVEVATALLAEPfDH--IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 275 CGAAGQRCMAISAaVFV--GAAREWIPELAERMAVLRPghwQDPD--AAYGPLISPQARQRVLRLIAEGKaegaecLLDG 350
Cdd:cd07087 233 FLNAGQTCIAPDY-VLVheSIKDELIEELKKAIKEFYG---EDPKesPDYGRIINERHFDRLASLLDDGK------VVIG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 351 SQCQVEGypngNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANP-----YgngtsLFTRSGGAARRY 425
Cdd:cd07087 303 GQVDKEE----RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPkplalY-----LFSEDKAVQERV 373
|
410 420
....*....|....*....|....*
gi 15595944 426 QHAVQVGQVGIN---VPIPVP-LPF 446
Cdd:cd07087 374 LAETSSGGVCVNdvlLHAAIPnLPF 398
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
45-407 |
3.70e-36 |
|
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: 138.90 E-value: 3.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 45 EQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAK-GDVWRGIEVVEHA-ANVASLMMG 122
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlTEILPVLSEINHAiKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 123 ETVENVAREIDTASWI--QPLGVCAGITPFNFPAMipLWMFPL--AIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKG 198
Cdd:cd07134 81 KRVRTPLLLFGTKSKIryEPKGVCLIISPWNYPFN--LAFGPLvsAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 199 VlQVIHGGREQVDALLTHPdIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGAA 278
Cdd:cd07134 159 V-AVFEGDAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 279 GQRCMA-----ISAAV---FVGAAREWIpelaERMAVLRPGHWQDPDaaYGPLISPQARQRVLRLIAEGKAEGAEcLLDG 350
Cdd:cd07134 237 GQTCIApdyvfVHESVkdaFVEHLKAEI----EKFYGKDAARKASPD--LARIVNDRHFDRLKGLLDDAVAKGAK-VEFG 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15595944 351 SQCQvegyPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANP 407
Cdd:cd07134 310 GQFD----AAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKP 362
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
40-477 |
1.26e-35 |
|
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: 137.74 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 40 TADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAK-GDVWRGI-EVVEHAANVA 117
Cdd:cd07135 3 PLDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKnDILHMLKNLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 118 SLMMGETVENVAreidTASWI-------QPLGVCAGITPFNFPAMIPLWmfPL--AIACGNTFVLKPSEQDPLTPNRLAE 188
Cdd:cd07135 83 KWAKDEKVKDGP----LAFMFgkprirkEPLGVVLIIGPWNYPVLLALS--PLvgAIAAGCTVVLKPSELTPHTAALLAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 189 LfLEAGAPKGVLQVIHGGREQVDALLTHP-DirAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAQVL 267
Cdd:cd07135 157 L-VPKYLDPDAFQVVQGGVPETTALLEQKfD--KIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 268 GNLVGASCGAAGQRCMAISaavFVGAAREWIPELAERMA-VLR---PGHWQDPDAaYGPLISPQARQRVLRLIAE----- 338
Cdd:cd07135 234 KRILWGKFGNAGQICVAPD---YVLVDPSVYDEFVEELKkVLDefyPGGANASPD-YTRIVNPRHFNRLKSLLDTtkgkv 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 339 ---GKAEGAECLLDgsqcqvegypngnwlgPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLF 415
Cdd:cd07135 310 vigGEMDEATRFIP----------------PTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIF 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595944 416 -------------TRSGGAArryqhavqVGQVGINVPIPVpLPffsFTGWKGSFYGDLHayGKQAVRFYTETKTV 477
Cdd:cd07135 374 tddkseidhiltrTRSGGVV--------INDTLIHVGVDN-AP---FGGVGDSGYGAYH--GKYGFDTFTHERTV 434
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
5-417 |
2.81e-35 |
|
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: 138.10 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 5 IPQLIDG-EWRGSRSRELVEVTDPATqdVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLL--KEHH 81
Cdd:cd07123 33 IPLVIGGkEVRTGNTGKQVMPHDHAH--VLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLsgKYRY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 82 delgELLArET----GKNLADAKGDVwrGIEVVE----HAANVASLMMGETVENVAREIDTASWiQPL-GVCAGITPFNF 152
