|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
10-487 |
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: 764.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 10 VAHFINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDEL 89
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 90 AAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVA 169
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 170 IACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKR 249
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 250 VQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPI 329
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 330 VTAEALKRIEDYVQIGVDEGATLVVDGRGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLI 409
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534885945 410 NSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMAWHGFGGWKASLFGDMHAYGEEGVRFYTRQKSIMQRW 487
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
10-487 |
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: 603.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 10 VAHFINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDEL 89
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 90 AAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVA 169
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 170 IACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKR 249
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 250 VQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVgDKLIPKLAARLKTLKVTDGMDLSAEMGPI 329
Cdd:TIGR01722 241 VQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGAEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 330 VTAEALKRIEDYVQIGVDEGATLVVDGRGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLI 409
Cdd:TIGR01722 320 ITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534885945 410 NSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMAWHGFGGWKASLFGDMHAYGEEGVRFYTRQKSIMQRW 487
Cdd:TIGR01722 400 NASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
6-487 |
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: 557.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 6 NDQTVAHFINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQH 85
Cdd:COG1012 2 TTPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 86 RDELAAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWM 165
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 166 FPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGD-KLAVETLLNHPDVAALSFVGSTPIAKFIYETGA 244
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 245 RNGKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSA 324
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 325 EMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRgqkPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTE 404
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGR---RPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 405 GLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMAWHGFGGWKASLFGDMHayGEEGVRFYTRQKSIM 484
Cdd:COG1012 399 AIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREG--GREGLEEYTETKTVT 476
|
...
gi 2534885945 485 QRW 487
Cdd:COG1012 477 IRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
22-483 |
6.63e-164 |
|
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: 472.02 E-value: 6.63e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 22 AGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVF 101
Cdd:pfam00171 4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 102 TDAQGEVSRGIDIIEFACGIPQLLKGDyTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPS 181
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLARRLDGE-TLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 182 ERDPSAGNFMARLLKEAGLPDGVFNVVHGD-KLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQALGGAKNHL 260
Cdd:pfam00171 163 ELTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 261 LVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIED 340
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 341 YVQIGVDEGATLVVDGrgqkPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSC 420
Cdd:pfam00171 323 YVEDAKEEGAKLLTGG----EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534885945 421 YTRDGNVAREFGRQVQVGMVGINVPIPVPMAWHGFGGWKASLFGDmhAYGEEGVRFYTRQKSI 483
Cdd:pfam00171 399 FTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGR--EGGPYGLEEYTEVKTV 459
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
10-502 |
8.03e-157 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 459.21 E-value: 8.03e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 10 VAHFINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDEL 89
Cdd:PLN02419 114 VPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 90 AAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVA 169
Cdd:PLN02419 194 AMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 170 IACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKR 249
Cdd:PLN02419 274 VTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 250 VQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDvGDKLIPKLAARLKTLKVTDGMDLSAEMGPI 329
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGD-AKSWEDKLVERAKALKVTCGSEPDADLGPV 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 330 VTAEALKRIEDYVQIGVDEGATLVVDGRGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLI 409
Cdd:PLN02419 433 ISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISII 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 410 NSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMAWHGFGGWKASLFGDMHAYGEEGVRFYTRQKSIMQRWPD 489
Cdd:PLN02419 513 NKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQKD 592
|
490
....*....|...
gi 2534885945 490 sIEKGAEFVMPTS 502
Cdd:PLN02419 593 -IHSPFSLAIPIL 604
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
67-484 |
2.58e-135 |
|
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: 398.12 E-value: 2.58e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 67 PPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPV 146
Cdd:cd07078 18 PPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGELAIVRREPL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 147 GVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGD-KLAVETLLNHPDVA 225
Cdd:cd07078 98 GVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDgDEVGAALASHPRVD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 226 ALSFVGSTPIAKFIYETGARNGKRVQA-LGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVaVMV-GDVGDKL 303
Cdd:cd07078 178 KISFTGSTAVGKAIMRAAAENLKRVTLeLGG-KSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASR-LLVhESIYDEF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 304 IPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGrgqKPAGFENGFYTGGTLFDNVKPNMR 383
Cdd:cd07078 256 VERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGG---KRLEGGKGYFVPPTVLTDVDPDMP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 384 IYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMAWHGFGGWKASLF 463
Cdd:cd07078 333 IAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPSAPFGGVKQSGI 412
|
410 420
....*....|....*....|.
gi 2534885945 464 GdmHAYGEEGVRFYTRQKSIM 484
Cdd:cd07078 413 G--REGGPYGLEEYTEPKTVT 431
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-483 |
2.15e-120 |
|
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: 361.67 E-value: 2.15e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 12 HFINGNTVSIAGSKTANVFNPS-LGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELA 90
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 91 AIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAI 170
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 171 ACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHG-DKLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKR 249
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 250 VQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPI 329
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 330 VTAEALKRIEDYVQIGVDEGATLVVDGRGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLI 409
Cdd:cd07131 321 INEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534885945 410 NSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVP-----IPVPmawhgFGGWKASLFGDMHAyGEEGVRFYTRQKSI 483
Cdd:cd07131 401 NDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPtigaeVHLP-----FGGVKKSGNGHREA-GTTALDAFTEWKAV 473
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
12-483 |
5.10e-120 |
|
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: 360.41 E-value: 5.10e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 12 HFINGNTVsiAGSKTANVFNPS-----LGTVARqvelADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHR 86
Cdd:cd07097 3 NYIDGEWV--AGGDGEENRNPSdtsdvVGKYAR----ASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 87 DELAAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMF 166
Cdd:cd07097 77 EELARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 167 PVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGAR 245
Cdd:cd07097 157 APALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 246 NGKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAE 325
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 326 MGPIVTAEALKRIEDYVQIGVDEGATLvVDGrGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEG 405
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKL-VYG-GERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 406 LNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVP-----IPVPmawhgFGGWKASLFGdMHAYGEEGVRFYTRQ 480
Cdd:cd07097 395 LAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPtagvdYHVP-----FGGRKGSSYG-PREQGEAALEFYTTI 468
|
...
gi 2534885945 481 KSI 483
Cdd:cd07097 469 KTV 471
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
29-483 |
3.40e-107 |
|
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: 326.70 E-value: 3.40e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEV 108
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 109 SRGIDIIE-FACGIPQLLkGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPC-MV-----PcwmfpvAIACGNTFILKPS 181
Cdd:cd07103 81 DYAASFLEwFAEEARRIY-GRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAaMItrkiaP------ALAAGCTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 182 ERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaknH 259
Cdd:cd07103 154 EETPLSALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSlELGG---N 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 260 --LLVMPDADLNQVTDALIGAAYGSAGERCMA---ISVAVmvgDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEA 334
Cdd:cd07103 231 apFIVFDDADLDKAVDGAIASKFRNAGQTCVCanrIYVHE---SIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 335 LKRIEDYVQIGVDEGATLVVDGRGQKPAGFengFYTgGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQY 414
Cdd:cd07103 308 VEKVEALVEDAVAKGAKVLTGGKRLGLGGY---FYE-PTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPY 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534885945 415 GNGVSCYTRDGNVAREFGRQVQVGMVGINVPIP----VPmawhgFGGWKASLFGdmHAYGEEGVRFYTRQKSI 483
Cdd:cd07103 384 GLAAYVFTRDLARAWRVAEALEAGMVGINTGLIsdaeAP-----FGGVKESGLG--REGGKEGLEEYLETKYV 449
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
66-484 |
4.11e-106 |
|
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: 321.10 E-value: 4.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 66 KPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQP 145
Cdd:cd06534 13 LPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEAYVRREP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 146 VGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGD-KLAVETLLNHPDV 224
Cdd:cd06534 93 LGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGgDEVGAALLSHPRV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 225 AALSFVGSTPIAKFIYETGARNGKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLI 304
Cdd:cd06534 173 DKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDEFV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 305 PKLAarlktlkvtdgmdlsaemgpivtaealkriedyvqigvdegatlvvdgrgqkpagfengfytggTLFDNVKPNMRI 384
Cdd:cd06534 253 EKLV----------------------------------------------------------------TVLVDVDPDMPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 385 YLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMAWHGFGGWKASLFG 464
Cdd:cd06534 269 AQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFGGVKNSGIG 348
|
410 420
....*....|....*....|
gi 2534885945 465 DMHayGEEGVRFYTRQKSIM 484
Cdd:cd06534 349 REG--GPYGLEEYTRTKTVV 366
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
29-483 |
1.46e-102 |
|
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: 314.89 E-value: 1.46e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQ-GE 107
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 108 VSRGIDIIEFACGIPQLLKGDYTEQVSTNIdNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSA 187
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGAL-NYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 188 GNFMARLLKEAGLPDGVFNVVHGD-KLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQA-LGGaKNHLLVMPD 265
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLeLGG-KNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 266 ADLNQVTDALIGAAYGSAGERCMAISvAVMVGD-VGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQI 344
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGS-RILVQRsIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 345 GVDEGATLVVDGRGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRD 424
Cdd:cd07093 318 ARAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534885945 425 GNVAREFGRQVQVGMVGINVPI----PVPmawhgFGGWKASlfGDmhayGEEG----VRFYTRQKSI 483
Cdd:cd07093 398 LGRAHRVARRLEAGTVWVNCWLvrdlRTP-----FGGVKAS--GI----GREGgdysLEFYTELKNV 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
29-484 |
5.51e-99 |
|
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: 305.63 E-value: 5.51e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKA--ALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQG 106
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAafEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 107 EVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPS 186
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 187 AGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQA-LGGaKNHLLVMP 264
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETgEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLeLGG-KSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 265 DADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQI 344
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 345 GVDEGATLVVDGRGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRD 424
Cdd:cd07114 320 AREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534885945 425 GNVAREFGRQVQVGMVGIN----VPIPVPmawhgFGGWKASLFGdmHAYGEEGVRFYTRQKSIM 484
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNtyraLSPSSP-----FGGFKDSGIG--RENGIEAIREYTQTKSVW 456
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
13-483 |
4.91e-97 |
|
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: 301.11 E-value: 4.91e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAI 92
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 93 ITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPC-MVPCWMFPvAIA 171
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFfLIARKLAP-ALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 172 CGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRV 250
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 251 Q-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPI 329
Cdd:cd07088 240 SlELGG-KAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 330 VTAEALKRIEDYVQIGVDEGATLVVDGrgqKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLI 409
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGG---KRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534885945 410 NSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMawHGF-GGWKASLFGDmhAYGEEGVRFYTRQKSI 483
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAM--QGFhAGWKKSGLGG--ADGKHGLEEYLQTKVV 466
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
7-483 |
3.43e-96 |
|
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: 299.71 E-value: 3.43e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 7 DQTVAHFINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANK-PPLQRVRIMNKFLALMNQH 85
Cdd:cd07144 5 DQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 86 RDELAAIITAEHGKVF-TDAQGEVSRGIDIIEFACGIPQLLKGDyTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCW 164
Cdd:cd07144 85 RDLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGK-TIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 165 MFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHG-DKLAVETLLNHPDVAALSFVGSTPIAKFIYETG 243
Cdd:cd07144 164 KLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 244 ARNGKRVQALGGAKNHLLVMPDADLNQVTD-ALIGAAYGSaGERCMAISVAVMVGDVGDKLIPKLAARLK-TLKVTDGMD 321
Cdd:cd07144 244 AQNLKAVTLECGGKSPALVFEDADLDQAVKwAAAGIMYNS-GQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 322 LSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGqKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVAN 401
Cdd:cd07144 323 DDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK-APEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 402 FTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVP----IPVPmawhgFGGWKASLFGdmHAYGEEGVRFY 477
Cdd:cd07144 402 YEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMSGIG--RELGEYGLETY 474
|
....*.
gi 2534885945 478 TRQKSI 483
Cdd:cd07144 475 TQTKAV 480
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
12-483 |
3.68e-96 |
|
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: 299.09 E-value: 3.68e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 12 HFINGNTVSiAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAA 91
Cdd:cd07086 1 GVIGGEWVG-SGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 92 IITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIA 171
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 172 CGNTFILKPSERDPSAGNFMARLLKEA----GLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETGA-RN 246
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVArRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 247 GKRVQALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEM 326
Cdd:cd07086 240 GRVLLELGG-NNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 327 GPIVTAEALKRIEDYVQIGVDEGATLVVDGRgqKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGL 406
Cdd:cd07086 319 GPLINQAAVEKYLNAIEIAKSQGGTVLTGGK--RIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 407 NLINSHQYGNGVSCYTRD-GNVAREFG-RQVQVGMVGINVP-----IpvpmawHG-FGGWKASlfGDMHAYGEEGVRFYT 478
Cdd:cd07086 397 AINNDVPQGLSSSIFTEDlREAFRWLGpKGSDCGIVNVNIPtsgaeI------GGaFGGEKET--GGGRESGSDAWKQYM 468
|
....*
gi 2534885945 479 RQKSI 483
Cdd:cd07086 469 RRSTC 473
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
31-483 |
8.35e-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: 8.35e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 31 NPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQG-EVS 109
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 110 RGIDIIEFACGIPQLLKGDyTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGN 189
Cdd:cd07115 83 RAADTFRYYAGWADKIEGE-VIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 190 FMARLLKEAGLPDGVFNVVHG-DKLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQALGGAKNHLLVMPDADL 268
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 269 NQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDE 348
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 349 GATLVVDGRGQKpagfENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVA 428
Cdd:cd07115 322 GARLLTGGKRPG----ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2534885945 429 REFGRQVQVGMVGIN----VPIPVPmawhgFGGWKASLFGDMHayGEEGVRFYTRQKSI 483
Cdd:cd07115 398 HRVAAALKAGTVWINtynrFDPGSP-----FGGYKQSGFGREM--GREALDEYTEVKSV 449
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
13-483 |
2.12e-92 |
|
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: 289.49 E-value: 2.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKA--ALPAWANKPPLQRVRIMNKFLALMNQHRDELA 90
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAafETGWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 91 AIITAEHGKVFTD-AQGEVSRGIDIIEFACGIPQLLKGDyTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVA 169
Cdd:cd07091 87 ALESLDNGKPLEEsAKGDVALSIKCLRYYAGWADKIQGK-TIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 170 IACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHG-DKLAVETLLNHPDVAALSFVGSTPIAKFIYETGAR-NG 247
Cdd:cd07091 166 LAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 248 KRVQ-ALGGaKNHLLVMPDADLNQvtdALIGAAYG---SAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLS 323
Cdd:cd07091 246 KKVTlELGG-KSPNIVFDDADLDK---AVEWAAFGiffNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 324 AEMGPIVTAEALKRIEDYVQIGVDEGATLVVDgrGQKPAGfeNGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFT 403
Cdd:cd07091 322 TFQGPQVSKAQFDKILSYIESGKKEGATLLTG--GERHGS--KGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 404 EGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGIN------VPIPvpmawhgFGGWKASLFG-DMhayGEEGVRF 476
Cdd:cd07091 398 EVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNtynvfdAAVP-------FGGFKQSGFGrEL---GEEGLEE 467
|
....*..
