|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
15-492 |
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: 802.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 15 LAHFIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDEL 94
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 95 AELITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVA 174
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 175 IACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKR 254
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 255 VQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPL 334
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 335 VTAAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELI 414
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490304777 415 NAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGGWKRSLFGDHHAYGEEGVRFYTRYKSVMQRW 492
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
17-492 |
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: 628.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 17 HFIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAE 96
Cdd:TIGR01722 3 HWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 97 LITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIA 176
Cdd:TIGR01722 83 LITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 177 CGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQ 256
Cdd:TIGR01722 163 CGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 257 ALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGvADALVERLAERAKALKIGNGMNADVEMGPLVT 336
Cdd:TIGR01722 243 ALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGA-ADEWVPEIRERAEKIRIGPGDDPGAEMGPLIT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 337 AAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINA 416
Cdd:TIGR01722 322 PQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490304777 417 HEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGGWKRSLFGDHHAYGEEGVRFYTRYKSVMQRW 492
Cdd:TIGR01722 402 SPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
17-492 |
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: 583.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 17 HFIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAE 96
Cdd:COG1012 8 LFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 97 LITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIA 176
Cdd:COG1012 88 LLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 177 CGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGD-KTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRV 255
Cdd:COG1012 168 AGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 256 QALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLV 335
Cdd:COG1012 248 TLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 336 TAAHRAKVSAYIDAGVAAGAKLVVDGRRHvvaGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELIN 415
Cdd:COG1012 328 SEAQLERVLAYIEDAVAEGAELLTGGRRP---DGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALAN 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304777 416 AHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGGWKRSLFGDHHayGEEGVRFYTRYKSVMQRW 492
Cdd:COG1012 405 DTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGREG--GREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
25-488 |
4.50e-170 |
|
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: 487.81 E-value: 4.50e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 25 DGASDRYgDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGK 104
Cdd:pfam00171 3 DSESETI-EVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 105 VFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQiGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLK 184
Cdd:pfam00171 82 PLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 185 PSERDPSASIRLAELLKEAGLPDGVFNVVHGD-KTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQALGGAKN 263
Cdd:pfam00171 161 PSELTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 264 HLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKV 343
Cdd:pfam00171 241 PLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 344 SAYIDAGVAAGAKLVVDGRrhvvAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGV 423
Cdd:pfam00171 321 LKYVEDAKEEGAKLLTGGE----AGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490304777 424 SCFTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGGWKRSLFGDhhAYGEEGVRFYTRYKSV 488
Cdd:pfam00171 397 GVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGR--EGGPYGLEEYTEVKTV 459
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
17-507 |
1.19e-165 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 481.94 E-value: 1.19e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 17 HFIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAE 96
Cdd:PLN02419 116 NLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 97 LITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIA 176
Cdd:PLN02419 196 NITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 177 CGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQ 256
Cdd:PLN02419 276 CGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQ 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 257 ALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGvADALVERLAERAKALKIGNGMNADVEMGPLVT 336
Cdd:PLN02419 356 SNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGD-AKSWEDKLVERAKALKVTCGSEPDADLGPVIS 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 337 AAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINA 416
Cdd:PLN02419 435 KQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 417 HEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGGWKRSLFGDHHAYGEEGVRFYTRYKSVMQRWPDsI 496
Cdd:PLN02419 515 NKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQKD-I 593
|
490
....*....|.
gi 490304777 497 AKGAEFTMPVA 507
Cdd:PLN02419 594 HSPFSLAIPIL 604
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
68-489 |
7.53e-146 |
|
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: 425.08 E-value: 7.53e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNL 147
Cdd:cd07078 14 WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGELAIVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 148 RQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGD-KTAVDALIAH 226
Cdd:cd07078 94 REPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDgDEVGAALASH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 227 PDVAALSFVGSTPIAEYIHTQAARRGKRVQA-LGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVA 305
Cdd:cd07078 174 PRVDKISFTGSTAVGKAIMRAAAENLKRVTLeLGG-KSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 306 DALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvvaGGENGFFLGGTLFDDVTT 385
Cdd:cd07078 253 DEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRL---EGGKGYFVPPTVLTDVDP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 386 DMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGGWKR 465
Cdd:cd07078 330 DMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPSAPFGGVKQ 409
|
410 420
....*....|....*....|....