Cdd:cd07123 111 ----ELNA-ATmlgqGKNVWQAEIDA--ACELIDflrfNVKYAEELYAQQPLSSPAGVWNRLEY-RPLeGFVYAVSPFNF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 153 PAM------IPLWMfplaiacGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHG-GREQVDALLTHPDIRAISFV 225
Cdd:cd07123 183 TAIggnlagAPALM-------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGdGPVVGDTVLASPHLAGLHFT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 226 GSVAVGQHVYRTGTAHLKRVQAF------AGAKNHMVILPDANKAQVLGNLVGASCGAAGQRCMAISAAvFVGAAR--EW 297
Cdd:cd07123 256 GSTPTFKSLWKQIGENLDRYRTYprivgeTGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRA-YVPESLwpEV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 298 IPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGKAE-GAECLLDGSQCQVEGYpngnWLGPTLFRAVTPKM 376
Cdd:cd07123 335 KERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGY----FVEPTVIETTDPKH 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15595944 377 GLYREEIFGPVLACL--EVESLEEAIALVN-ANPYGNGTSLFTR 417
Cdd:cd07123 411 KLMTEEIFGPVLTVYvyPDSDFEETLELVDtTSPYALTGAIFAQ 454
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
20-409 |
3.78e-34 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 137.41 E-value: 3.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 20 ELVEVTDPATQ-DVLALAPKATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLAD 98
Cdd:PRK11809 659 EMSPVINPADPrDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSN 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 99 AKGDVWRGIEVVEHAANvaslmmgetveNVAREIDTASWIqPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQ 178
Cdd:PRK11809 739 AIAEVREAVDFLRYYAG-----------QVRDDFDNDTHR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQ 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 179 DPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLT-HPDIRAISFVGSVAVGQHVYRTGTAHLKR------VQAFAGA 251
Cdd:PRK11809 807 TPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVaDARVRGVMFTGSTEVARLLQRNLAGRLDPqgrpipLIAETGG 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 252 KNHMVILPDANKAQVLGNLVGASCGAAGQRCMAI------------SAAVFVGAAREWIPELAERMAVlrpghwqdpDAa 319
Cdd:PRK11809 887 QNAMIVDSSALTEQVVADVLASAFDSAGQRCSALrvlclqddvadrTLKMLRGAMAECRMGNPDRLST---------DI- 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 320 yGPLISPQARQRVLRLIAEGKAEGaECLLDGSQCQVEGYPNGNWLGPTLFRavTPKMGLYREEIFGPVLACLEV--ESLE 397
Cdd:PRK11809 957 -GPVIDAEAKANIERHIQAMRAKG-RPVFQAARENSEDWQSGTFVPPTLIE--LDSFDELKREVFGPVLHVVRYnrNQLD 1032
|
410
....*....|..
gi 15595944 398 EAIALVNANPYG 409
Cdd:PRK11809 1033 ELIEQINASGYG 1044
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
46-437 |
8.44e-32 |
|
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: 126.83 E-value: 8.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 46 QAIASAQR-AFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLAD--AKGDVWRGIEVVEHAA-NVASLMM 121
Cdd:cd07133 1 QALLERQKaAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGHRSRHetLLAEILPSIAGIKHARkHLKKWMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 122 GETVENVAREIDTASWI--QPLGVCAGITPFNFPAMipLWMFPL--AIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPK 197
Cdd:cd07133 81 PSRRHVGLLFLPAKAEVeyQPLGVVGIIVPWNYPLY--LALGPLiaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 198 gVLQVIHGGREqVDALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGASCGA 277
Cdd:cd07133 159 -EVAVVTGGAD-VAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 278 AGQRCMAI--------SAAVFVGAAREWI----PELAErmavlrpghwqDPDaaYGPLISPQARQRVLRLIAEGKAEGAE 345
Cdd:cd07133 237 AGQTCVAPdyvlvpedKLEEFVAAAKAAVakmyPTLAD-----------NPD--YTSIINERHYARLQGLLEDARAKGAR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 346 CLldgsQC--QVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANP-----YgngtsLFTRS 418
Cdd:cd07133 304 VI----ELnpAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPrplalY-----YFGED 374
|
410
....*....|....*....