gi 2534885945 477 YTRQKSI 483
Cdd:cd07091 468 YTQVKAV 474
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
11-487 |
3.81e-92 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 288.96 E-value: 3.81e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 11 AHFINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAA-LPAWANKPPLQRVRIMNKFLALMNQHRDEL 89
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 90 AAIITAEHGKVFTdaqgeVSRGIdiiEFACGIPQLlkgDYTEQVSTNIDN-----------------WTLRQPVGVVAGI 152
Cdd:cd07113 81 AQLETLCSGKSIH-----LSRAF---EVGQSANFL---RYFAGWATKINGetlapsipsmqgerytaFTRREPVGVVAGI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 153 TPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGS 232
Cdd:cd07113 150 VPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 233 TPIAKFIYETGARNGKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLK 312
Cdd:cd07113 230 VATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 313 TLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGqkPAGfeNGFYTGGTLFDNVKPNMRIYLEEIFGP 392
Cdd:cd07113 310 SFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEA--LAG--EGYFVQPTLVLARSADSRLMREETFGP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 393 VLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGIN----VPIPVPmawhgFGGWKASLFGdmHA 468
Cdd:cd07113 386 VVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmhtfLDPAVP-----FGGMKQSGIG--RE 458
|
490
....*....|....*....
gi 2534885945 469 YGEEGVRFYTRQKSIMQRW 487
Cdd:cd07113 459 FGSAFIDDYTELKSVMIRY 477
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
31-468 |
1.14e-91 |
|
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: 287.19 E-value: 1.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 31 NPSLGTVARQVELADIATVNKAVEAAKAALPAWA--NKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDaqgev 108
Cdd:cd07112 8 NPATGRVLAEVAACDAADVDRAVAAARRAFESGVwsRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISD----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 109 SRGIDIIEFACGI---PQLLKGDYTEQVSTNIDNWTL--RQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSER 183
Cdd:cd07112 83 ALAVDVPSAANTFrwyAEAIDKVYGEVAPTGPDALALitREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 184 DPSAGNFMARLLKEAGLPDGVFNVVHGD-KLAVETLLNHPDVAALSFVGSTPIAKFIYETGAR-NGKRVQALGGAKNHLL 261
Cdd:cd07112 163 SPLTALRLAELALEAGLPAGVLNVVPGFgHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 262 VMPDA-DLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIED 340
Cdd:cd07112 243 VFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 341 YVQIGVDEGATLVVDG-RGQKPAGfenGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVS 419
Cdd:cd07112 323 YIESGKAEGARLVAGGkRVLTETG---GFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2534885945 420 CYTRDGNVAREFGRQVQVGMVGIN----VPIPVPmawhgFGGWKASLFG---DMHA 468
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNcfdeGDITTP-----FGGFKQSGNGrdkSLHA 450
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
70-483 |
3.09e-91 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 285.77 E-value: 3.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 70 QRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVV 149
Cdd:cd07118 44 ERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 150 AGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALS 228
Cdd:cd07118 124 GIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 229 FVGSTPIAKFIYETGARNGKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLA 308
Cdd:cd07118 204 FTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 309 ARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGrgqKPAGFENGFYTGGTLFDNVKPNMRIYLEE 388
Cdd:cd07118 284 ARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGG---ERLASAAGLFYQPTIFTDVTPDMAIAREE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 389 IFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPI----PVPmawhgFGGWKASLFG 464
Cdd:cd07118 361 IFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLdgspELP-----FGGFKQSGIG 435
|
410
....*....|....*....
gi 2534885945 465 dmHAYGEEGVRFYTRQKSI 483
Cdd:cd07118 436 --RELGRYGVEEYTELKTV 452
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
13-483 |
1.54e-90 |
|
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: 284.97 E-value: 1.54e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAA--LPAWANKPPLQRVRIMNKFLALMNQHRDELA 90
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 91 AIITAEHGKVFTDAQGEVSRGIDIIEFACGipqLLKGDYTEQVST--NIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPV 168
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAG---LATKETGEVYDVppHVISRTVREPVGVCGLITPWNYPLLQAAWKLAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 169 AIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNG 247
Cdd:cd07119 158 ALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 248 KRVQ-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEM 326
Cdd:cd07119 238 KKVAlELGG-KNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 327 GPIVTAEALKRIEDYVQIGVDEGATLVVDGRGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGL 406
Cdd:cd07119 317 GPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAI 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534885945 407 NLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINV--PIPVPMAWhgfGGWKASLFGdmHAYGEEGVRFYTRQKSI 483
Cdd:cd07119 397 RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDyhPYFAEAPW---GGYKQSGIG--RELGPTGLEEYQETKHI 470
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-483 |
4.66e-90 |
|
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: 282.85 E-value: 4.66e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 12 HFINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAA 91
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 92 IITAEHG---KVFTDAQgeVSRGIDIIEFAcgIPQLLKGDYTEQVSTNIdnwTLRQPVGVVAGITPFNFPC-MVPCWMFP 167
Cdd:cd07138 81 AITLEMGapiTLARAAQ--VGLGIGHLRAA--ADALKDFEFEERRGNSL---VVREPIGVCGLITPWNWPLnQIVLKVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 168 vAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARN 246
Cdd:cd07138 154 -ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEAAADT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 247 GKRV-QALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAE 325
Cdd:cd07138 233 VKRVaLELGG-KSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 326 MGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGqKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEG 405
Cdd:cd07138 312 LGPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534885945 406 LNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMAwhGFGGWKASlfGDMHAYGEEGVRFYTRQKSI 483
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGA--PFGGYKQS--GNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
29-472 |
3.28e-89 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 280.37 E-value: 3.28e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEV 108
Cdd:cd07150 3 DLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 109 SRGIDIIEFACGIPQLLKG-----DYTEQVSTnidnwTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSER 183
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGetlpsDSPGTVSM-----SVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 184 DPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQALGGAKNHLLV 262
Cdd:cd07150 158 TPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 263 MPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYV 342
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 343 QIGVDEGATLVVDGRgqkpagfENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYT 422
Cdd:cd07150 318 EDAVAKGAKLLTGGK-------YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILT 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534885945 423 RDGNVAREFGRQVQVGMVGINVP-----IPVPmawhgFGGWKASLFG------DMHAYGEE 472
Cdd:cd07150 391 NDLQRAFKLAERLESGMVHINDPtildeAHVP-----FGGVKASGFGreggewSMEEFTEL 446
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
13-461 |
4.53e-89 |
|
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: 281.80 E-value: 4.53e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSiaGSKTANVFNPS-----LGTVARqvelADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRD 87
Cdd:cd07124 36 VIGGKEVR--TEEKIESRNPAdpsevLGTVQK----ATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 88 ELAAIITAEHGKVFTDAQGEVSRGIDIIEFACGipQLLKGD-YTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMF 166
Cdd:cd07124 110 ELAAWMVLEVGKNWAEADADVAEAIDFLEYYAR--EMLRLRgFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 167 PVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYE---- 241
Cdd:cd07124 188 TAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYEraak 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 242 --TGARNGKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDG 319
Cdd:cd07124 268 vqPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 320 MDLSAEMGPIVTAEALKRIEDYVQIGVDEGaTLVVDGRGqkPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRV 399
Cdd:cd07124 348 EDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEV--LELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKA 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534885945 400 ANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIpvPMAW---HGFGGWKAS 461
Cdd:cd07124 425 KDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKI--TGALvgrQPFGGFKMS 487
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
49-464 |
1.28e-88 |
|
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: 278.26 E-value: 1.28e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 49 VNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGD 128
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 129 YTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFM-ARLLKEAGLPDGVFNV 207
Cdd:cd07104 82 ILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLiAEIFEEAGLPKGVLNV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 208 VHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGE 285
Cdd:cd07104 162 VPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVAlELGG-NNPLIVLDDADLDLAVSAAAFGAFLHQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 286 RCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRgqkpagfE 365
Cdd:cd07104 241 ICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT-------Y 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 366 NGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGIN-V 444
Cdd:cd07104 314 EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINdQ 393
|
410 420
....*....|....*....|....
gi 2534885945 445 PIP----VPmawhgFGGWKASLFG 464
Cdd:cd07104 394 TVNdephVP-----FGGVKASGGG 412
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
29-483 |
2.58e-87 |
|
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: 275.72 E-value: 2.58e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEV 108
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 109 SRGIDIIEFACGIPQLLKGDYTEQVSTNIdNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAG 188
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPGGSF-AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 189 NFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVMPDAD 267
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTlELGG-KSPLIIFDDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 268 LNQVTDALIGAAYGSAGERCM-AISVAVMVGdVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGV 346
Cdd:cd07090 239 LENAVNGAMMANFLSQGQVCSnGTRVFVQRS-IKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 347 DEGATLVVDGRGQKP-AGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDG 425
Cdd:cd07090 318 QEGAKVLCGGERVVPeDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDL 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534885945 426 NVAREFGRQVQVGMVGIN----VPIPVPmawhgFGGWKASLFGDMHayGEEGVRFYTRQKSI 483
Cdd:cd07090 398 QRAHRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
13-483 |
2.64e-85 |
|
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: 270.99 E-value: 2.64e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEA--AKAALPAWANKPPLQRVRIMNKFLALMNQHRDELA 90
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAarRAFDNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 91 AIITAEHG---KVFTDAQGEVSRGI--DIIEFACGIPqllkgdYTEQVSTNIDNWTL--RQPVGVVAGITPFNFPCMVPC 163
Cdd:cd07139 82 RLWTAENGmpiSWSRRAQGPGPAALlrYYAALARDFP------FEERRPGSGGGHVLvrREPVGVVAAIVPWNAPLFLAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 164 WMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETG 243
Cdd:cd07139 156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 244 ARNGKRVQ-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDL 322
Cdd:cd07139 236 GERLARVTlELGG-KSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 323 SAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDgrGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANF 402
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTG--GGRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 403 TEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMAwhGFGGWKASLFGdmHAYGEEGVRFYTRQKS 482
Cdd:cd07139 393 DDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFGA--PFGGFKQSGIG--REGGPEGLDAYLETKS 468
|
.
gi 2534885945 483 I 483
Cdd:cd07139 469 I 469
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
67-483 |
2.06e-84 |
|
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: 268.34 E-value: 2.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 67 PPLQRVRIMNKFLALMNQHRDELAAIITAEHGK-VFTDAQGEVSRGIDIIEFACGipQLLKGDYTEQVSTNIDNWTL--- 142
Cdd:cd07089 40 DAEERARCLRQLHEALEARKEELRALLVAEVGApVMTARAMQVDGPIGHLRYFAD--LADSFPWEFDLPVPALRGGPgrr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 143 ---RQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHG-DKLAVETL 218
Cdd:cd07089 118 vvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGsDNAVGEAL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 219 LNHPDVAALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVG 297
Cdd:cd07089 198 TTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLlELGG-KSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPR 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 298 DVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRgqKPAGFENGFYTGGTLFDN 377
Cdd:cd07089 277 SRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGG--RPAGLDKGFYVEPTLFAD 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 378 VKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINvpipvPMAWHG--- 454
Cdd:cd07089 355 VDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN-----GGGGYGpda 429
|
410 420 430
....*....|....*....|....*....|
gi 2534885945 455 -FGGWKASLFGdmHAYGEEGVRFYTRQKSI 483
Cdd:cd07089 430 pFGGYKQSGLG--RENGIEGLEEFLETKSI 457
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
29-483 |
4.32e-84 |
|
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: 267.15 E-value: 4.32e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEV 108
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 109 SRGIDIIEFACGIPQLLKGdytEQV----STNIDN---WTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPS 181
Cdd:cd07149 83 DRAIETLRLSAEEAKRLAG---ETIpfdaSPGGEGrigFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 182 ERDPSAGNFMARLLKEAGLPDGVFNVVHGD-KLAVETLLNHPDVAALSFVGSTPIAKFIYETGARngKRVQALGGAKNHL 260
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSgETVGDALVTDPRVRMISFTGSPAVGEAIARKAGL--KKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 261 LVMPDADLNQVTDALIGAAYGSAGERCmaISVA-VMV-GDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRI 338
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVC--ISVQrIFVhEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 339 EDYVQIGVDEGATLVVDGRgqkpagFENGFYTGgTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGV 418
Cdd:cd07149 316 EEWVEEAVEGGARLLTGGK------RDGAILEP-TVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQA 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 419 SCYTRDGNVAREFGRQVQVGMVGINvPIPVPMAWH-GFGGWKASlfgdmhAYGEEGVRF----YTRQKSI 483
Cdd:cd07149 389 GVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHmPYGGVKES------GTGREGPRYaieeMTEIKLV 451
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
29-485 |
1.02e-83 |
|
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: 266.14 E-value: 1.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEV 108
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 109 SRGIDIIEFACGIPQLLKGDYTEQV---STNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDP 185
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAVplpSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 186 SAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQALGGAKNHLLVMP 264
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAgAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 265 DADLNQVTDALIGAAYGSAGERCMAISvAVMVGD-VGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQ 343
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATS-RLLVHEsIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 344 IGVDEGATLVVDGRgqKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLsCVR-VANFTEGLNLINSHQYGNGVSCYT 422
Cdd:cd07110 320 RGKEEGARLLCGGR--RPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVL-CVRsFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534885945 423 RDGNVAREFGRQVQVGMVGINVPIPV-PMA-WhgfGGWKASLFGdmHAYGEEGVRFYTRQKSIMQ 485
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCfPQApW---GGYKRSGIG--RELGEWGLDNYLEVKQITR 456
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
8-483 |
4.17e-83 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 265.59 E-value: 4.17e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 8 QTVAHFINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRD 87
Cdd:PRK13252 5 PLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 88 ELAAIITAEHGKVFTDAQ-GEVSRGIDIIEFACGIPQLLKGdytEQVSTNIDNW--TLRQPVGVVAGITPFNFPCMVPCW 164
Cdd:PRK13252 85 ELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEG---EQIPLRGGSFvyTRREPLGVCAGIGAWNYPIQIACW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 165 MFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETGA 244
Cdd:PRK13252 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 245 RNGKRV-QALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAiSVAVMV-GDVGDKLIPKLAARLKTLKVTDGMDL 322
Cdd:PRK13252 242 ASLKEVtMELGG-KSPLIVFDDADLDRAADIAMLANFYSSGQVCTN-GTRVFVqKSIKAAFEARLLERVERIRIGDPMDP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 323 SAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLS------- 395
Cdd:PRK13252 320 ATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSvltfdde 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 396 --CVRVANFTEglnlinshqYGNGVSCYTRDGNVAREFGRQVQVGMVGINV----PIPVPmawhgFGGWKASLFGDMHay 469
Cdd:PRK13252 400 deVIARANDTE---------YGLAAGVFTADLSRAHRVIHQLEAGICWINTwgesPAEMP-----VGGYKQSGIGREN-- 463
|
490
....*....|....