gi 490304777 466 SLFGDHHayGEEGVRFYTRYKSVM 489
Cdd:cd07078 410 SGIGREG--GPYGLEEYTEPKTVT 431
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
17-488 |
2.50e-133 |
|
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: 394.69 E-value: 2.50e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 17 HFIGGRALDGASDRYgdVFDPA-LGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELA 95
Cdd:cd07097 3 NYIDGEWVAGGDGEE--NRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 96 ELITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAI 175
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 176 ACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIHTQAARRGKR 254
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 255 VQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPL 334
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 335 VTAAHRAKVSAYIDAGVAAGAKLVVDGRRhvVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELI 414
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGAKLVYGGER--LKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490304777 415 NAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVP-----IPVPmawhsFGGWKRSLFGDHHAyGEEGVRFYTRYKSV 488
Cdd:cd07097 399 NDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPtagvdYHVP-----FGGRKGSSYGPREQ-GEAALEFYTTIKTV 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
17-488 |
2.99e-130 |
|
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: 387.09 E-value: 2.99e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 17 HFIGGRALDGASDRYGDVFDPA-LGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELA 95
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 96 ELITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAI 175
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 176 ACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHG-DKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKR 254
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 255 VQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPL 334
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 335 VTAAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELI 414
Cdd:cd07131 321 INEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490304777 415 NAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGGWKRSLFGdHHAYGEEGVRFYTRYKSV 488
Cdd:cd07131 401 NDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNG-HREAGTTALDAFTEWKAV 473
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
34-488 |
1.40e-117 |
|
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: 353.66 E-value: 1.40e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 34 VFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEV 113
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 114 MRGIEVVEFACG---------IPNLLktdftdqigGGIDNWNLRQPLGVVAGITPFNFPM-MV-----PcwmfpvAIACG 178
Cdd:cd07103 81 DYAASFLEWFAEearriygrtIPSPA---------PGKRILVIKQPVGVVAAITPWNFPAaMItrkiaP------ALAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 179 NTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQ- 256
Cdd:cd07103 146 CTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSl 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 257 ALGGaknH--LVVMPDANLDQAVDALVGAAYGSAGERCMA---ISVAVavgGVADALVERLAERAKALKIGNGMNADVEM 331
Cdd:cd07103 226 ELGG---NapFIVFDDADLDKAVDGAIASKFRNAGQTCVCanrIYVHE---SIYDEFVEKLVERVKKLKVGNGLDEGTDM 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 332 GPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvvagGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAV 411
Cdd:cd07103 300 GPLINERAVEKVEALVEDAVAKGAKVLTGGKRL----GLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 412 ELINAHEFanGVSC--FTSDGGIARAFARKIQVGMVGINVP-IPVPMAwhSFGGWKRSLFGdhHAYGEEGVRFYTRYKSV 488
Cdd:cd07103 376 ARANDTPY--GLAAyvFTRDLARAWRVAEALEAGMVGINTGlISDAEA--PFGGVKESGLG--REGGKEGLEEYLETKYV 449
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
34-489 |
1.10e-115 |
|
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: 348.77 E-value: 1.10e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 34 VFDPALGTVTARVPLASGA--EVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKG 111
Cdd:cd07114 1 SINPATGEPWARVPEASAAdvDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 112 EVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPS 191
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 192 ASIRLAELLKEAGLPDGVFNVVHGD-KTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQA-LGGaKNHLVVMP 269
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLeLGG-KSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 270 DANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDA 349
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 350 GVAAGAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSD 429
Cdd:cd07114 320 AREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490304777 430 ggIARAF--ARKIQVGMVGIN----VPIPVPmawhsFGGWKRSLFGDHHayGEEGVRFYTRYKSVM 489
Cdd:cd07114 400 --LARAHrvARAIEAGTVWVNtyraLSPSSP-----FGGFKDSGIGREN--GIEAIREYTQTKSVW 456