gi 15595944 419 GGAARRYQHAVQVGQVGIN 437
Cdd:cd07133 375 KAEQDRVLRRTHSGGVTIN 393
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
38-446 |
1.53e-28 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 118.21 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 38 KATADEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGK--------NLADAKGDVWRGIev 109
Cdd:PTZ00381 3 PDNPEIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRhpfetkmtEVLLTVAEIEHLL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 110 vehaANVASLMMGETVENVAREIDTASWIQ--PLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLA 187
Cdd:PTZ00381 81 ----KHLDEYLKPEKVDTVGVFGPGKSYIIpePLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 188 ELFLEAgAPKGVLQVIHGGREQVDALLTHP-DIraISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAQV 266
Cdd:PTZ00381 157 KLLTKY-LDPSYVRVIEGGVEVTTELLKEPfDH--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 267 LGNLVGASCGAAGQRCMAISaAVFV--GAAREWIPELAERMavlrpghwqdpDAAYGPliSPQARQRVLRLIAEGKAEGA 344
Cdd:PTZ00381 234 ARRIAWGKFLNAGQTCVAPD-YVLVhrSIKDKFIEALKEAI-----------KEFFGE--DPKKSEDYSRIVNEFHTKRL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 345 ECLLDGSQCQVegYPNGN------WLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRS 418
Cdd:PTZ00381 300 AELIKDHGGKV--VYGGEvdienkYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGED 377
|
410 420 430
....*....|....*....|....*....|..
gi 15595944 419 GGAARRYQHAVQVGQVGINVPI----PVPLPF 446
Cdd:PTZ00381 378 KRHKELVLENTSSGAVVINDCVfhllNPNLPF 409
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
45-402 |
2.07e-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: 117.34 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 45 EQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKN---LADAKGDVWRgIEVVEHAANVASLMM 121
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGwmfAENICGDQVQ-LRARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 122 GETVE-NVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGA-PKGV 199
Cdd:cd07084 81 EPGNHlGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 200 LQVIHGGREQVDALLTHPDIRAISFVGSVAVGQHVYrtGTAHLKRVQAFAGAKNHMVILPDAN-KAQVLGNLVGASCGAA 278
Cdd:cd07084 161 VTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLA--LDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 279 GQRCMAISaAVFVGAAREWIPELAERMAVLRpgHWQDPDAAYGPLISPQARQRVLRLIAEGkaeGAECLLDGSQCQVEGY 358
Cdd:cd07084 239 GQKCTAQS-MLFVPENWSKTPLVEKLKALLA--RRKLEDLLLGPVQTFTTLAMIAHMENLL---GSVLLFSGKELKNHSI 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15595944 359 PN--GNWLGPTLFRAVTP---KMGLYREEIFGPVLACLEVESLEEAIAL 402
Cdd:cd07084 313 PSiyGACVASALFVPIDEilkTYELVTEEIFGPFAIVVEYKKDQLALVL 361
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
136-437 |
2.34e-28 |
|
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: 117.22 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 136 SWIQ--PLGVCAGITPFNFPAMipLWMFPL--AIACGNTFVLKPSEQDPLTPNRLAELFLEAgAPKGVLQVIHGGREQVD 211
Cdd:cd07136 94 SYIYyePYGVVLIIAPWNYPFQ--LALAPLigAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 212 ALLTHP-DirAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDAN-----KAQVLGNLVGAscgaaGQRCMA- 284
Cdd:cd07136 171 ELLDQKfD--YIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANlklaaKRIVWGKFLNA-----GQTCVAp 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 285 ----ISAAV---FVGAAREWIPELAERMAVlrpghwQDPDaaYGPLISPQARQRVLRLIAEGKaegaecLLDGSQCQveg 357
Cdd:cd07136 244 dyvlVHESVkekFIKELKEEIKKFYGEDPL------ESPD--YGRIINEKHFDRLAGLLDNGK------IVFGGNTD--- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 358 yPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANP-----YgngtsLFTRSGGAARRYQHAVQVG 432