gi 2534885945 470 GEEGVRFYTRQKSI 483
Cdd:PRK13252 464 GIATLEHYTQIKSV 477
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
29-483 |
7.56e-83 |
|
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: 264.10 E-value: 7.56e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANK-PPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGE 107
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 108 VSRGIDIIEFACGIPQLLKGDyTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSA 187
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGE-TIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 188 GNFMARLLKEAGLPDGVFNVVHGdkLAVET---LLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVM 263
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTG--LGAEAgaaLVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTlELGG-KSPQIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 264 PDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDlSAEMGPIVTAEALKRIEDYVQ 343
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 344 IGVDEGATLVVDGRGQKPAGfENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTR 423
Cdd:cd07109 316 RARARGARIVAGGRIAEGAP-AGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534885945 424 DGNVAREFGRQVQVGMVGINV-----PIPVPmawhgFGGWKASLFGdmHAYGEEGVRFYTRQKSI 483
Cdd:cd07109 395 DGDRALRVARRLRAGQVFVNNygaggGIELP-----FGGVKKSGHG--REKGLEALYNYTQTKTV 452
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
29-484 |
1.56e-82 |
|
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: 262.85 E-value: 1.56e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEV 108
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 109 SRGIDIIEFACGI---PQLLKGDYTEQVStnidnwTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDP 185
Cdd:cd07106 81 GGAVAWLRYTASLdlpDEVIEDDDTRRVE------LRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 186 SAGNFMARLLKEAgLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVMP 264
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTlELGG-NDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 265 DADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQI 344
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 345 GVDEGATlVVDGrGQKPAGfeNGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRD 424
Cdd:cd07106 313 AKAKGAK-VLAG-GEPLDG--PGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSD 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534885945 425 GNVAREFGRQVQVGMVGINVPIPV-PMAWhgFGGWKASLFGdmHAYGEEGVRFYTRQKSIM 484
Cdd:cd07106 389 LERAEAVARRLEAGTVWINTHGALdPDAP--FGGHKQSGIG--VEFGIEGLKEYTQTQVIN 445
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
29-483 |
1.86e-82 |
|
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: 263.14 E-value: 1.86e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEV 108
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 109 SRGIDIIEFACGIPQLLKGDY----TEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERD 184
Cdd:cd07094 83 DRAIDTLRLAAEEAERIRGEEipldATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 185 PSAGNFMARLLKEAGLPDGVFNVVHGDK-LAVETLLNHPDVAALSFVGSTPIAKFIYETGArnGKRVQALGGAKNHLLVM 263
Cdd:cd07094 163 PLSALELAKILVEAGVPEGVLQVVTGEReVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 264 PDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQ 343
Cdd:cd07094 241 RDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 344 IGVDEGATLVV----DGRGQKPagfengfytggTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVS 419
Cdd:cd07094 321 EAVEAGARLLCggerDGALFKP-----------TVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534885945 420 CYTRDGNVAREFGRQVQVGMVGINVPIPVPMAWHGFGGWKASlfgdmhAYGEEGVRF----YTRQKSI 483
Cdd:cd07094 390 IFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKES------GVGREGVPYameeMTEEKTV 451
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
29-475 |
3.33e-81 |
|
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: 259.97 E-value: 3.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEV 108
Cdd:cd07145 3 VRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 109 SRGIDIIEFACGIPQLLKGDYTeqvstNIDNW---------TLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILK 179
Cdd:cd07145 83 ERTIRLFKLAAEEAKVLRGETI-----PVDAYeynerriafTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 180 PSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQ-ALGGAk 257
Cdd:cd07145 158 PSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVAlELGGS- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 258 NHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKR 337
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 338 IEDYVQIGVDEGATLVVDGRGQKpagfenGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNG 417
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKRDE------GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQ 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2534885945 418 VSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMAWHGFGGWKASlfgdmhAYGEEGVR 475
Cdd:cd07145 391 ASVFTNDINRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKS------GIGREGVR 442
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
29-484 |
9.16e-81 |
|
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: 258.41 E-value: 9.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTD-AQGE 107
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 108 VSRGIDIIEFACG----IPQLLKGDYTEQVSTNIdnwtLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSER 183
Cdd:cd07092 81 LPGAVDNFRFFAGaartLEGPAAGEYLPGHTSMI----RREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 184 DPSAGNFMARLLKEaGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLL 261
Cdd:cd07092 157 TPLTTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHlELGG-KAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 262 VMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDY 341
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 342 VQiGVDEGATLVVDGRgqkpAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCY 421
Cdd:cd07092 315 VE-RAPAHARVLTGGR----RAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVW 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534885945 422 TRDGNVAREFGRQVQVGMVGINVPIPVP--MAWhgfGGWKASLFG-DMHAYGEEGvrfYTRQKSIM 484
Cdd:cd07092 390 TRDVGRAMRLSARLDFGTVWVNTHIPLAaeMPH---GGFKQSGYGkDLSIYALED---YTRIKHVM 449
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
29-483 |
1.29e-80 |
|
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: 258.06 E-value: 1.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAAlpawanKPPL---QRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQ 105
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALAASY------RSTLtryQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 106 GEVSRGIDIIEFAcgIPQLLKGDyTEQVSTNIDN-------WTLRQPVGVVAGITPFNFPC-MVPCWMFPvAIACGNTFI 177
Cdd:cd07146 77 YEVGRAADVLRFA--AAEALRDD-GESFSCDLTAngkarkiFTLREPLGVVLAITPFNHPLnQVAHKIAP-AIAANNRIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 178 LKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGD-KLAVETLLNHPDVAALSFVGSTPIAKFIYETGArnGKR-VQALGG 255
Cdd:cd07146 153 LKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRqLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 256 aKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEAL 335
Cdd:cd07146 231 -NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 336 KRIEDYVQIGVDEGATLVVDGRgqkpagfENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYG 415
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQ-------RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYG 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534885945 416 NGVSCYTRDGNVAREFGRQVQVGMVGIN-VP------IPvpmawhgFGGWKASLFGdmhayGEEGVR----FYTRQKSI 483
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVNeVPgfrselSP-------FGGVKDSGLG-----GKEGVReamkEMTNVKTY 449
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
13-490 |
2.48e-79 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 256.29 E-value: 2.48e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAwaNKPP----LQRVRIMNKFLALMNQHRDE 88
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDH--GPWPrmsgFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 89 LAAIITAEHGKVFTDAQG-EVSRGIDIIEFACGIPQLLKGDyTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFP 167
Cdd:PLN02766 102 LAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGE-TLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 168 VAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHG-DKLAVETLLNHPDVAALSFVGSTPIAKFIYETGAR- 245
Cdd:PLN02766 181 PALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATs 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 246 NGKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAIS-VAVMVGdVGDKLIPKLAARLKTLKVTDGMDLSA 324
Cdd:PLN02766 261 NLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSrVYVQEG-IYDEFVKKLVEKAKDWVVGDPFDPRA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 325 EMGPIVTAEALKRIEDYVQIGVDEGATLVVDGrgqKPAGfENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTE 404
Cdd:PLN02766 340 RQGPQVDKQQFEKILSYIEHGKREGATLLTGG---KPCG-DKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 405 GLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIP----VPmawhgFGGWKASLFG-DMhayGEEGVRFYTR 479
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAfdpdCP-----FGGYKMSGFGrDQ---GMDALDKYLQ 487
|
490
....*....|.
gi 2534885945 480 QKSIMQRWPDS 490
Cdd:PLN02766 488 VKSVVTPLYNS 498
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
13-464 |
2.79e-79 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 256.16 E-value: 2.79e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAI 92
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 93 ITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIAC 172
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 173 GNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQ 251
Cdd:PLN02278 188 GCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 252 ALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVT 331
Cdd:PLN02278 268 LELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLIN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 332 AEALKRIEDYVQIGVDEGATLVVDGRGQKPAGfenGFYTgGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINS 411
Cdd:PLN02278 348 EAAVQKVESHVQDAVSKGAKVLLGGKRHSLGG---TFYE-PTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAND 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2534885945 412 HQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIpVPMAWHGFGGWKASLFG 464
Cdd:PLN02278 424 TEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLG 475
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
13-483 |
4.80e-79 |
|
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: 254.80 E-value: 4.80e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGsKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPL-QRVRIMNKFLALMNQHRDELAA 91
Cdd:cd07082 5 LINGEWKESSG-KTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLeERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 92 IITAEHGKVFTDAQGEVSRGIDIIEFACG-----IPQLLKGDYTEQVStNIDNWTLRQPVGVVAGITPFNFPCMVP-CWM 165
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRDTIEelkrlDGDSLPGDWFPGTK-GKIAQVRREPLGVVLAIGPFNYPLNLTvSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 166 FPVAIAcGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGD-KLAVETLLNHPDVAALSFVGSTPIAKFIYETGA 244
Cdd:cd07082 163 IPALIM-GNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 245 RngKRVQaLG-GAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLS 323
Cdd:cd07082 242 M--KRLV-LElGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 324 AEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGQKpagfENGFYTggTLFDNVKPNMRIYLEEIFGPVLSCVRVANFT 403
Cdd:cd07082 319 VDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG----GNLIYP--TLLDPVTPDMRLAWEEPFGPVLPIIRVNDIE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 404 EGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINvpipvPMAWHG-----FGGWKASlfgdmhAYGEEGV---- 474
Cdd:cd07082 393 EAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN-----SKCQRGpdhfpFLGRKDS------GIGTQGIgdal 461
|
....*....
gi 2534885945 475 RFYTRQKSI 483
Cdd:cd07082 462 RSMTRRKGI 470
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
13-483 |
6.03e-79 |
|
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: 254.73 E-value: 6.03e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWA--NKPPLQRVRIMNKFLALMNQHRDELA 90
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPwpRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 91 AIITAEHGKVFTDA-QGEVSRGIDIIEFACGIPQLLKGDyTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVA 169
Cdd:cd07142 87 ALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGM-TLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 170 IACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHG-DKLAVETLLNHPDVAALSFVGSTPIAKFIYETGAR-NG 247
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 248 KRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMG 327
Cdd:cd07142 246 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 328 PIVTAEALKRIEDYVQIGVDEGATLVVDGR--GQKpagfenGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEG 405
Cdd:cd07142 326 PQVDKEQFEKILSYIEHGKEEGATLITGGDriGSK------GYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 406 LNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGIN------VPIPvpmawhgFGGWKASLFGdmHAYGEEGVRFYTR 479
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcydvfdASIP-------FGGYKMSGIG--REKGIYALNNYLQ 470
|
....
gi 2534885945 480 QKSI 483
Cdd:cd07142 471 VKAV 474
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
13-487 |
6.13e-79 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 254.45 E-value: 6.13e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGsKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAI 92
Cdd:PRK13473 6 LINGELVAGEG-EKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 93 ITAEHGKVFTDA-QGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIA 171
Cdd:PRK13473 85 ESLNCGKPLHLAlNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 172 CGNTFILKPSERDPSAGNFMARLLKEAgLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRV 250
Cdd:PRK13473 165 AGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 251 Q-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPI 329
Cdd:PRK13473 244 HlELGG-KAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 330 VTAEALKRIEDYVQIGVDEGATLVVDGrGQKPAGfeNGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLI 409
Cdd:PRK13473 323 ISAAHRDRVAGFVERAKALGHIRVVTG-GEAPDG--KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 410 NSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPV----PmawHgfGGWKASLFG-DMHAYG-EEgvrfYTRQKSI 483
Cdd:PRK13473 400 NDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLvsemP---H--GGQKQSGYGkDMSLYGlED----YTVVRHV 470
|
....
gi 2534885945 484 MQRW 487
Cdd:PRK13473 471 MVKH 474
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
29-483 |
7.32e-79 |
|
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: 253.84 E-value: 7.32e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEV 108
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 109 SRGIDIIEFACGIPQLLKGDyTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAG 188
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGE-TIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 189 NFMARLLKEAgLPDGVFNVVHGD-KLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQALGGAKNHLLVMPDAD 267
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDgATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 268 LNQVTDALI-GAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGV 346
Cdd:cd07107 239 PEAAADAAVaGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 347 DEGATLVVDGRGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGN 426
Cdd:cd07107 319 REGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534885945 427 VAREFGRQVQVGMVGIN--------VPipvpmawhgFGGWKASLFGDMHAYGEegVRFYTRQKSI 483
Cdd:cd07107 399 QAHRTARRVEAGYVWINgssrhflgAP---------FGGVKNSGIGREECLEE--LLSYTQEKNV 452
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
5-483 |
3.46e-77 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 250.14 E-value: 3.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 5 KNDQTVAHFINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAA--LPAWANKPPLQRVRIMNKFLALM 82
Cdd:cd07143 2 KYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfeTDWGLKVSGSKRGRCLSKLADLM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 83 NQHRDELAAIITAEHGKVF-TDAQGEVSRGIDIIEFACGIPQllkGDYTEQVSTNIDN--WTLRQPVGVVAGITPFNFPC 159
Cdd:cd07143 82 ERNLDYLASIEALDNGKTFgTAKRVDVQASADTFRYYGGWAD---KIHGQVIETDIKKltYTRHEPIGVCGQIIPWNFPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 160 MVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGD-KLAVETLLNHPDVAALSFVGSTPIAKF 238
Cdd:cd07143 159 LMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYgRTCGNAISSHMDIDKVAFTGSTLVGRK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 239 IYETGAR-NGKRVQALGGAKNHLLVMPDADLNQvtdALIGAAYG---SAGERCMAISVAVMVGDVGDKLIPKLAARLKTL 314
Cdd:cd07143 239 VMEAAAKsNLKKVTLELGGKSPNIVFDDADLES---AVVWTAYGiffNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 315 KVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGrgqKPAGFEnGFYTGGTLFDNVKPNMRIYLEEIFGPVL 394
Cdd:cd07143 316 KVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGG---KRHGNE-GYFIEPTIFTDVTEDMKIVKEEIFGPVV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 395 SCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGIN----VPIPVPmawhgFGGWKASLFGdmHAYG 470
Cdd:cd07143 392 AVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcynlLHHQVP-----FGGYKQSGIG--RELG 464
|
490
....*....|...
gi 2534885945 471 EEGVRFYTRQKSI 483
Cdd:cd07143 465 EYALENYTQIKAV 477
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
7-482 |
5.02e-77 |
|
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: 249.62 E-value: 5.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 7 DQTVAHFINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHR 86
Cdd:cd07111 19 DRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 87 DELAAIITAEHGKVFTDaqgevSRGIDI------IEFACGIPQLLKgdyteqvsTNIDNWtlrQPVGVVAGITPFNFPCM 160
Cdd:cd07111 99 RLFAVLESLDNGKPIRE-----SRDCDIplvarhFYHHAGWAQLLD--------TELAGW---KPVGVVGQIVPWNFPLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 161 VPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIY 240
Cdd:cd07111 163 MLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 241 ETGARNGKRVQ-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDG 319
Cdd:cd07111 243 RATAGTGKKLSlELGG-KSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 320 MDLSAEMGPIVTAEALKRIEDYVQIGVDEGATlvvdgRGQKPAGF-ENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVR 398
Cdd:cd07111 322 LDKAIDMGAIVDPAQLKRIRELVEEGRAEGAD-----VFQPGADLpSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 399 VANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVpipvpmawH-------GFGGWKASLFGdmHAYGE 471
Cdd:cd07111 397 FRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING--------HnlfdaaaGFGGYRESGFG--REGGK 466
|
490
....*....|.