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
34-488 |
5.05e-110 |
|
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: 334.15 E-value: 5.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 34 VFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAK-GE 112
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 113 VMRGIEVVEFACGIPNLLKTDFTDQIGGGIdNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSA 192
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGAL-NYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 193 SIRLAELLKEAGLPDGVFNVVHGD-KTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQA-LGGaKNHLVVMPD 270
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLeLGG-KNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 271 ANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAG 350
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 351 VAAGAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDG 430
Cdd:cd07093 319 RAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490304777 431 GIARAFARKIQVGMVGINVPI----PVPmawhsFGGWKRSLF---GDHHAYgeegvRFYTRYKSV 488
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLvrdlRTP-----FGGVKASGIgreGGDYSL-----EFYTELKNV 453
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
17-488 |
1.36e-107 |
|
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: 328.75 E-value: 1.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 17 HFIGGRALDGASDRYgDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAE 96
Cdd:cd07086 1 GVIGGEWVGSGGETF-TSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 97 LITREHGKVFSDAKGEVMRGIEVVEFACGIpnllktdfTDQIGGGI--------DNWNLRQPLGVVAGITPFNFPMMVPC 168
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGL--------SRMLYGLTipserpghRLMEQWNPLGVVGVITAFNFPVAVPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 169 WMFPVAIACGNTFVLKPSERDPSASIRLAELLKEA----GLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYI 244
Cdd:cd07086 152 WNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 245 HTQAARRGKRVQA-LGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGN 323
Cdd:cd07086 232 GETVARRFGRVLLeLGG-NNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 324 GMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhvVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVR 403
Cdd:cd07086 311 PLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKR--IDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 404 VPDFASAVELINAHEFanGVSC--FTSDGGIARAF--ARKIQVGMVGINVP-----IPVPmawhsFGGWKRSlfGDHHAY 474
Cdd:cd07086 389 FDSLEEAIAINNDVPQ--GLSSsiFTEDLREAFRWlgPKGSDCGIVNVNIPtsgaeIGGA-----FGGEKET--GGGRES 459
|
490
....*....|....
gi 490304777 475 GEEGVRFYTRYKSV 488
Cdd:cd07086 460 GSDAWKQYMRRSTC 473
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
18-488 |
3.66e-107 |
|
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: 327.73 E-value: 3.66e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAA--FPAWSETSPLKRARVMFKFKELLDRHHDELA 95
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 96 ELITREHGKVFSDAKGEVMRGIEVVEFACGipnLLK--TDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPV 173
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAG---LATkeTGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 174 AIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIHTQAARRG 252
Cdd:cd07119 158 ALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 253 KRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMG 332
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 333 PLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVE 412
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 413 LINAHEF--ANGVscFTSDGGIARAFARKIQVGMVGINV--PIPVPMAWhsfGGWKRSLFGdhHAYGEEGVRFYTRYKSV 488
Cdd:cd07119 398 LANDTPYglAGAV--WTKDIARANRVARRLRAGTVWINDyhPYFAEAPW---GGYKQSGIG--RELGPTGLEEYQETKHI 470
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
68-489 |
1.51e-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: 322.26 E-value: 1.51e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNL 147
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEAYVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 148 RQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGD-KTAVDALIAH 226
Cdd:cd06534 90 REPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGgDEVGAALLSH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 227 PDVAALSFVGSTPIAEYIHTQAARRGKRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVAD 306
Cdd:cd06534 170 PRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 307 ALVERLAerakalkigngmnadvemgplvtaahrakvsayidagvaagaklvvdgrrhvvaggengfflggTLFDDVTTD 386
Cdd:cd06534 250 EFVEKLV----------------------------------------------------------------TVLVDVDPD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 387 MSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGGWKRS 466
Cdd:cd06534 266 MPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFGGVKNS 345
|
410 420
....*....|....*....|...