Cdd:cd07136 307 -RETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPkplalY-----LFSEDKKVEKKVLENLSFG 380
|
....*
gi 15595944 433 QVGIN 437
Cdd:cd07136 381 GGCIN 385
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
44-477 |
3.43e-24 |
|
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: 104.80 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 44 IEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDvwrGIEVVEHAANVA-----S 118
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRD---EVSVLVSSCKLAikelkK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 119 LMMGETVE-NVAREIDTASWI-QPLGVCAGITPFNFPamIPLWMFPL--AIACGNTFVLKPSEQDPLTPNRLAELFLEAG 194
Cdd:cd07137 78 WMAPEKVKtPLTTFPAKAEIVsEPLGVVLVISAWNFP--FLLSLEPVigAIAAGNAVVLKPSELAPATSALLAKLIPEYL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 195 APKGVlQVIHGGREQVDALLTHP-DirAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAQVLGNLVGA 273
Cdd:cd07137 156 DTKAI-KVIEGGVPETTALLEQKwD--KIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 274 SCGA-AGQRCMAISaavFVGAAREWIPELAERM-AVLRPGHWQDP----DAAYgpLISPQARQRVLRLIAEGKAegAECL 347
Cdd:cd07137 233 KWGCnNGQACIAPD---YVLVEESFAPTLIDALkNTLEKFFGENPkeskDLSR--IVNSHHFQRLSRLLDDPSV--ADKI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 348 LDGSQCQVEGYpngnWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQH 427
Cdd:cd07137 306 VHGGERDEKNL----YIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVA 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 15595944 428 AVQVGQVGIN-VPIPVPLPFFSFTGWKGSFYGDLHayGKQAVRFYTETKTV 477
Cdd:cd07137 382 ETSSGGVTFNdTVVQYAIDTLPFGGVGESGFGAYH--GKFSFDAFSHKKAV 430
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
45-404 |
1.46e-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: 103.07 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 45 EQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAkgdVWRGIEVVE----HA-ANVASL 119
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEA---VLSEILLVKneikYAiSNLPEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 120 MMGETVE-NVAREIDTAsWIQ--PLGVCAGITPFNFPamIPLWMFPL--AIACGNTFVLKPSEQDPLTPNRLAELFleag 194
Cdd:cd07132 78 MKPEPVKkNLATLLDDV-YIYkePLGVVLIIGAWNYP--LQLTLVPLvgAIAAGNCVVIKPSEVSPATAKLLAELI---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 195 aPKGV----LQVIHGGREQVDALLTHpdiR--AISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDANKAQVLG 268
Cdd:cd07132 151 -PKYLdkecYPVVLGGVEETTELLKQ---RfdYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 269 NLVGASCGAAGQRCMA-----ISAAV---FVGAAREWIPElaermavlrpghW------QDPDaaYGPLISPQARQRVLR 334
Cdd:cd07132 227 RIAWGKFINAGQTCIApdyvlCTPEVqekFVEALKKTLKE------------FygedpkESPD--YGRIINDRHFQRLKK 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595944 335 LIAEGK-AEGAECllDGSQCQVEgypngnwlgPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVN 404
Cdd:cd07132 293 LLSGGKvAIGGQT--DEKERYIA---------PTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFIN 352
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
9-425 |
3.25e-21 |
|
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: 96.57 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 9 IDGEWRGSrSRELVEVTDPATQDVLAlapKATADEIEQAiasaqRAFETWREVPAP--------ERARlMLRY--QHLLk 78
Cdd:cd07128 5 VAGQWHAG-TGDGRTLHDAVTGEVVA---RVSSEGLDFA-----AAVAYAREKGGPalraltfhERAA-MLKAlaKYLM- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 79 EHHDELGELLAReTGKNLADAKGDVWRGIEVVEHAANVASLMM--------GETVE------NVAREIDTaswiqPL-GV 143
Cdd:cd07128 74 ERKEDLYALSAA-TGATRRDSWIDIDGGIGTLFAYASLGRRELpnahflveGDVEPlskdgtFVGQHILT-----PRrGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 144 CAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGA-PKGVLQVIHGGreqVDALLTHPDIR-A 221