gi 2534885945 472 EGVRFYTRQKS 482
Cdd:cd07111 467 EGLYEYLRPSW 477
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
13-483 |
5.56e-77 |
|
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: 249.57 E-value: 5.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWA---NKPPLQRVRIMNKFLALMNQHRDEL 89
Cdd:cd07141 10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSpwrTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 90 AAIITAEHGKVFTDAQ-GEVSRGIDIIEFACGIPQLLKGDyTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPV 168
Cdd:cd07141 90 ASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGK-TIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 169 AIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHG-DKLAVETLLNHPDVAALSFVGSTPIAKFIYE-TGARN 246
Cdd:cd07141 169 ALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQaAGKSN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 247 GKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEM 326
Cdd:cd07141 249 LKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 327 GPIVTAEALKRIEDYVQIGVDEGATLVVDGrgqKPAGfENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGL 406
Cdd:cd07141 329 GPQIDEEQFKKILELIESGKKEGAKLECGG---KRHG-DKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534885945 407 NLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPV-PMAwhGFGGWKASLFGdmHAYGEEGVRFYTRQKSI 483
Cdd:cd07141 405 ERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVsPQA--PFGGYKMSGNG--RELGEYGLQEYTEVKTV 478
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
35-461 |
1.02e-76 |
|
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: 247.59 E-value: 1.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 35 GTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRGIDI 114
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 115 IEFACGIPQLLKGdytEQVSTNIDNWTL--RQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFM- 191
Cdd:cd07152 81 LHEAAGLPTQPQG---EILPSAPGRLSLarRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVi 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 192 ARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVMPDADLNQ 270
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSlELGG-KNALIVLDDADLDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 271 VTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGA 350
Cdd:cd07152 237 AASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 351 TLVVDGRgqkpagFENGFYTgGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVARE 430
Cdd:cd07152 317 RLEAGGT------YDGLFYR-PTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2534885945 431 FGRQVQVGMVGIN---------VPipvpmawhgFGGWKAS 461
Cdd:cd07152 390 LADRLRTGMLHINdqtvndephNP---------FGGMGAS 420
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
65-464 |
9.48e-76 |
|
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: 244.68 E-value: 9.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 65 NKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRGIDIIEF-ACGIPQLLKGDYTEqvSTNIDNWTLR 143
Cdd:cd07100 17 KTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyAENAEAFLADEPIE--TDAGKAYVRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 144 QPVGVVAGITPFNFP------CMVPcwmfpvAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAVET 217
Cdd:cd07100 95 EPLGVVLGIMPWNFPfwqvfrFAAP------NLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 218 LLNHPDVAALSFVGSTPIAKFIYETGARNGKR-VQALGGAkNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMV 296
Cdd:cd07100 169 IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKsVLELGGS-DPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVH 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 297 GDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVdgRGQKPAGfeNGFYTGGTLFD 376
Cdd:cd07100 248 EDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLL--GGKRPDG--PGAFYPPTVLT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 377 NVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVP------IPvpm 450
Cdd:cd07100 324 DVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMvksdprLP--- 400
|
410
....*....|....
gi 2534885945 451 awhgFGGWKASLFG 464
Cdd:cd07100 401 ----FGGVKRSGYG 410
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
29-483 |
9.63e-76 |
|
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: 245.73 E-value: 9.63e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVF-TDAQGE 107
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 108 VSRGIDIIEFACGIPQLLKGDyTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSA 187
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGE-TLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 188 GNFMARLLKEAgLPDGVFNVVHG-DKLAVETLLNHPDVAALSFVGSTPIAKFIYETGArnGKRVQA---LGGaKNHLLVM 263
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA--DRLIPVsleLGG-KSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 264 PDADLNQVTDALI-GAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYV 342
Cdd:cd07108 236 PDADLDDAVDGAIaGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 343 QIGVDE-GATLVVDGRGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCY 421
Cdd:cd07108 316 DLGLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534885945 422 TRDGNVAREFGRQVQVGMVGINVPIpVPMAWHGFGGWKASLFGdmHAYGEEG-VRFYTRQKSI 483
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLG--REASLEGmLEHFTQKKTV 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
22-464 |
1.42e-74 |
|
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: 242.60 E-value: 1.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 22 AGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVF 101
Cdd:cd07151 7 TSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 102 TDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPS 181
Cdd:cd07151 87 IKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 182 ERDP-SAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKN 258
Cdd:cd07151 167 SDTPiTGGLLLAKIFEEAGLPKGVLNVVVGAGSEIgDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVAlELGG-NN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 259 HLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRI 338
Cdd:cd07151 246 PFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 339 EDYVQIGVDEGATLVVDGRGQkpagfenGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGV 418
Cdd:cd07151 326 LDKIEQAVEEGATLLVGGEAE-------GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSG 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2534885945 419 SCYTRDGNVAREFGRQVQVGMVGINvPIPV---PMAwhGFGGWKASLFG 464
Cdd:cd07151 399 AVFTSDLERGVQFARRIDAGMTHIN-DQPVndePHV--PFGGEKNSGLG 444
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
67-483 |
6.74e-74 |
|
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: 240.17 E-value: 6.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 67 PPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPV 146
Cdd:cd07105 20 PPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIPSDKPGTLAMVVKEPV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 147 GVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKL----AVETLLNHP 222
Cdd:cd07105 100 GVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSPEdapeVVEALIAHP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 223 DVAALSFVGSTPIAKFIYETGARNGKRV-QALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGD 301
Cdd:cd07105 180 AVRKVNFTGSTRVGRIIAETAAKHLKPVlLELGG-KAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 302 KLIPKLAARLKtlKVTDGmdlSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVdgrGQKPAGFENGFYTGGTLFDNVKPN 381
Cdd:cd07105 259 EFVEKLKAAAE--KLFAG---PVVLGSLVSAAAADRVKELVDDALSKGAKLVV---GGLADESPSGTSMPPTILDNVTPD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 382 MRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVP-------IPvpmawhg 454
Cdd:cd07105 331 MDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMtvhdeptLP------- 403
|
410 420
....*....|....*....|....*....
gi 2534885945 455 FGGWKASLFGDMHayGEEGVRFYTRQKSI 483
Cdd:cd07105 404 HGGVKSSGYGRFN--GKWGIDEFTETKWI 430
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
14-487 |
1.94e-73 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 241.38 E-value: 1.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 14 INGNTVSiaGSKTANVFNPS-----LGTVARqvelADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDE 88
Cdd:PRK03137 41 IGGERIT--TEDKIVSINPAnksevVGRVSK----ATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 89 LAAIITAEHGKVFTDAQGEVSRGIDIIEFACgiPQLLKGDYTEQVST--NIDNWTLRQPVGVVAGITPFNFPCMVPCWMF 166
Cdd:PRK03137 115 FSAWLVKEAGKPWAEADADTAEAIDFLEYYA--RQMLKLADGKPVESrpGEHNRYFYIPLGVGVVISPWNFPFAIMAGMT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 167 PVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGAR 245
Cdd:PRK03137 193 LAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFITFTGSREVGLRIYERAAK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 246 --NG----KRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDG 319
Cdd:PRK03137 273 vqPGqiwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 320 MDlSAEMGPIVTAEALKRIEDYVQIGVDEGaTLVVDGRGqkpaGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRV 399
Cdd:PRK03137 353 ED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEG----DDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 400 ANFTEGLNLINSHQYGNGVSCYTRDG---NVARE--------FGRQVQVGMVGinvpipvpmaWHGFGGWKASlfG-DMH 467
Cdd:PRK03137 427 KDFDHALEIANNTEYGLTGAVISNNRehlEKARRefhvgnlyFNRGCTGAIVG----------YHPFGGFNMS--GtDSK 494
|
490 500
....*....|....*....|
gi 2534885945 468 AYGEEGVRFYTRQKSIMQRW 487
Cdd:PRK03137 495 AGGPDYLLLFLQAKTVSEMF 514
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
29-482 |
1.76e-71 |
|
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: 234.45 E-value: 1.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEV 108
Cdd:cd07147 3 VTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 109 SRGIDIIEFACGIP-----QLLKGDYTEQvSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSER 183
Cdd:cd07147 83 ARAIDTFRIAAEEAtriygEVLPLDISAR-GEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 184 DPSAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAkfiYETGARNGKR--VQALGGAKNhLL 261
Cdd:cd07147 162 TPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVG---WDLKARAGKKkvVLELGGNAA-VI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 262 VMPDADLNQVTDALIGAAYGSAGERCmaISVA-VMV-GDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIE 339
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSC--ISVQrVLVhRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 340 DYVQIGVDEGATLVVDGRgqkpagfENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVS 419
Cdd:cd07147 316 GWVNEAVDAGAKLLTGGK-------RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAG 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534885945 420 CYTRDGNVAREFGRQVQVGMVGIN-VPI----PVPmawhgFGGWKASLFgdmhayGEEGVRF----YTRQKS 482
Cdd:cd07147 389 VFTRDLEKALRAWDELEVGGVVINdVPTfrvdHMP-----YGGVKDSGI------GREGVRYaieeMTEPRL 449
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
13-483 |
2.09e-71 |
|
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: 235.08 E-value: 2.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAA--LPAWANKPPLQRVRIMNKFLALMNQHRDELA 90
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 91 AIITAEHGKVFTDA-QGEVSRGIDIIEFACGIPQLLKGDyTEQVSTNIDN----WTLRQPVGVVAGITPFNFPCMVPCWM 165
Cdd:cd07140 89 TIESLDSGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGK-TIPINQARPNrnltLTKREPIGVCGIVIPWNYPLMMLAWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 166 FPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGD-KLAVETLLNHPDVAALSFVGSTPIAKFIYETGA 244
Cdd:cd07140 168 MAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSgSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 245 -RNGKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLS 323
Cdd:cd07140 248 vSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 324 AEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRgQKPagfENGFYTGGTLFDNVKPNMRIYLEEIFGPVLScvrVANFT 403
Cdd:cd07140 328 TDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGK-QVD---RPGFFFEPTVFTDVEDHMFIAKEESFGPIMI---ISKFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 404 EG-----LNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMAwHGFGGWKASLFG-DMhayGEEGVRFY 477
Cdd:cd07140 401 DGdvdgvLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVA-APFGGFKQSGFGkDL---GEEALNEY 476
|
....*.
gi 2534885945 478 TRQKSI 483
Cdd:cd07140 477 LKTKTV 482
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
12-464 |
2.31e-71 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 236.63 E-value: 2.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 12 HFINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWA--NKPPLQRVRIMNKFLALMNQHRDEL 89
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPwpKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 90 AAIITAEHGKVFTD-AQGEVSRGIDIIEFACGIPQLLKGdYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPV 168
Cdd:PLN02466 140 AALETWDNGKPYEQsAKAELPMFARLFRYYAGWADKIHG-LTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 169 AIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHG-DKLAVETLLNHPDVAALSFVGSTPIAKFIYETGAR-N 246
Cdd:PLN02466 219 ALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKsN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 247 GKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEM 326
Cdd:PLN02466 299 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 327 GPIVTAEALKRIEDYVQIGVDEGATLVVDGR--GQKpagfenGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTE 404
Cdd:PLN02466 379 GPQIDSEQFEKILRYIKSGVESGATLECGGDrfGSK------GYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDE 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534885945 405 GLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGIN------VPIPvpmawhgFGGWKASLFG 464
Cdd:PLN02466 453 VIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfdAAIP-------FGGYKMSGIG 511
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
31-483 |
1.02e-70 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 232.50 E-value: 1.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 31 NPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSR 110
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 111 GIDIIEFACG-IPQLLKgdyTEQVST-----NIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERD 184
Cdd:cd07099 82 ALEAIDWAARnAPRVLA---PRKVPTgllmpNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 185 PSAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPdVAALSFVGSTPIAKFIYETGARNGKRVQA-LGGaKNHLLVM 263
Cdd:cd07099 159 PLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLeLGG-KDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 264 PDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQ 343
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 344 IGVDEGATLVVDGrgqkPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTR 423
Cdd:cd07099 317 DAVAKGAKALTGG----ARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534885945 424 DGNVAREFGRQVQVGMVGINVPIPVPMAWHG-FGGWKASLFGDMHayGEEGVRFYTRQKSI 483
Cdd:cd07099 393 DLARAEAIARRLEAGAVSINDVLLTAGIPALpFGGVKDSGGGRRH--GAEGLREFCRPKAI 451
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
13-464 |
1.22e-70 |
|
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: 233.00 E-value: 1.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAI 92
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 93 ITAEHGKVFTDaqgevSRGIDI---IE----FACGIpqllKGDytEQVSTNIDNWTL----RQPVGVVAGITPFNFPCMV 161
Cdd:cd07559 84 ETLDNGKPIRE-----TLAADIplaIDhfryFAGVI----RAQ--EGSLSEIDEDTLsyhfHEPLGVVGQIIPWNFPLLM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 162 PCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAgLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIY 240
Cdd:cd07559 153 AAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAgKPLASHPRIAKLAFTGSTTVGRLIM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 241 ETGARNGKRVQ-ALGGaKNHLLVMPDADLNQVT--DALIGAAYGSA---GERCMAISVAVMVGDVGDKLIPKLAARLKTL 314
Cdd:cd07559 232 QYAAENLIPVTlELGG-KSPNIFFDDAMDADDDfdDKAEEGQLGFAfnqGEVCTCPSRALVQESIYDEFIERAVERFEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 315 KVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVL 394
Cdd:cd07559 311 KVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVL 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 395 SCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPmAWHGFGGWKASLFG 464
Cdd:cd07559 391 AVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYP-AHAPFGGYKKSGIG 459
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
31-484 |
2.48e-70 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 231.37 E-value: 2.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 31 NPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSR 110
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 111 GIDIIEFACGI-PQLLKgDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGN 189
Cdd:cd07102 82 MLERARYMISIaEEALA-DIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 190 FMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVMPDADL 268
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGlELGG-KDPAYVRPDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 269 NQVTDALI-GAAYGSaGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVD 347
Cdd:cd07102 240 DAAAESLVdGAFFNS-GQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 348 EGATLVVDGRGQkPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNV 427
Cdd:cd07102 319 KGARALIDGALF-PEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIAR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 428 AREFGRQVQVGMVGIN---VPIPVpMAWhgfGGWKASlfGDMHAYGEEGVRFYTRQKSIM 484
Cdd:cd07102 398 AEALGEQLETGTVFMNrcdYLDPA-LAW---TGVKDS--GRGVTLSRLGYDQLTRPKSYH 451
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
26-464 |
4.65e-70 |
|
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: 232.47 E-value: 4.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 26 TANVFNPSLG--TVARqVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTD 103
Cdd:cd07125 47 GAPVIDPADHerTIGE-VSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 104 AQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSER 183
Cdd:cd07125 126 ADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 184 DPSAGNFMARLLKEAGLPDGVFNVVHGD-KLAVETLLNHPDVAALSFVGSTPIAKFIYETGA-RNGKRVQ--ALGGAKNH 259
Cdd:cd07125 206 TPLIAARAVELLHEAGVPRDVLQLVPGDgEEIGEALVAHPRIDGVIFTGSTETAKLINRALAeRDGPILPliAETGGKNA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 260 LLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIE 339
Cdd:cd07125 286 MIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 340 DYVQIGVDEgATLVvdgrGQKPAGFENGFYTGGTLFDNVkpNMRIYLEEIFGPVLSCVRVANFT--EGLNLINSHQYGNG 417
Cdd:cd07125 366 AHTELMRGE-AWLI----APAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKAEDldEAIEDINATGYGLT 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2534885945 418 VSCYTRDGNVAREFGRQVQVGMVGINVPI--------PvpmawhgFGGWKASLFG 464
Cdd:cd07125 439 LGIHSRDEREIEYWRERVEAGNLYINRNItgaivgrqP-------FGGWGLSGTG 486
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
68-469 |
1.59e-69 |
|
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: 229.15 E-value: 1.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 68 PLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTE----QVSTnidnwTLR 143
Cdd:cd07120 41 PRLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARTEAGRMIEpepgSFSL-----VLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 144 QPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEA-GLPDGVFNVVHGDKLAV-ETLLNH 221
Cdd:cd07120 116 EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGaAHLVAS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 222 PDVAALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVG 300
Cdd:cd07120 196 PDVDVISFTGSTATGRAIMAAAAPTLKRLGlELGG-KTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 301 DKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGrGQKPAGFENGFYTGGTLFDNVKP 380
Cdd:cd07120 275 DEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRG-GPVTEGLAKGAFLRPTLLEVDDP 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 381 NMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVpipvpmawHG------ 454
Cdd:cd07120 354 DADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND--------WNklfaea 425
|
410
....*....|....*.