gi 490304777 467 LFGDHHayGEEGVRFYTRYKSVM 489
Cdd:cd06534 346 GIGREG--GPYGLEEYTRTKTVV 366
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
18-488 |
6.79e-104 |
|
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: 318.83 E-value: 6.79e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAEL 97
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 98 ITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFtdqIGGGIDNWNL---RQPLGVVAGITPFNFPMMVPCWMFPVA 174
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEI---IPSDRPNENIfifKVPIGVVAGILPWNFPFFLIARKLAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 175 IACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGD-KTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGK 253
Cdd:cd07088 158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRgSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 254 RVQ-ALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMG 332
Cdd:cd07088 238 KVSlELGG-KAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 333 PLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhvvAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVE 412
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKR---PEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490304777 413 LINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPM-AWHSfgGWKRS-LFGDHHAYGEEGvrfYTRYKSV 488
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMqGFHA--GWKKSgLGGADGKHGLEE---YLQTKVV 466
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
68-471 |
2.30e-103 |
|
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: 316.39 E-value: 2.30e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNL 147
Cdd:cd07104 16 WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDVPGKESMVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 148 RQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDP-SASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIA 225
Cdd:cd07104 96 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvTGGLLIAEIFEEAGLPKGVLNVVPGGGSEIgDALVE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 226 HPDVAALSFVGSTPIAEYIHTQAARRGKRVQ-ALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGV 304
Cdd:cd07104 176 HPRVRMISFTGSTAVGRHIGELAGRHLKKVAlELGG-NNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 305 ADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhvvaggeNGFFLGGTLFDDVT 384
Cdd:cd07104 255 YDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-------EGLFYQPTVLSDVT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 385 TDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPiPVPMAWHS-FGGW 463
Cdd:cd07104 328 PDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQ-TVNDEPHVpFGGV 406
|
....*...
gi 490304777 464 KRSLFGDH 471
Cdd:cd07104 407 KASGGGRF 414
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
34-488 |
6.64e-102 |
|
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: 313.47 E-value: 6.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 34 VFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEV 113
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 114 MRGIEVVEFACGI-PNLLKTDFtdQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSA 192
Cdd:cd07090 81 DSSADCLEYYAGLaPTLSGEHV--PLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 193 SIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQ-ALGGaKNHLVVMPDA 271
Cdd:cd07090 159 ALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTlELGG-KSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 272 NLDQAVDALVGAAYGSAGERCM-AISVAVAVgGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAG 350
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSnGTRVFVQR-SIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 351 VAAGAKLVVDGRRHVVAGG-ENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEF--ANGVscFT 427
Cdd:cd07090 317 KQEGAKVLCGGERVVPEDGlENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYglAAGV--FT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304777 428 SDggIARAF--ARKIQVGMVGIN----VPIPVPmawhsFGGWKRSLFGDHHayGEEGVRFYTRYKSV 488
Cdd:cd07090 395 RD--LQRAHrvIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
17-488 |
3.56e-101 |
|
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: 311.74 E-value: 3.56e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 17 HFIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAE 96
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 97 LITREHGKVFSDAKG-EVMRGIEVVEFAcgIPNLLKTDFTDQIGGGIdnwNLRQPLGVVAGITPFNFPM-MVPCWMFPvA 174
Cdd:cd07138 81 AITLEMGAPITLARAaQVGLGIGHLRAA--ADALKDFEFEERRGNSL---VVREPIGVCGLITPWNWPLnQIVLKVAP-A 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 175 IACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIHTQAARRGK 253
Cdd:cd07138 155 LAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 254 RV-QALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMG 332
Cdd:cd07138 235 RVaLELGG-KSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 333 PLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVE 412
Cdd:cd07138 314 PLASAAQFDRVQGYIQKGIEEGARLVAGGPGR-PEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490304777 413 LINAHEF--ANGVscFTSDGGIARAFARKIQVGMVGINVPIPVPMAwhSFGGWKRSlfGDHHAYGEEGVRFYTRYKSV 488
Cdd:cd07138 393 IANDTPYglAGYV--WSADPERARAVARRLRAGQVHINGAAFNPGA--PFGGYKQS--GNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
68-488 |
1.86e-100 |
|
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: 309.65 E-value: 1.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNL 147
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 148 RQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAH 226
Cdd:cd07118 117 REPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVgQAMTEH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 227 PDVAALSFVGSTPIAEYIHTQAARRGKRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVAD 306
Cdd:cd07118 197 PDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIAD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 307 ALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhvvAGGENGFFLGGTLFDDVTTD 386
Cdd:cd07118 277 AFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGER---LASAAGLFYQPTIFTDVTPD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 387 MSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPI----PVPmawhsFGG 462
Cdd:cd07118 354 MAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLdgspELP-----FGG 428
|
410 420
....*....|....*....|....*.