Cdd:cd07128 148 AVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHLGEQdV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 222 ISFVGSVAVGQHVyRTG---TAHLKRVQAFAGAKNHMVILPDANKAQ-----VLGNLVGASCGAAGQRCMAISAAvFVGA 293
Cdd:cd07128 225 VAFTGSAATAAKL-RAHpniVARSIRFNAEADSLNAAILGPDATPGTpefdlFVKEVAREMTVKAGQKCTAIRRA-FVPE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 294 ARE--WIPELAERMAVLRPGHWQDPDAAYGPLISPQARQRVLRLIAEGKAEGAECLLDGSQCQVEGYPN--GNWLGPTLF 369
Cdd:cd07128 303 ARVdaVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVGADAekGAFFPPTLL 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595944 370 RAVTP--KMGLYREEIFGPVLACLEVESLEEAIALVNAnpyGNG---TSLFTRSGGAARRY 425
Cdd:cd07128 383 LCDDPdaATAVHDVEAFGPVATLMPYDSLAEAIELAAR---GRGslvASVVTNDPAFAREL 440
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
38-482 |
3.12e-18 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 87.09 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 38 KATADEIEQAIASAQRAFET-------WREvpapERARLMLRyqhLLKEHHDELGELLARETGKNLADAKGDvwrGIEVV 110
Cdd:PLN02203 2 EAPGETLEGSVAELRETYESgrtrsleWRK----SQLKGLLR---LLKDNEEAIFKALHQDLGKHRVEAYRD---EVGVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 111 EHAANVASLMMGETVENVAREIDTASWI-------QPLGVCAGITPFNFPamIPLWMFPL--AIACGNTFVLKPSEQDPL 181
Cdd:PLN02203 72 TKSANLALSNLKKWMAPKKAKLPLVAFPataevvpEPLGVVLIFSSWNFP--IGLSLEPLigAIAAGNAVVLKPSELAPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 182 TPNRLAE---LFLEAGAPKgvlqVIHGGREQVDALLTHP-DirAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVI 257
Cdd:PLN02203 150 TSAFLAAnipKYLDSKAVK----VIEGGPAVGEQLLQHKwD--KIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 258 --LPDANKAQVLGN-LVGASCGA-AGQRCMAISaavFVGAAREWIPELAErmaVLRP------GHWQDPDAAYGPLISPQ 327
Cdd:PLN02203 224 dsLSSSRDTKVAVNrIVGGKWGScAGQACIAID---YVLVEERFAPILIE---LLKStikkffGENPRESKSMARILNKK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 328 ARQRVLRLIAEGKAegAECLLDGSQCQvegyPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALVNANP 407
Cdd:PLN02203 298 HFQRLSNLLKDPRV--AASIVHGGSID----EKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKP 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595944 408 YGNGTSLFTRSGGAARRYQHAVQVGQVGIN-VPIPVPLPFFSFTGWKGSFYGDLHayGKQAVRFYTETKTVTSRWF 482
Cdd:PLN02203 372 KPLAIYAFTNNEKLKRRILSETSSGSVTFNdAIIQYACDSLPFGGVGESGFGRYH--GKYSFDTFSHEKAVLRRSL 445
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
44-405 |
9.95e-18 |
|
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: 85.67 E-value: 9.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 44 IEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNLADAKGDVWRGIEVVEHAANVAslmmge 123
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 124 tVENVARE--IDTA-------------SWIQPLGVCAGITPFNFP-AmiplwmFPL-------AIACGNTFVLKPSEQDP 180
Cdd:cd07129 75 -REGSWLDarIDPAdpdrqplprpdlrRMLVPLGPVAVFGASNFPlA------FSVaggdtasALAAGCPVVVKAHPAHP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 181 LTPNRLAELFLEA----GAPKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVYRTGTAHLKRVQAFA--GAKN 253
Cdd:cd07129 148 GTSELVARAIRAAlratGLPAGVFSLLQGGGREVgVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEPIPFYAelGSVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 254 HMVILPDA---NKAQVLGNLVGASCGAAGQRC------MAISAAvfvgAAREWIPELAERMAvlrpghwqdpDAAYGPLI 324
Cdd:cd07129 228 PVFILPGAlaeRGEAIAQGFVGSLTLGAGQFCtnpglvLVPAGP----AGDAFIAALAEALA----------AAPAQTML 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 325 SPQarqrvlrlIAEGKAEGAECLLD--GSQCQVEGY--PNGNWLGPTLFRAV------TPKMglyREEIFGPVLACLEVE 394
Cdd:cd07129 294 TPG--------IAEAYRQGVEALAAapGVRVLAGGAaaEGGNQAAPTLFKVDaaaflaDPAL---QEEVFGPASLVVRYD 362
|
410
....*....|.