gi 2534885945 455 -FGGWKASLFGDMHAY 469
Cdd:cd07120 426 eEGGYRQSGLGRLHGV 441
|
|
| lactal_redase_Meth |
NF040648 |
lactaldehyde dehydrogenase; |
13-483 |
8.45e-69 |
|
lactaldehyde dehydrogenase;
Pssm-ID: 468615 [Multi-domain] Cd Length: 463 Bit Score: 227.57 E-value: 8.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSiagSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAI 92
Cdd:NF040648 2 FINGKWID---REDIDVINPYNLEVIDKIPSLSREEVKEAIEIANEAKEVMKNLSPRKRYNILMDIAEELKKNKEELAKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 93 ITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDyteqvSTNIDN---WTLRQPVGVVAGITPFNFPCMVPCWMFPVA 169
Cdd:NF040648 79 ITIDAGKPIKQSIIEVDRSIETFKLAAFYAKEIRGE-----TIPSDAgliFTKKEPLGVVGAITPFNYPLNLAAHKIAPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 170 IACGNTFILKPSERDPSAGNFMARL----LKEAGLPDGVFNVV--HGDKLAVETLLNhPDVAALSFVGSTPIAKFIyetg 243
Cdd:NF040648 154 IATGNSVVLHPSSKAPLAAIELAKIiekvLKKMNIPLGVFNLVtgYGEVVGDEIVKN-EKVNKISFTGSVEVGESI---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 244 ARNG--KRVQ-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGM 320
Cdd:NF040648 229 SKKAgmKKITlELGG-NNPLIVLKDADIEKAVESAVKGSFLNSGQVCISVGRVIVEEEIADEFIKKLVEETKKLKVGNPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 321 DLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGqkpagfENGFYTGGTLfdNVKPNMRIYLEEIFGPVLSCVRVA 400
Cdd:NF040648 308 DEKTDIGPLITEEAAIRVENLVNEAIEEGAKLLCGGNR------EGSLFYPTVL--DVDEDNILVKVETFGPVLPIIRVK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 401 NFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVP-------IPvpmawhgFGGWKASlfgdmhAYGEEG 473
Cdd:NF040648 380 DIDEAIEIANNTKYGLQAGVFTNDINKALKFADELEYGGVIINKSstfrtdnMP-------FGGFKKS------GLGKEG 446
|
490
....*....|....
gi 2534885945 474 VRF----YTRQKSI 483
Cdd:NF040648 447 IKYaveeMTEIKTI 460
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
13-461 |
1.09e-67 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 225.55 E-value: 1.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPslgtvARQVELADIA-----TVNKAVEAAKAALPAW--ANKPPLQRVRIMNKFLALMNQH 85
Cdd:PRK09847 23 FINGEYTAAAENETFETVDP-----VTQAPLAKIArgksvDIDRAVSAARGVFERGdwSLSSPAKRKAVLNKLADLMEAH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 86 RDELAAIITAEHGKVFTDA-QGEVSRGIDIIE-FACGIPQLlkgdYTEQVSTNIDNWTL--RQPVGVVAGITPFNFPCMV 161
Cdd:PRK09847 98 AEELALLETLDTGKPIRHSlRDDIPGAARAIRwYAEAIDKV----YGEVATTSSHELAMivREPVGVIAAIVPWNFPLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 162 PCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHG-DKLAVETLLNHPDVAALSFVGSTPIAK-FI 239
Cdd:PRK09847 174 TCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKqLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 240 YETGARNGKRVQALGGAKNHLLVMPDA-DLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTD 318
Cdd:PRK09847 254 KDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 319 GMDLSAEMGPIVTAEALKRIEDYVQIGVDEGaTLVVDGRGQKPAGfengfYTGGTLFDNVKPNMRIYLEEIFGPVLSCVR 398
Cdd:PRK09847 334 PLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-----AIGPTIFVDVDPNASLSREEIFGPVLVVTR 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534885945 399 VANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINV----PIPVPmawhgFGGWKAS 461
Cdd:PRK09847 408 FTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMTVP-----FGGYKQS 469
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
28-486 |
3.02e-66 |
|
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: 222.07 E-value: 3.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 28 NVFNPslGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGE 107
Cdd:cd07083 38 SPFAP--SEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 108 VSRGIDIIEFACGIPQLLKGDYTEQVS-TNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPS 186
Cdd:cd07083 116 VAEAIDFIRYYARAALRLRYPAVEVVPyPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 187 AGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNG------KRVQALGGAKNH 259
Cdd:cd07083 196 VGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLApgqtwfKRLYVETGGKNA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 260 LLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIE 339
Cdd:cd07083 276 IIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 340 DYVQIGVDEGATLVvdgRGQKPAGfeNGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRV--ANFTEGLNLINSHQYGNG 417
Cdd:cd07083 356 SYIEHGKNEGQLVL---GGKRLEG--EGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYkdDDFAEALEVANSTPYGLT 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 418 VSCYTRDGNVAREFGRQVQVGMVGINVPIP-VPMAWHGFGGWKASLFGDmHAYGEEGVRFYTRQKSIMQR 486
Cdd:cd07083 431 GGVYSRKREHLEEARREFHVGNLYINRKITgALVGVQPFGGFKLSGTNA-KTGGPHYLRRFLEMKAVAER 499
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
13-484 |
2.21e-64 |
|
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: 216.17 E-value: 2.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAI 92
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 93 ITAEHGKVFTDaqgevSRGIDII-------EFACGIpqllKGDytEQVSTNIDNWTL----RQPVGVVAGITPFNFPCMV 161
Cdd:cd07117 84 ETLDNGKPIRE-----TRAVDIPlaadhfrYFAGVI----RAE--EGSANMIDEDTLsivlREPIGVVGQIIPWNFPFLM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 162 PCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAgLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIY 240
Cdd:cd07117 153 AAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSgEYLLNHPGLDKLAFTGSTEVGRDVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 241 ETGARngKRVQA---LGGaKNHLLVMPDADLNQvtdALIGAAYG---SAGERCMAISVAVMVGDVGDKLIPKLAARLKTL 314
Cdd:cd07117 232 IAAAK--KLIPAtleLGG-KSANIIFDDANWDK---ALEGAQLGilfNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 315 KVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGQKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVL 394
Cdd:cd07117 306 KVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 395 SCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPmAWHGFGGWKASLFG-DMHAYGEEG 473
Cdd:cd07117 386 TVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIP-AGAPFGGYKKSGIGrETHKSMLDA 464
|
490
....*....|.
gi 2534885945 474 vrfYTRQKSIM 484
Cdd:cd07117 465 ---YTQMKNIY 472
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
18-487 |
2.81e-62 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 212.05 E-value: 2.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 18 TVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEH 97
Cdd:PRK09407 25 RVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 98 GKVFTDAQGEVSrgiDII----EFACGIPQLLK-----------GDYTEqvstnidnwtLRQPVGVVAGITPFNFPC--- 159
Cdd:PRK09407 105 GKARRHAFEEVL---DVAltarYYARRAPKLLAprrragalpvlTKTTE----------LRQPKGVVGVISPWNYPLtla 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 160 ---MVPcwmfpvAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVaaLSFVGSTPI 235
Cdd:PRK09407 172 vsdAIP------ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVgTALVDNADY--LMFTGSTAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 236 AKFIYETGARNGKRVQA-LGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTL 314
Cdd:PRK09407 244 GRVLAEQAGRRLIGFSLeLGG-KNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 315 KVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGQK---PAGFENgfytggTLFDNVKPNMRIYLEEIFG 391
Cdd:PRK09407 323 RLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPdlgPLFYEP------TVLTGVTPDMELAREETFG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 392 PVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVP-------IPVPMawhgfGGWKASLFG 464
Cdd:PRK09407 397 PVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGyaaawgsVDAPM-----GGMKDSGLG 471
|
490 500
....*....|....*....|....
gi 2534885945 465 DMHayGEEGVRFYTRQKSI-MQRW 487
Cdd:PRK09407 472 RRH--GAEGLLKYTESQTIaTQRV 493
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
67-478 |
2.06e-60 |
|
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: 205.24 E-value: 2.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 67 PPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVsrgIDII----EFACGIPQLLKgdyTEQVSTNIDNWT- 141
Cdd:cd07101 38 PFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEV---LDVAivarYYARRAERLLK---PRRRRGAIPVLTr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 142 ---LRQPVGVVAGITPFNFPC------MVPcwmfpvAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDK 212
Cdd:cd07101 112 ttvNRRPKGVVGVISPWNYPLtlavsdAIP------ALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 213 LAV-ETLLNHPDVaaLSFVGSTPIAKFIYETGARNGKRVQA-LGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAI 290
Cdd:cd07101 186 SEVgGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLeLGG-KNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 291 SVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGQK---PAGFENg 367
Cdd:cd07101 263 ERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPdlgPYFYEP- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 368 fytggTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGIN---- 443
Cdd:cd07101 342 -----TVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNegya 416
|
410 420 430
....*....|....*....|....*....|....*...
gi 2534885945 444 ---VPIPVPMawhgfGGWKASLFGDMHayGEEGVRFYT 478
Cdd:cd07101 417 aawASIDAPM-----GGMKDSGLGRRH--GAEGLLKYT 447
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
13-464 |
3.66e-59 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 202.83 E-value: 3.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAI 92
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 93 ITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMFPVAIAC 172
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 173 GNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQ 251
Cdd:PRK11241 174 GCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 252 ALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVT 331
Cdd:PRK11241 254 LELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLID 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 332 AEALKRIEDYVQIGVDEGATLVVDGrgqKPAGFENGFYTgGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINS 411
Cdd:PRK11241 334 EKAVAKVEEHIADALEKGARVVCGG---KAHELGGNFFQ-PTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAND 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2534885945 412 HQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIpVPMAWHGFGGWKASLFG 464
Cdd:PRK11241 410 TEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLG 461
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
13-485 |
5.03e-59 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 202.66 E-value: 5.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANK-----PPLQRVRIMNKFLALMNQHRD 87
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRNKGKdwartTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 88 ELAAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVS---TNIDNWTLRQPVGVVAGITPFNFPCMVPCW 164
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSlpmETFKGYVLKEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 165 MFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHG-DKLAVETLLNHPDVAALSFVGSTPIAKFIYETG 243
Cdd:PLN02467 171 KVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGlGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 244 ARNGKRVQALGGAKNHLLVMPDADLNQVTD-ALIGaAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDL 322
Cdd:PLN02467 251 AQMVKPVSLELGGKSPIIVFDDVDLDKAVEwAMFG-CFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 323 SAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRgqKPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANF 402
Cdd:PLN02467 330 GCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGK--RPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 403 TEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIP--VPMAWhgfGGWKASLFGdmHAYGEEGVRFYTRQ 480
Cdd:PLN02467 408 DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPcfCQAPW---GGIKRSGFG--RELGEWGLENYLSV 482
|
....*
gi 2534885945 481 KSIMQ 485
Cdd:PLN02467 483 KQVTK 487
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
31-464 |
1.08e-57 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 198.04 E-value: 1.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 31 NPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSR 110
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 111 GIDIIEF-ACGIPQLLKGDYTEQVSTNIDNWTLR-QPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAG 188
Cdd:PRK09406 87 CAKGFRYyAEHAEALLADEPADAAAVGASRAYVRyQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 189 NFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKR-VQALGGAkNHLLVMPDAD 267
Cdd:PRK09406 167 LYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKtVLELGGS-DPFIVMPSAD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 268 LNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVD 347
Cdd:PRK09406 246 LDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 348 EGATLVVDGRgqKPAGfeNGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNV 427
Cdd:PRK09406 326 AGATILCGGK--RPDG--PGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAE 401
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2534885945 428 AREFGRQVQVGMVGIN---VPIP-VPmawhgFGGWKASLFG 464
Cdd:PRK09406 402 QERFIDDLEAGQVFINgmtVSYPeLP-----FGGVKRSGYG 437
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
75-477 |
2.08e-57 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 196.11 E-value: 2.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 75 MNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITP 154
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 155 FNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGST 233
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 234 PIAKFIYETGARNGKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKT 313
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 314 LKVTDGMDLSA-EMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGQKpagfENGFYTGGTLFDNVKPNMRIYLEEIFGP 392
Cdd:PRK10090 241 VQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE----GKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 393 VLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMawHGF-GGWKASLFGDmhAYGE 471
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAM--QGFhAGWRKSGIGG--ADGK 392
|
....*.
gi 2534885945 472 EGVRFY 477
Cdd:PRK10090 393 HGLHEY 398
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
65-461 |
2.08e-57 |
|
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: 196.72 E-value: 2.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 65 NKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRGIDIIEFAcgIPQLLKGDYTEQVSTNIDNWTLRQ 144
Cdd:cd07095 18 ALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDIS--IKAYHERTGERATPMAQGRAVLRH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 145 -PVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPD 223
Cdd:cd07095 96 rPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRETGEALAAHEG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 224 VAALSFVGSTPIAKFIYETGARNGKRVQALG-GAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAIS-VAVMVGDVGD 301
Cdd:cd07095 176 IDGLLFTGSAATGLLLHRQFAGRPGKILALEmGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARrLIVPDGAVGD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 302 KLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRgqkpAGFENGFYTGGTLFD----N 377
Cdd:cd07095 256 AFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME----RLVAGTAFLSPGIIDvtdaA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 378 VKPNmriylEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMAWHGFGG 457
Cdd:cd07095 332 DVPD-----EEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGASSTAPFGG 406
|
....
gi 2534885945 458 WKAS 461
Cdd:cd07095 407 VGLS 410
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
21-460 |
5.75e-54 |
|
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: 188.57 E-value: 5.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 21 IAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKV 100
Cdd:cd07130 8 GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 101 FTDAQGEVSRGIDIIEFACGIPQLLKGdyteQVSTN-------IDNWtlrQPVGVVAGITPFNFPCMVPCWMFPVAIACG 173
Cdd:cd07130 88 LPEGLGEVQEMIDICDFAVGLSRQLYG----LTIPSerpghrmMEQW---NPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 174 NTFILKPSERDP----SAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYET-GARNGK 248
Cdd:cd07130 161 NVVVWKPSPTTPltaiAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAvAARFGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 249 RVQALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGP 328
Cdd:cd07130 241 SLLELGG-NNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 329 IVTAEALKRIEDYVQIGVDEGATLVVDG-RGQKPagfenGFYTGGTLFDnVKPNMRIYLEEIFGPVLSCVRVANFTEGLN 407
Cdd:cd07130 320 LHTKAAVDNYLAAIEEAKSQGGTVLFGGkVIDGP-----GNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIA 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2534885945 408 LINSHQYGNGVSCYTRD-GNVAREFG-RQVQVGMVgiNVPIPVPMAWHG--FGGWKA 460
Cdd:cd07130 394 WNNEVPQGLSSSIFTTDlRNAFRWLGpKGSDCGIV--NVNIGTSGAEIGgaFGGEKE 448
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
13-464 |
3.22e-53 |
|
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: 186.89 E-value: 3.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 13 FINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAI 92
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 93 ITAEHGKVFTDAQG-EVSRGIDIIEFACGIPQLLKGDYTEqvstnIDNWT----LRQPVGVVAGITPFNFPCMVPCWMFP 167
Cdd:cd07116 84 ETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSISE-----IDENTvayhFHEPLGVVGQIIPWNFPLLMATWKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 168 VAIACGNTFILKPSERDPSAGNFMARLLKEAgLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARN 246
Cdd:cd07116 159 PALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAgKPLASSKRIAKVAFTGETTTGRLIMQYASEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 247 GKRVQ-ALGGAKNHLL---VMpDADLNQVTDALIGAAYGS--AGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGM 320
Cdd:cd07116 238 IIPVTlELGGKSPNIFfadVM-DADDAFFDKALEGFVMFAlnQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 321 DLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDG-RGQKPAGFENGFYTGGTLFDNVKpnMRIYLEEIFGPVLSCVRV 399
Cdd:cd07116 317 DTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGeRNELGGLLGGGYYVPTTFKGGNK--MRIFQEEIFGPVLAVTTF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534885945 400 ANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPmAWHGFGGWKASLFG 464
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYP-AHAAFGGYKQSGIG 458
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
12-445 |
2.29e-51 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 182.26 E-value: 2.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 12 HFINGNTVSIAGSKTANVFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAA 91
Cdd:PLN00412 18 YYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 92 IITAEHGKVFTDAQGEVSRGIDIIEFAC--GIPQLLKGDYTeqVStniDNW----------TLRQPVGVVAGITPFNFPC 159
Cdd:PLN00412 98 CLVKEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFL--VS---DSFpgnernkyclTSKIPLGVVLAIPPFNYPV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 160 MVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLN-HPDVAALSFVGStpiakf 238
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTmHPGVNCISFTGG------ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 239 iyETGARNGKR-----VQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKT 313
Cdd:PLN00412 247 --DTGIAISKKagmvpLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 314 LKVTDGMDlSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRgqkpagfENGFYTGGTLFDNVKPNMRIYLEEIFGPV 393
Cdd:PLN00412 325 LTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWK-------REGNLIWPLLLDNVRPDMRIAWEEPFGPV 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2534885945 394 LSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVP 445
Cdd:PLN00412 397 LPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA 448
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
29-464 |
1.16e-48 |
|
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: 173.76 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANK-PPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGE 107
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWlPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 108 VSRGIDIIEFACGIPQLLKG-----DYTeQVSTNIDNWTLRQPVGVVAGITPFNFPC------MVPcwmfpvAIACGNTF 176
Cdd:cd07148 83 VTRAIDGVELAADELGQLGGreipmGLT-PASAGRIAFTTREPIGVVVAISAFNHPLnlivhqVAP------AIAAGCPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 177 ILKPSERDP-SAGNFMaRLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETGArNGKRVqAL-- 253
Cdd:cd07148 156 IVKPALATPlSCLAFV-DLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLA-PGTRC-ALeh 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 254 GGAKNhLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAE 333
Cdd:cd07148 233 GGAAP-VIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 334 ALKRIEDYVQIGVDEGATLVVDGRGQKPAGFENgfytggTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQ 413
Cdd:cd07148 312 EVDRVEEWVNEAVAAGARLLCGGKRLSDTTYAP------TVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLP 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2534885945 414 YGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIPVPMAWHGFGGWKASLFG 464
Cdd:cd07148 386 VAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
70-484 |
1.87e-48 |
|
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: 173.64 E-value: 1.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 70 QRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQ-GEVSRGIDIIEF--ACGiPQLLKgdyTEQVSTNIDNWTLR--- 143
Cdd:cd07098 41 ERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEILVTCEKIRWtlKHG-EKALR---PESRPGGLLMFYKRarv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 144 --QPVGVVAGITPFNFPcmvpcwmF-----PV--AIACGNTFILKPSERDP-SAGNFMA---RLLKEAGLPDGVFNVVHG 210
Cdd:cd07098 117 eyEPLGVVGAIVSWNYP-------FhnllgPIiaALFAGNAIVVKVSEQVAwSSGFFLSiirECLAACGHDPDLVQLVTC 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 211 DKLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQA-LGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMA 289
Cdd:cd07098 190 LPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLeLGG-KDPAIVLDDADLDQIASIIMRGTFQSSGQNCIG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 290 ISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGQKPAGFENGFY 369
Cdd:cd07098 269 IERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHY 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 370 TGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGIN------ 443
Cdd:cd07098 349 FPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfgvny 428
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2534885945 444 --VPIPvpmawhgFGGWKASLFGDMHayGEEGVRFYTRQKSIM 484
Cdd:cd07098 429 yvQQLP-------FGGVKGSGFGRFA--GEEGLRGLCNPKSVT 462
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
21-443 |
1.45e-45 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 171.15 E-value: 1.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 21 IAGSKTAN-VFNPS-LGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHG 98
Cdd:PRK11904 557 INGEGEARpVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAG 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 99 KVFTDAQGEVSRGIDIIEFACGI-------PQLLKGdyteqvSTNIDNWTLRQPVGVVAGITPfnfpcmvpcWMFPVAI- 170
Cdd:PRK11904 637 KTLQDAIAEVREAVDFCRYYAAQarrlfgaPEKLPG------PTGESNELRLHGRGVFVCISP---------WNFPLAIf 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 171 --------ACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGST-------- 233
Cdd:PRK11904 702 lgqvaaalAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIAGVAFTGSTetariinr 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 234 -------PIAKFIYETGARNGkrvqalggaknhLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPK 306
Cdd:PRK11904 782 tlaardgPIVPLIAETGGQNA------------MIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEM 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 307 LAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQiGVDEGATLVVdgRGQKPAGFENGFYTGGTLF--DNVKpnmri 384
Cdd:PRK11904 850 LKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIE-RMKREARLLA--QLPLPAGTENGHFVAPTAFeiDSIS----- 921
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534885945 385 YLE-EIFGPVLSCVR--VANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGIN 443
Cdd:PRK11904 922 QLErEVFGPILHVIRykASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
12-446 |
9.12e-44 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 161.28 E-value: 9.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 12 HFINGNTVSIAGSKTANvFNPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAA 91
Cdd:PRK09457 3 LWINGDWIAGQGEAFES-RNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 92 IITAEHGKVFTDAQGEVSRGIDIIefACGIPQLLKGDYTEQVSTNIDNWTLR-QPVGVVAGITPFNFPCMVPCWMFPVAI 170
Cdd:PRK09457 82 VIARETGKPLWEAATEVTAMINKI--AISIQAYHERTGEKRSEMADGAAVLRhRPHGVVAVFGPYNFPGHLPNGHIVPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 171 ACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRV 250
Cdd:PRK09457 160 LAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 251 QALG-GAKNHLLVMPDADLNQVTDALIGAAYGSAGERCM-AISVAVMVGDVGDKLIPKLAARLKTLKVtDGMDlsAE--- 325
Cdd:PRK09457 240 LALEmGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTcARRLLVPQGAQGDAFLARLVAVAKRLTV-GRWD--AEpqp 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 326 -MGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGQKPAGfenGFYTGGtLFD--NVK--PNmriylEEIFGPVLSCVRVA 400
Cdd:PRK09457 317 fMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGT---GLLTPG-IIDvtGVAelPD-----EEYFGPLLQVVRYD 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2534885945 401 NFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPI 446
Cdd:PRK09457 388 DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPL 433
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
31-464 |
1.07e-42 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 157.72 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 31 NPSLGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSR 110
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 111 GIDIIE-FACGIPQLLKGDYTeqVSTNIDNWTLRQPVGVVAGITPFNFPCmvpcWMF-----PVAIAcGNTFILKPSERD 184
Cdd:PRK13968 93 SANLCDwYAEHGPAMLKAEPT--LVENQQAVIEYRPLGTILAIMPWNFPL----WQVmrgavPILLA-GNGYLLKHAPNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 185 PSAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFI-YETGARNGKRVQALGGAkNHLLVM 263
Cdd:PRK13968 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIgAQAGAALKKCVLELGGS-DPFIVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 264 PDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQ 343
Cdd:PRK13968 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 344 IGVDEGATLVVDGrgQKPAGfeNGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTR 423
Cdd:PRK13968 325 ATLAEGARLLLGG--EKIAG--AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2534885945 424 DGNVAREFGRQVQVGMVGINvPIPVPMAWHGFGGWKASLFG 464
Cdd:PRK13968 401 DETQARQMAARLECGGVFIN-GYCASDARVAFGGVKKSGFG 440
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
40-443 |
1.22e-42 |
|
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: 158.54 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 40 QVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRGIDIIEFac 119
Cdd:TIGR01238 67 QVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRY-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 120 gipqllkgdYTEQVSTNIDNWTLRqPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAG 199
Cdd:TIGR01238 145 ---------YAKQVRDVLGEFSVE-SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 200 LPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGK---RVQALGGAKNHLLVMPDADLNQVTDAL 275
Cdd:TIGR01238 215 FPAGTIQLLPGRGADVgAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDapvPLIAETGGQNAMIVDSTALPEQVVRDV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 276 IGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATlVVD 355
Cdd:TIGR01238 295 LRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKK-IAQ 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 356 GRGQKPAGFENGFYTGGTLFDnvKPNMRIYLEEIFGPVLSCVRVA--NFTEGLNLINSHQYGNGVSCYTRDGNVAREFGR 433
Cdd:TIGR01238 374 LTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIETTYRWIEK 451
|
410
....*....|
gi 2534885945 434 QVQVGMVGIN 443
Cdd:TIGR01238 452 HARVGNCYVN 461
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
14-398 |
6.65e-41 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 157.41 E-value: 6.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 14 INGNTvsiAGSKTANVFNPS-----LGTVArqveLADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDE 88
Cdd:COG4230 562 IAGEA---ASGEARPVRNPAdhsdvVGTVV----EATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAE 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 89 LAAIITAEHGKVFTDAQGEVSRGIDIIEFacgipqllkgdYTEQVSTNIDNWTLRQPVGVVAGITPfnfpcmvpcWMFPV 168
Cdd:COG4230 635 LMALLVREAGKTLPDAIAEVREAVDFCRY-----------YAAQARRLFAAPTVLRGRGVFVCISP---------WNFPL 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 169 AI---------ACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGST----- 233
Cdd:COG4230 695 AIftgqvaaalAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVgAALVADPRIAGVAFTGSTetarl 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 234 ----------PIAKFIYETGARNGkrvqalggaknhLLVmpD--ADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGD 301
Cdd:COG4230 775 inrtlaardgPIVPLIAETGGQNA------------MIV--DssALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIAD 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 302 KLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIGVDEGATLvvdGRGQKPAGFENGFYTGGTLF--DNVK 379
Cdd:COG4230 841 RVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLV---HQLPLPEECANGTFVAPTLIeiDSIS 917
|
410 420
....*....|....*....|
gi 2534885945 380 pnmriYLE-EIFGPVLSCVR 398
Cdd:COG4230 918 -----DLErEVFGPVLHVVR 932
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
10-411 |
7.60e-40 |
|
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: 150.81 E-value: 7.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 10 VAHFINGNTVSiaGSKTANVFNPS-----LGTVARqvelADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMN- 83
Cdd:cd07123 33 IPLVIGGKEVR--TGNTGKQVMPHdhahvLATYHY----ADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSg 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 84 QHRDELAA---------IITAEhgkvfTDAQGEVsrgIDIIEFACGIPQLLkgdYTEQ-VSTNIDNWTL---RQPVGVVA 150
Cdd:cd07123 107 KYRYELNAatmlgqgknVWQAE-----IDAACEL---IDFLRFNVKYAEEL---YAQQpLSSPAGVWNRleyRPLEGFVY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 151 GITPFNFP------CMVPCWMfpvaiacGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFNVVHGD-KLAVETLLNHPD 223
Cdd:cd07123 176 AVSPFNFTaiggnlAGAPALM-------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDgPVVGDTVLASPH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 224 VAALSFVGSTPIAKFIYETGA------RNGKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVG 297
Cdd:cd07123 249 LAGLHFTGSTPTFKSLWKQIGenldryRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 298 DVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIG-VDEGATLVVDGRGQKpagfENGFYTGGTLFD 376
Cdd:cd07123 329 SLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAkSDPEAEIIAGGKCDD----SVGYFVEPTVIE 404
|
410 420 430
....*....|....*....|....*....|....*...