gi 15595944 395 SLEEAIALVNA 405
Cdd:cd07129 363 DAAELLAVAEA 373
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
139-480 |
4.60e-16 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 80.48 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 139 QPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELfLEAGAPKGVLQVIHGGREQVDALLTHpD 218
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTETTALLEQ-K 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 219 IRAISFVGSVAVGQHVYRTGTAHLKRVQAFAGAKNHMVILPDAN-KAQVLGNLVGASCGAAGQRCMAISaavFVGAAREW 297
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDlKVTVRRIIAGKWGCNNGQACISPD---YILTTKEY 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 298 IPELAERMAV-LRPGHWQDP--DAAYGPLISPQARQRVLRLIAEgkAEGAECLLDGSQCQVEGYPngnwLGPTLFRAVTP 374
Cdd:PLN02174 266 APKVIDAMKKeLETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDE--KEVSDKIVYGGEKDRENLK----IAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 375 KMGLYREEIFGPVLACLEVESLEEAIALVNANPYGNGTSLFTRSGGAARRYQHAVQVGQVGIN-VPIPVPLPFFSFTGWK 453
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVG 419
|
330 340
....*....|....*....|....*..
gi 15595944 454 GSFYGDLHayGKQAVRFYTETKTVTSR 480
Cdd:PLN02174 420 ESGMGAYH--GKFSFDAFSHKKAVLYR 444
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
1-403 |
8.17e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 76.67 E-value: 8.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 1 MAKAIPQLIDGEWRGSrSRELVEVTDPATQDVLALApKATADEIEQAIASA-QRAFETWREVPAPERARLMLRYQHLLKE 79
Cdd:PRK11903 1 MTELLANYVAGRWQAG-SGAGTPLFDPVTGEELVRV-SATGLDLAAAFAFArEQGGAALRALTYAQRAALLAAIVKVLQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 80 HHDELGELLARETGKNLADAKGDVWRGIEVVEHAA-------NVASLMMGETVEnVAREIDTAS---WIQPLGVCAGITP 149
Cdd:PRK11903 79 NRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAklgaalgDARLLRDGEAVQ-LGKDPAFQGqhvLVPTRGVALFINA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 150 FNFPAMiPLW-MFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGA-PKGVLQVIHGGREQVDALLTHPDIraISFVGS 227
Cdd:PRK11903 158 FNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFDV--VSFTGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 228 VAVGQhVYRTGTAHLK---RVQAFAGAKNHMVILPDANK-----AQVLGNLVGASCGAAGQRCMAISAaVFVGAA--REW 297
Cdd:PRK11903 235 AETAA-VLRSHPAVVQrsvRVNVEADSLNSALLGPDAAPgseafDLFVKEVVREMTVKSGQKCTAIRR-IFVPEAlyDAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 298 IPELAERMAVLRPGHWQDPDAAYGPLISpQARQRVLRLIAEGKAEGAECLLDGSQCQ-VEGYPN-GNWLGPTLFRAVTPK 375
Cdd:PRK11903 313 AEALAARLAKTTVGNPRNDGVRMGPLVS-RAQLAAVRAGLAALRAQAEVLFDGGGFAlVDADPAvAACVGPTLLGASDPD 391
|
410 420 430
....*....|....*....|....*....|
gi 15595944 376 MG--LYREEIFGPVLACLEVESLEEAIALV 403
Cdd:PRK11903 392 AAtaVHDVEVFGPVATLLPYRDAAHALALA 421
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
8-234 |
1.17e-13 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 72.91 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 8 LIDGEWRGSRsrELVEVTDPATQDVLALAPKATADEIEQAIASAQRAFETWREVP--APERARL----MLRYQHLLK--E 79
Cdd:cd07126 2 LVAGKWKGAS--NYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPlkNPERYLLygdvSHRVAHELRkpE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 80 HHDELGELLARETGKNLADAKGDVWRGIEVVEHAAnvaslmmGETVENVAREIDTASWIQ---------PLGVCAGITPF 150
Cdd:cd07126 80 VEDFFARLIQRVAPKSDAQALGEVVVTRKFLENFA-------GDQVRFLARSFNVPGDHQgqqssgyrwPYGPVAIITPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 151 NFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVIHGGREQVDALLTHPDIRAISFVGSVAV 230
Cdd:cd07126 153 NFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKV 232
|
....