gi 2534885945 377 NVKPNMRIYLEEIFGPVLScVRV---ANFTEGLNLINS 411
Cdd:cd07123 405 TTDPKHKLMTEEIFGPVLT-VYVypdSDFEETLELVDT 441
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
29-398 |
1.76e-39 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 153.10 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 29 VFNPS-LGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGE 107
Cdd:PRK11905 571 VLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 108 VSRGIDIIEFacgipqllkgdYTEQVSTNIDNwTLRQPVGVVAGITPFNFPCMVpcwmF----PVAIACGNTFILKPSER 183
Cdd:PRK11905 651 VREAVDFLRY-----------YAAQARRLLNG-PGHKPLGPVVCISPWNFPLAI----FtgqiAAALVAGNTVLAKPAEQ 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 184 DPsagnFMA----RLLKEAGLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGARNGKRVQAL----G 254
Cdd:PRK11905 715 TP----LIAaravRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaetG 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 255 GaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEA 334
Cdd:PRK11905 791 G-QNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEA 869
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534885945 335 LKRIEDYVQIGVDEGATLVvdgRGQKPAGFENGFYTGGTLFDnvKPNMRIYLEEIFGPVLSCVR 398
Cdd:PRK11905 870 QANIEAHIEAMRAAGRLVH---QLPLPAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVR 928
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
71-485 |
4.27e-39 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 146.90 E-value: 4.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 71 RVRIMNKFLALMNQHRDELAAIITAEHGK-VFTDAQGEVSRGIDIIEFACG-IPQLLKgdyTEQVSTNIDN-----WTLR 143
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKpPAEAYLTEIAVVLGEIDHALKhLKKWMK---PRRVSVPLLLqpakaYVIP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 144 QPVGVVAGITPFNFP---CMVPCwmfpV-AIACGNTFILKPSERDPSAGNFMARLLKEAgLPDGVFNVVHGDKLAVETLL 219
Cdd:cd07087 99 EPLGVVLIIGPWNYPlqlALAPL----IgAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVATALL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 220 NHP-DVaaLSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVaVMV- 296
Cdd:cd07087 174 AEPfDH--IFFTGSPAVGKIVMEAAAKHLTPVTlELGG-KSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY-VLVh 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 297 GDVGDKLIPKLAARLKTLKVTDgMDLSAEMGPIVTAEALKRIEDYVqigvdEGATLVVDGRGQKpagfeNGFYTGGTLFD 376
Cdd:cd07087 250 ESIKDELIEELKKAIKEFYGED-PKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQVDK-----EERYIAPTILD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 377 NVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIpVPMAWHG-- 454
Cdd:cd07087 319 DVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVL-LHAAIPNlp 397
|
410 420 430
....*....|....*....|....*....|.
gi 2534885945 455 FGGWKASLFGDMHayGEEGVRFYTRQKSIMQ 485
Cdd:cd07087 398 FGGVGNSGMGAYH--GKAGFDTFSHLKSVLK 426
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
20-443 |
2.36e-35 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 140.88 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 20 SIAGSKTANVFNPS-LGTVARQVELADIATVNKAVEAAKAALPAWANKPPLQRVRIMNKFLALMNQHRDELAAIITAEHG 98
Cdd:PRK11809 654 PVAAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAG 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 99 KVFTDAQGEVSRGIDIIEFacgipqllkgdYTEQVSTNIDNWTLRqPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFIL 178
Cdd:PRK11809 734 KTFSNAIAEVREAVDFLRY-----------YAGQVRDDFDNDTHR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLA 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 179 KPSERDPSAGNFMARLLKEAGLPDGVFNVVHGDKlavET----LLNHPDVAALSFVGSTPIAKFIyetgARN-GKRVQAL 253
Cdd:PRK11809 802 KPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRG---ETvgaaLVADARVRGVMFTGSTEVARLL----QRNlAGRLDPQ 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 254 G---------GAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSA 324
Cdd:PRK11809 875 GrpipliaetGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLST 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 325 EMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGQkPAGFENGFYTGGTL-----FDNVKpnmriylEEIFGPVLSCVRV 399
Cdd:PRK11809 955 DIGPVIDAEAKANIERHIQAMRAKGRPVFQAAREN-SEDWQSGTFVPPTLieldsFDELK-------REVFGPVLHVVRY 1026
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2534885945 400 A--NFTEGLNLINSHQYGNGVSCYTR-DGNVAREFGRqVQVGMVGIN 443
Cdd:PRK11809 1027 NrnQLDELIEQINASGYGLTLGVHTRiDETIAQVTGS-AHVGNLYVN 1072
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
87-461 |
5.86e-35 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 136.89 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 87 DELAAIITAEHGKVFTDAQGEVSRGIDIIEFACGIPQLLKGDYTEQVSTNIDNWTLRQPVGVVAGITPFNFPCMVPCWMF 166
Cdd:PLN02315 96 DYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 167 PVAIACGNTFILKPSERDP----SAGNFMARLLKEAGLPDGVFNVVHGDKLAVETLLNHPDVAALSFVGSTPIAKFIYET 242
Cdd:PLN02315 176 CIALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQT 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 243 -GARNGKRVQALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMD 321
Cdd:PLN02315 256 vNARFGKCLLELSG-NNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 322 LSAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGQKPagfeNGFYTGGTLFDnVKPNMRIYLEEIFGPVLSCVRVAN 401
Cdd:PLN02315 335 KGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIES----EGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKT 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534885945 402 FTEGLNLINSHQYGNGVSCYTRD-GNVAREFGRQ-VQVGMVGINVPIPVPMAWHGFGGWKAS 461
Cdd:PLN02315 410 LEEAIEINNSVPQGLSSSIFTRNpETIFKWIGPLgSDCGIVNVNIPTNGAEIGGAFGGEKAT 471
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
65-486 |
1.21e-32 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 130.15 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 65 NKPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQgEVSRGIDIIEFACGIPQLLKGDYTEQVSTNI-----DN 139
Cdd:PTZ00381 25 TRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETK-MTEVLLTVAEIEHLLKHLDEYLKPEKVDTVGvfgpgKS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 140 WTLRQPVGVVAGITPFNFP---CMVPCwmfPVAIACGNTFILKPSERDPSAGNFMARLLKEAgLPDGVFNVVHGDKLAVE 216
Cdd:PTZ00381 104 YIIPEPLGVVLVIGAWNYPlnlTLIPL---AGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 217 TLLNHP-DVaaLSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAV 294
Cdd:PTZ00381 180 ELLKEPfDH--IFFTGSPRVGKLVMQAAAENLTPCTlELGG-KSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 295 MVGDVGDKLIPKLAARLKTLKVTDGMDlSAEMGPIVTAEALKRIEDYVQigvDEGATLVVDGRGQKpagfeNGFYTGGTL 374
Cdd:PTZ00381 257 VHRSIKDKFIEALKEAIKEFFGEDPKK-SEDYSRIVNEFHTKRLAELIK---DHGGKVVYGGEVDI-----ENKYVAPTI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 375 FDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQygNGVSCY--TRDGNVAREFGRQVQVGMVGIN------VPI 446
Cdd:PTZ00381 328 IVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRP--KPLALYyfGEDKRHKELVLENTSSGAVVINdcvfhlLNP 405
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2534885945 447 PVPmawhgFGGWKASLFGDMHayGEEGVRFYTRQKSIMQR 486
Cdd:PTZ00381 406 NLP-----FGGVGNSGMGAYH--GKYGFDTFSHPKPVLNK 438
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
139-485 |
2.15e-28 |
|
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: 117.20 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 139 NWTLRQPVGVVAGITPFNFPCMVPcwMFPV--AIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVfNVVHGDklave 216
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYLA--LGPLiaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-AVVTGG----- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 217 tllnhPDVAA---------LSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGER 286
Cdd:cd07133 167 -----ADVAAafsslpfdhLLFTGSTAVGRHVMRAAAENLTPVTlELGG-KSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 287 CmaisVA---VMV--GDVgDKLIPKLAARLKTL--KVTDGMDLSAemgpIVTAEALKRIEDYVQIGVDEGATLVVDGrgQ 359
Cdd:cd07133 241 C----VApdyVLVpeDKL-EEFVAAAKAAVAKMypTLADNPDYTS----IINERHYARLQGLLEDARAKGARVIELN--P 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 360 KPAGFENGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQ-----YgngvsCYTRDGNVAREFGRQ 434
Cdd:cd07133 310 AGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPrplalY-----YFGEDKAEQDRVLRR 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2534885945 435 VQVGMVGINVPIpvpmaWH------GFGGWKASlfGdMHAY-GEEGVRFYTRQKSIMQ 485
Cdd:cd07133 385 THSGGVTINDTL-----LHvaqddlPFGGVGAS--G-MGAYhGKEGFLTFSHAKPVFK 434
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
144-485 |
7.86e-27 |
|
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: 112.70 E-value: 7.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 144 QPVGVVAGITPFNFPCMVPcwMFPV--AIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFnVVHGDKLAVETLLNH 221
Cdd:cd07134 99 EPKGVCLIISPWNYPFNLA--FGPLvsAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEGDAEVAQALLEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 222 PdVAALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVG 300
Cdd:cd07134 176 P-FDHIFFTGSPAVGKIVMAAAAKHLASVTlELGG-KSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 301 DKLIPKLAARLKTLKVTDGMDL-SAEMGPIVTAEALKRIEDYVQIGVDEGATLVVDGRGQkpagfENGFYTGGTLFDNVK 379
Cdd:cd07134 254 DAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD-----AAQRYIAPTVLTNVT 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 380 PNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRD-GNVAREFGRqVQVGMVGIN------VPIPVPmaw 452
Cdd:cd07134 329 PDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDkANVNKVLAR-TSSGGVVVNdvvlhfLNPNLP--- 404
|
330 340 350
....*....|....*....|....*....|...
gi 2534885945 453 hgFGGWKASLFGDMHayGEEGVRFYTRQKSIMQ 485
Cdd:cd07134 405 --FGGVNNSGIGSYH--GVYGFKAFSHERAVLR 433
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
130-486 |
9.61e-27 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 112.60 E-value: 9.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 130 TEQVSTNIDN-----WTLRQPVGVVAGITPFNFP---CMVPCwmfpV-AIACGNTFILKPSERDPSAGNFMARLLKEAgL 200
Cdd:cd07136 80 PKRVKTPLLNfpsksYIYYEPYGVVLIIAPWNYPfqlALAPL----IgAIAAGNTAVLKPSELTPNTSKVIAKIIEET-F 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 201 PDGVFNVVHGDKLAVETLLNHP-DvaALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVMPDADLNQVTDALIGA 278
Cdd:cd07136 155 DEEYVAVVEGGVEENQELLDQKfD--YIFFTGSVRVGKIVMEAAAKHLTPVTlELGG-KSPCIVDEDANLKLAAKRIVWG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 279 AYGSAGERCMAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDlSAEMGPIVTAEALKRIEDYVqigvdEGATLVVDGRG 358
Cdd:cd07136 232 KFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGLL-----DNGKIVFGGNT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 359 QKpagfeNGFYTGGTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHqyGNGVSCY--TRDGNVAREFGRQVQ 436
Cdd:cd07136 306 DR-----ETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSR--PKPLALYlfSEDKKVEKKVLENLS 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2534885945 437 VGMVGINVPIpvpMawH------GFGGWKASLFGDMHayGEEGVRFYTRQKSIMQR 486
Cdd:cd07136 379 FGGGCINDTI---M--HlanpylPFGGVGNSGMGSYH--GKYSFDTFSHKKSILKK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
71-484 |
1.51e-26 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 111.73 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 71 RVRIMNKFLALMNQHRDELAAIITAEHGKVFTDA-QGEVSRGIDIIEFAcgIPQLLKGDYTEQVSTNIDNW-----TLRQ 144
Cdd:cd07137 23 RKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCKLA--IKELKKWMAPEKVKTPLTTFpakaeIVSE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 145 PVGVVAGITPFNFPCMVPcwMFPV--AIACGNTFILKPSERDPSAGNFMARLLKEAgLPDGVFNVVHGDKLAVETLLNHP 222
Cdd:cd07137 101 PLGVVLVISAWNFPFLLS--LEPVigAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVPETTALLEQK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 223 -DvaALSFVGSTPIAKFIYETGARNGKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGS-AGERCMAISVAVMVGDVG 300
Cdd:cd07137 178 wD--KIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEESFA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 301 DKLIPKLAARLKTLKVTDGMDlSAEMGPIVTAEALKRIEDYVQigvDEG-ATLVVDGrGQKPagfENGFYTGGTLFDNVK 379
Cdd:cd07137 256 PTLIDALKNTLEKFFGENPKE-SKDLSRIVNSHHFQRLSRLLD---DPSvADKIVHG-GERD---EKNLYIEPTILLDPP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 380 PNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPIpVPMAWHG--FGG 457
Cdd:cd07137 328 LDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTV-VQYAIDTlpFGG 406
|
410 420
....*....|....*....|....*..
gi 2534885945 458 WKASLFGDMHayGEEGVRFYTRQKSIM 484
Cdd:cd07137 407 VGESGFGAYH--GKFSFDAFSHKKAVL 431
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
113-484 |
3.33e-26 |
|
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: 110.77 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 113 DIIEFACGIPQLLKgdyTEQVSTNIDNWTL------RQPVGVVAGITPFNFPCMVPcwMFPV--AIACGNTFILKPSERD 184
Cdd:cd07135 73 DILHMLKNLKKWAK---DEKVKDGPLAFMFgkprirKEPLGVVLIIGPWNYPVLLA--LSPLvgAIAAGCTVVLKPSELT 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 185 PSAGNFMARLLKEAgLPDGVFNVVHGDKLAVETLLNHP-DvaALSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLV 262
Cdd:cd07135 148 PHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQKfD--KIFYTGSGRVGRIIAEAAAKHLTPVTlELGG-KSPVIV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 263 MPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLIpklaARLKtlKVTD-----GMDLSAEMGPIVTAEALKR 337
Cdd:cd07135 224 TKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFV----EELK--KVLDefypgGANASPDYTRIVNPRHFNR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 338 IEDYVQigvDEGATLVVDG-RGQKPAGFENgfytggTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSH---- 412
Cdd:cd07135 298 LKSLLD---TTKGKVVIGGeMDEATRFIPP------TIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRdtpl 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 413 -QY--------GNGVSCYTRDGNVArefgrqvqVGMVGINVPIP-VPmawhgFGGWKASLFGDMHayGEEGVRFYTRQKS 482
Cdd:cd07135 369 aLYiftddkseIDHILTRTRSGGVV--------INDTLIHVGVDnAP-----FGGVGDSGYGAYH--GKYGFDTFTHERT 433
|
..