gi 15595944 231 GQHV 234
Cdd:cd07126 233 AERL 236
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
43-464 |
3.46e-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: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 43 EIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETGKNL-----ADAKGDVWRGIEVVEHAAnva 117
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFmmafqAGGPHAQDRGLEAVAYAW--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 118 slmmgetvENVAREIDTASWIQPLG-------------VCAGITPFNFPAMIPLW-----MFPlAIACGNTFVLKPSEQD 179
Cdd:cd07127 162 --------REMSRIPPTAEWEKPQGkhdplamektftvVPRGVALVIGCSTFPTWngypgLFA-SLATGNPVIVKPHPAA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 180 PL----TPNRLAELFLEAG-APKGVLQVIHGGREQV-DALLTHPDIRAISFVGSVAVGQHVyrtgTAHLKRVQAF---AG 250
Cdd:cd07127 233 ILplaiTVQVAREVLAEAGfDPNLVTLAADTPEEPIaQTLATRPEVRIIDFTGSNAFGDWL----EANARQAQVYtekAG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 251 AkNHMVILPDANKAQVLGNLVGASCGAAGQRCMAiSAAVFVGAA-------REWIPELAERMAVLRPGHWQDPDAAYGPL 323
Cdd:cd07127 309 V-NTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTT-PQNIYVPRDgiqtddgRKSFDEVAADLAAAIDGLLADPARAAALL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 324 ISPQArQRVLRLIAEGkAEGAECLLDGSQCQVEGYPNGNWLGPTLFRAVTPKMGLYREEIFGPVLACLEVESLEEAIALV 403
Cdd:cd07127 387 GAIQS-PDTLARIAEA-RQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELA 464
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 404 NANPYGNGT---SLFTRSGGAARRYQHAVQvgQVGINVPIpvplpffSFTGwkGSF------YGDLHAYG 464
Cdd:cd07127 465 RESVREHGAmtvGVYSTDPEVVERVQEAAL--DAGVALSI-------NLTG--GVFvnqsaaFSDFHGTG 523
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
76-306 |
1.46e-09 |
|
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: 59.93 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 76 LLKEHHDELGELLARETGKNLADAKGDVWRGIEVVEHAAN---VASLMMGETVENVARE--IDTASWIQ---PLGVCAGI 147
Cdd:cd07077 28 ALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYkniDTERGITASVGHIQDVllPDNGETYVrafPIGVTMHI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 148 TPFNFPAMIPLWMFpLAIACGNTFVLKPSEQDPLTPNRLAELFLEA---GAPKGVLQVI-HGGREQVDALLTHPDIRAIS 223
Cdd:cd07077 108 LPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVpHPSDELAEELLSHPKIDLIV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 224 FVGSVAVGQHVYRTGTAhlKRVQAFAGAKNHMVILPDANKAQVLGnLVGASCGAAGQRCMAISAAVFVGAAREwipELAE 303
Cdd:cd07077 187 ATGGRDAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERASG-SVHDSKFFDQNACASEQNLYVVDDVLD---PLYE 260
|
...