gi 2534885945 483 IM 484
Cdd:cd07135 434 VV 435
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
143-411 |
1.74e-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: 102.68 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 143 RQPVGVVAGITPFNFPCMVPcwMFPV--AIACGNTFILKPSERDPSAGNFMARLL-----KEAglpdgvFNVVHGDklAV 215
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQLT--LVPLvgAIAAGNCVVIKPSEVSPATAKLLAELIpkyldKEC------YPVVLGG--VE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 216 ET--LLNHP-DVaaLSFVGSTPIAKFIYETGARNGKRVQ-ALGGaKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAIS 291
Cdd:cd07132 168 ETteLLKQRfDY--IFYTGSTSVGKIVMQAAAKHLTPVTlELGG-KSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 292 VAVMVGDVGDKLIPKLAARLKTLKVTDGMDlSAEMGPIVTAEALKRIEDYVqigvdEGATLVVDGRGQkpagfENGFYTG 371
Cdd:cd07132 245 YVLCTPEVQEKFVEALKKTLKEFYGEDPKE-SPDYGRIINDRHFQRLKKLL-----SGGKVAIGGQTD-----EKERYIA 313
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2534885945 372 GTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINS 411
Cdd:cd07132 314 PTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINS 353
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
70-457 |
6.01e-23 |
|
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: 101.16 E-value: 6.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 70 QRVRIMNKFLALMNQHRDELAaiitaeHGKVFTDAQGEVSRGidiiEFACGIPQLL------KGDYTEQVSTNIDNWTLR 143
Cdd:cd07084 22 KRADFLARIIQRLAAKSYDIA------AGAVLVTGKGWMFAE----NICGDQVQLRarafviYSYRIPHEPGNHLGQGLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 144 Q-------PVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAG-LPDGVFNVVHGDKLAV 215
Cdd:cd07084 92 QqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKTM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 216 ETLLNHPDVAALSFVGSTPIAkfiyETGARNGK--RVQALGGAKNHLLVMPDAD-LNQVTDALIGAAYGSAGERCMAISV 292
Cdd:cd07084 172 QALLLHPNPKMVLFTGSSRVA----EKLALDAKqaRIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 293 A-VMVGDVGDKLIPKLAARLKTLKVTDgmdlsAEMGPIVTAEALKRIEdyvQIGVDEGATLVVDGRgQKPAGFENGFYTG 371
Cdd:cd07084 248 LfVPENWSKTPLVEKLKALLARRKLED-----LLLGPVQTFTTLAMIA---HMENLLGSVLLFSGK-ELKNHSIPSIYGA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 372 ---GTLFDNVKPNMRIYL---EEIFGPVLSCVRVANFTEG--LNLINSHQYGNGVSCY-TRDGNVAREFGRQVQVGMVGI 442
Cdd:cd07084 319 cvaSALFVPIDEILKTYElvtEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYsNDPIFLQELIGNLWVAGRTYA 398
|
410
....*....|....*...
gi 2534885945 443 NVPIP---VPMAWHGFGG 457
Cdd:cd07084 399 ILRGRtgvAPNQNHGGGP 416
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
144-486 |
1.63e-17 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 85.10 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 144 QPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLkEAGLPDGVFNVVHGDKLAVETLLNHpD 223
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQ-K 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 224 VAALSFVGSTPIAKFIYETGARNGKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYG-SAGERCMAISVAVMVGDVGDK 302
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYAPK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 303 LIPKLAARLKTLKVTDGMDlSAEMGPIVTAEALKRIEDYVQigVDEGATLVVDGrGQKPAgfENgFYTGGTLFDNVKPNM 382
Cdd:PLN02174 269 VIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLD--EKEVSDKIVYG-GEKDR--EN-LKIAPTILLDVPLDS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 383 RIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINvPIPVPMAWHG--FGGWKA 460
Cdd:PLN02174 342 LIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVN-DIAVHLALHTlpFGGVGE 420
|
330 340
....*....|....*....|....*.
gi 2534885945 461 SLFGDMHayGEEGVRFYTRQKSIMQR 486
Cdd:PLN02174 421 SGMGAYH--GKFSFDAFSHKKAVLYR 444
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
66-473 |
7.83e-15 |
|
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: 76.11 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 66 KPPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRGIDIIEFAcgipqLLKGDYTEQVSTNIDNWTLRQ- 144
Cdd:cd07077 13 NHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESK-----LYKNIDTERGITASVGHIQDVl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 145 ------------PVGVVAGITPFNFPCMVPCWMFpVAIACGNTFILKPSERDPSAGNFMARLLKEA----GLPDGVFNVV 208
Cdd:cd07077 88 lpdngetyvrafPIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPFTNRALALLFQAAdaahGPKILVLYVP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 209 HGDKLAVETLLNHPDVAALSFVGSTPIAKFIYETGarNGKRVQALGGAKNHLLVMPDADLNQVTD-ALIGAAYGSAGerC 287
Cdd:cd07077 167 HPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHS--PHIPVIGFGAGNSPVVVDETADEERASGsVHDSKFFDQNA--C 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 288 MAISVAVMVGDVGDKLIPKLAARLKtlkvtdgmdlsaemgpivtaealkriedYVQIGVDEGATLvvdgrgqkpagfeng 367
Cdd:cd07077 243 ASEQNLYVVDDVLDPLYEEFKLKLV----------------------------VEGLKVPQETKP--------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 368 fytggtLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGL--NLINSHQYGNGVS--CYTRDGNVAREFGRQVQVGMVGIN 443
Cdd:cd07077 280 ------LSKETTPSFDDEALESMTPLECQFRVLDVISAVenAWMIIESGGGPHTrcVYTHKINKVDDFVQYIDTASFYPN 353
|
410 420 430
....*....|....*....|....*....|.
gi 2534885945 444 VP-IPVPMAWHGFGGWKASLFGDMHAYGEEG 473
Cdd:cd07077 354 ESsKKGRGAFAGKGVERIVTSGMNNIFGAGV 384
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
144-486 |
2.65e-14 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 75.15 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 144 QPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKeAGLPDGVFNVVHGDKLAVETLLNHPD 223
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP-KYLDSKAVKVIEGGPAVGEQLLQHKW 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 224 VAALsFVGSTPIAKFIYETGARNGKRVQALGGAKNHLLV---MPDADLNQVTDALIGAAYGS-AGERCMAISVAVmvgdV 299
Cdd:PLN02203 186 DKIF-FTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVL----V 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 300 GDKLIPKLAARLK-TLK--VTDGMDLSAEMGPIVTAEALKRIEDY-----VQIGVDEGATlvVDgrgqkpagfENGFYTG 371
Cdd:PLN02203 261 EERFAPILIELLKsTIKkfFGENPRESKSMARILNKKHFQRLSNLlkdprVAASIVHGGS--ID---------EKKLFIE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 372 GTLFDNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREFGRQVQVGMVGINVPI----- 446
Cdd:PLN02203 330 PTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIiqyac 409
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2534885945 447 -PVPmawhgFGGWKASLFGDMHayGEEGVRFYTRQKSIMQR 486
Cdd:PLN02203 410 dSLP-----FGGVGESGFGRYH--GKYSFDTFSHEKAVLRR 443
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
67-411 |
1.73e-13 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 72.19 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 67 PPLQRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRgidiiefACGipQL-------LKGDYTE-QVSTNID 138
Cdd:cd07129 19 SPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGR-------TTG--QLrlfadlvREGSWLDaRIDPADP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 139 NWT------LRQ---PVGVVAGITPFNFPcmvpcWMFPV-------AIACGNTFILKPSERDPSAGNFMARL----LKEA 198
Cdd:cd07129 90 DRQplprpdLRRmlvPLGPVAVFGASNFP-----LAFSVaggdtasALAAGCPVVVKAHPAHPGTSELVARAiraaLRAT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 199 GLPDGVFNVVHGDKLAV-ETLLNHPDVAALSFVGSTPIAKFIYETGAR--NGKRVQALGGAKNHLLVMPDA---DLNQVT 272
Cdd:cd07129 165 GLPAGVFSLLQGGGREVgVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILPGAlaeRGEAIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 273 DALIGAAYGSAGERCMAISVAVMV-GDVGDKLIPKLAARLKtlkvtdgmdlSAEMGPIVTAealkRIEDYVQIGVDE--- 348
Cdd:cd07129 245 QGFVGSLTLGAGQFCTNPGLVLVPaGPAGDAFIAALAEALA----------AAPAQTMLTP----GIAEAYRQGVEAlaa 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534885945 349 --GATLVVDGrGQKPAGFENG---FYTGGTLFDNvKPNMRiylEEIFGPVLSCVRVANFTEGLNLINS 411
Cdd:cd07129 311 apGVRVLAGG-AAAEGGNQAAptlFKVDAAAFLA-DPALQ---EEVFGPASLVVRYDDAAELLAVAEA 373
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
70-431 |
1.29e-12 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 69.73 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 70 QRVRIMNKFLALMNQHRDELAAIITAEHGKVFTDAQGEVSRGIDIIEF------ACGIPQLLKGdyTEQVSTNIDNWTLR 143
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYyaklgaALGDARLLRD--GEAVQLGKDPAFQG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 144 QPV-----GVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAG-LPDGVFNVVHGdklAVET 217
Cdd:PRK11903 142 QHVlvptrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG---SSAG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 218 LLNH---PDVaaLSFVGSTPIAKFIYETGA--RNGKRVQALGGAKNHLLVMPDADLNQVT-DALIGAAYGS----AGERC 287
Cdd:PRK11903 219 LLDHlqpFDV--VSFTGSAETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAAPGSEAfDLFVKEVVREmtvkSGQKC 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 288 MAISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALkrieDYVQIGVD---EGATLVVDGRGQKPAGF 364
Cdd:PRK11903 297 TAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQL----AAVRAGLAalrAQAEVLFDGGGFALVDA 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534885945 365 EN--GFYTGGTLFDNVKPN--MRIYLEEIFGPVLSCVRVANFTEGLNLINSHQYGNGVSCYTRDGNVAREF 431
Cdd:PRK11903 373 DPavAACVGPTLLGASDPDaaTAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAA 443
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
127-392 |
7.79e-11 |
|
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: 64.05 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 127 GDYTEQVSTNidnwtLRQPVGVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAGLPDGVFN 206
Cdd:cd07126 129 GDHQGQQSSG-----YRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 207 VVHGDKLAVETLLNHPDVAALSFVGSTPIAkfiyETGARNGK-RVQALGGAKNHLLVMPD-ADLNQVTDALIGAAYGSAG 284
Cdd:cd07126 204 LIHSDGPTMNKILLEANPRMTLFTGSSKVA----ERLALELHgKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSG 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 285 ERCMAISVAVM------VGDVgDKlIPKLAARLKTLKVTdgmdlsaeMGPIVTAEAlKRIEDYV-QIGVDEGATLVVDGR 357
Cdd:cd07126 280 QKCSAQSILFAhenwvqAGIL-DK-LKALAEQRKLEDLT--------IGPVLTWTT-ERILDHVdKLLAIPGAKVLFGGK 348
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2534885945 358 ----GQKPAGFenGFYTGGTLF-----DNVKPNMRIYLEEIFGP 392
Cdd:cd07126 349 pltnHSIPSIY--GAYEPTAVFvpleeIAIEENFELVTTEVFGP 390
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
85-445 |
9.91e-10 |
|
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: 60.74 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 85 HRDELAAIITAEHG------KVFTD-AQGEVSRGIDIIEFACGIpqlLKGDYTEQVSTnidnwtLRQPVGVVAGITPFNF 157
Cdd:cd07081 37 ARIDLAKLAVSETGmgrvedKVIKNhFAAEYIYNVYKDEKTCGV---LTGDENGGTLI------IAEPIGVVASITPSTN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 158 PCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEA----GLPDGVFNVVhgDKLAVET---LLNHPDVAALSFV 230
Cdd:cd07081 108 PTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGWI--DNPSIELaqrLMKFPGIGLLLAT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 231 GSTPIAKFIYetgaRNGKRVQALGGAKNHLLVMPDADLNQVTDALIGAAYGSAGERCMAISVAVMVGDVGDKLipklaar 310
Cdd:cd07081 186 GGPAVVKAAY----SSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEV------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 311 lktlkvtdgMDLSAEMGP-IVTAEALKRIEDYVQIGVDEGATLVvdGRGQKPAGFENGFytggtlfdNVKPNMRI----- 384
Cdd:cd07081 255 ---------MRLFEGQGAyKLTAEELQQVQPVILKNGDVNRDIV--GQDAYKIAAAAGL--------KVPQETRIligev 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534885945 385 --------YLEEIFGPVLSCVRVANFTEG----LNLINSHQYGNGVSCYTRDGNvARE----FGRQVQVGMVGINVP 445
Cdd:cd07081 316 tslaehepFAHEKLSPVLAMYRAANFADAdakaLALKLEGGCGHTSAMYSDNIK-AIEnmnqFANAMKTSRFVKNGP 391
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
144-445 |
1.85e-09 |
|
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: 59.81 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 144 QPVGVVAGITPFNFPCMVPcwMFPVAIA--CGNTFILKPSERDPSAGNFMARLLKEA----GLPDGVFNVV-HGDKLAVE 216
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTA--IFKALIAlkTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIeEPSIELTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 217 TLLNHPDVAALSFVGSTPIAKFIYETGArngkrvQALG-GAKN-HLLVMPDADLNQ-VTDALIGAA--YGSAgerCMAIS 291
Cdd:cd07122 172 ELMKHPDVDLILATGGPGMVKAAYSSGK------PAIGvGPGNvPAYIDETADIKRaVKDIILSKTfdNGTI---CASEQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 292 VAVMVGDVGDKLIPKLAARlktlkvtdGmdlsaemGPIVTAEALKRIEDYVqigVDEGATLVVDGRGQKP------AGFE 365
Cdd:cd07122 243 SVIVDDEIYDEVRAELKRR--------G-------AYFLNEEEKEKLEKAL---FDDGGTLNPDIVGKSAqkiaelAGIE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 366 ngfytggtlfdnVKPNMRIYLEEIFG-------------PVLSCVRVANFTEGLNLINS--HQYGNGVSC--YTRDGNVA 428
Cdd:cd07122 305 ------------VPEDTKVLVAEETGvgpeeplsreklsPVLAFYRAEDFEEALEKAREllEYGGAGHTAviHSNDEEVI 372
|
330
....*....|....*..
gi 2534885945 429 REFGRQVQVGMVGINVP 445
Cdd:cd07122 373 EEFALRMPVSRILVNTP 389
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
147-486 |
1.18e-06 |
|
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: 51.12 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 147 GVVAGITPFNFPCMVPCWMFPVAIACGNTFILKPSERDPSAGNFMARLLKEAG-LPDGVFNVVHGDklaVETLLNH---P 222
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGS---VGDLLDHlgeQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 223 DVaaLSFVGSTpiakfiyETGA---------RNGKRVQALGGAKNHLLVMPDADLNQVT-DALIGAAY----GSAGERCM 288
Cdd:cd07128 223 DV--VAFTGSA-------ATAAklrahpnivARSIRFNAEADSLNAAILGPDATPGTPEfDLFVKEVAremtVKAGQKCT 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 289 AISVAVMVGDVGDKLIPKLAARLKTLKVTDGMDLSAEMGPIVTAEALKRIEDYVQIgVDEGATLVVDGRGQ---KPAGFE 365
Cdd:cd07128 294 AIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDRfevVGADAE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534885945 366 NGFYTGGTLF--DNVKPNMRIYLEEIFGPVLSCVRVANFTEGLNLINShqyGNG---VSCYTRDGNVAREFGRQVQ--VG 438
Cdd:cd07128 373 KGAFFPPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAAR---GRGslvASVVTNDPAFARELVLGAApyHG 449
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534885945 439 MVGINVP----------IPVPMAWHG----FGGwkaslfgdmhayGEE-----GVRFYtrqksiMQR 486
Cdd:cd07128 450 RLLVLNRdsakestghgSPLPQLVHGgpgrAGG------------GEElgglrGVKHY------MQR 498
|
|
| |