gi 15595944 304 RMA 306
Cdd:cd07077 261 EFK 263
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
42-257 |
1.97e-06 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 50.29 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 42 DEIEQAIASAQRAFETWREVPAPERARLMLRYQHLLKEHHDELGELLARETG---------KNLADAK------------ 100
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGmgrvedkiaKNVAAAEktpgvedlttea 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 101 --GDvwRGIEVVEHAanvaslmmgetvenvareidtaswiqPLGVCAGITPFNFPA---------MiplwmfplaIACGN 169
Cdd:PRK15398 116 ltGD--NGLTLIEYA--------------------------PFGVIGAVTPSTNPTetiinnaisM---------LAAGN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 170 TFVLKPSEQDPLTPNRLAELF----LEAGAPKGVLQVIHGGR-EQVDALLTHPDIRAISFVGSVAVGQHVYRTGtahlKR 244
Cdd:PRK15398 159 SVVFSPHPGAKKVSLRAIELLneaiVAAGGPENLVVTVAEPTiETAQRLMKHPGIALLVVTGGPAVVKAAMKSG----KK 234
|
250
....*....|...
gi 15595944 245 VQAfAGAKNHMVI 257
Cdd:PRK15398 235 AIG-AGAGNPPVV 246
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
79-222 |
3.83e-06 |
|
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: 49.03 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 79 EHHDELGELLARETG---------KNLADAKGdvwrgieVVEHAANVASlmMGETVENVAREIDTASWiqPLGVCAGITP 149
Cdd:cd07122 36 DAAEELAKMAVEETGmgvvedkviKNHFASEY-------VYNDIKDMKT--VGVIEEDEEKGIVEIAE--PVGVIAALIP 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595944 150 FNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEA----GAPKGVLQVI-HGGREQVDALLTHPDIRAI 222
Cdd:cd07122 105 STNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIeEPSIELTQELMKHPDVDLI 182
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
42-258 |
1.26e-04 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 44.56 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 42 DEIEQAIASAQRAFETWREvpapERARLMLRYQHLLKEHHD-ELGELLARETGKNLADAKgdVWRGIEVVEHAANVASLM 120
Cdd:cd07081 2 DDAVAAAKVAQQGLSCKSQ----EMVDLIFRAAAEAAEDARiDLAKLAVSETGMGRVEDK--VIKNHFAAEYIYNVYKDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 121 MGETVENVAREIDTASWIQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEA----GAP 196
Cdd:cd07081 76 KTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595944 197 KGVLQVI-HGGREQVDALLTHPDIRAISFVGSVAVGQHVYRTGtahlKRVQAfAGAKNHMVIL 258
Cdd:cd07081 156 ENLIGWIdNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSG----KPAIG-VGAGNTPVVI 213
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
139-222 |
2.04e-03 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 40.34 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 139 QPLGVCAGITPFNFPaMIPLWMFPLAIACGNTFVLKPSEQDPLTPNRLAELFLEAGAPKGVLQVI------HGGREQVDA 212
Cdd:cd07080 111 QPRGLVVHIIAGNVP-LLPVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLADVDPNHPLTDSIsvvywpGGDAELEER 189
|
90
....*....|
gi 15595944 213 LLTHPDIRAI 222
Cdd:cd07080 190 ILASADAVVA 199
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
140-222 |
4.43e-03 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 39.78 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595944 140 PLGVCAGITPF-N------FPAMIplwmfplAIACGNTFVLKPSEQDPLTPNRLAELFLEA----GAPKGVLQVI-HGGR 207
Cdd:PRK13805 108 PVGVIAGITPTtNptstaiFKALI-------ALKTRNPIIFSFHPRAQKSSIAAAKIVLDAavaaGAPKDIIQWIeEPSV 180
|
90
....*....|....*
gi 15595944 208 EQVDALLTHPDIRAI 222
Cdd:PRK13805 181 ELTNALMNHPGIALI 195
|
|
| |