gi 490304777 463 WKRSLFGdhHAYGEEGVRFYTRYKSV 488
Cdd:cd07118 429 FKQSGIG--RELGRYGVEEYTELKTV 452
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
36-488 |
2.20e-100 |
|
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: 309.37 E-value: 2.20e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 36 DPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKG-EVM 114
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 115 RGIEVVEFACGIPNLLKTDfTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASI 194
Cdd:cd07115 83 RAADTFRYYAGWADKIEGE-VIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 195 RLAELLKEAGLPDGVFNVVHG-DKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQALGGAKNHLVVMPDANL 273
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 274 DQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAA 353
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 354 GAKLVVDGRRHvvagGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIA 433
Cdd:cd07115 322 GARLLTGGKRP----GARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 490304777 434 RAFARKIQVGMVGIN----VPIPVPmawhsFGGWKRSLFGDHHayGEEGVRFYTRYKSV 488
Cdd:cd07115 398 HRVAAALKAGTVWINtynrFDPGSP-----FGGYKQSGFGREM--GREALDEYTEVKSV 449
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
33-469 |
8.83e-99 |
|
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: 305.41 E-value: 8.83e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 33 DVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGE 112
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 113 VMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSA 192
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 193 SIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQALGGAKNHLVVMPDA 271
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 272 NLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGV 351
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 352 AAGAKLvvdgrrhVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGG 431
Cdd:cd07150 322 AKGAKL-------LTGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQ 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 490304777 432 IARAFARKIQVGMVGINVP-----IPVPmawhsFGGWKRSLFG 469
Cdd:cd07150 395 RAFKLAERLESGMVHINDPtildeAHVP-----FGGVKASGFG 432
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
68-469 |
1.26e-98 |
|
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: 305.30 E-value: 1.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRG-IEVVEF---ACgipnllktdftDQIGGGI- 142
Cdd:cd07112 42 WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAVDVPSaANTFRWyaeAI-----------DKVYGEVa 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 143 ----DNWNL--RQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGD 216
Cdd:cd07112 111 ptgpDALALitREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 217 -KTAVDALIAHPDVAALSFVGSTPIAEYIHTQAAR-RGKRVQALGGAKNHLVVMPDA-NLDQAVDALVGAAYGSAGERCM 293
Cdd:cd07112 191 gHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 294 AISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGGenGF 373
Cdd:cd07112 271 AGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGKRVLTETG--GF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 374 FLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDggIARAF--ARKIQVGMVGIN--- 448
Cdd:cd07112 349 FVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSD--LSRAHrvARRLRAGTVWVNcfd 426
|
410 420
....*....|....*....|..
gi 490304777 449 -VPIPVPmawhsFGGWKRSLFG 469
Cdd:cd07112 427 eGDITTP-----FGGFKQSGNG 443
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
17-488 |
1.34e-98 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 306.04 E-value: 1.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 17 HFIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAE 96
Cdd:PRK13252 9 LYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 97 LITREHGKVFSDAK-GEVMRGIEVVEFACGIPNLLKTDFTdQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAI 175
Cdd:PRK13252 89 LETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQI-PLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 176 ACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRV 255
Cdd:PRK13252 168 AAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 256 -QALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCM-AISVAVAvGGVADALVERLAERAKALKIGNGMNADVEMGP 333
Cdd:PRK13252 248 tMELGG-KSPLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVFVQ-KSIKAAFEARLLERVERIRIGDPMDPATNFGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 334 LVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVrvpDFASAVEL 413
Cdd:PRK13252 326 LVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVL---TFDDEDEV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 414 I---NAHEF--ANGVscFTSDggIARA--FARKIQVGMVGINV----PIPVPmawhsFGGWKRSLFGDHHayGEEGVRFY 482
Cdd:PRK13252 403 IaraNDTEYglAAGV--FTAD--LSRAhrVIHQLEAGICWINTwgesPAEMP-----VGGYKQSGIGREN--GIATLEHY 471
|
....*.
gi 490304777 483 TRYKSV 488
Cdd:PRK13252 472 TQIKSV 477
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
16-492 |
1.64e-97 |
|
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: 302.82 E-value: 1.64e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 16 AHFIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAA-FPAWSETSPLKRARVMFKFKELLDRHHDEL 94
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 95 AELITREHGKVFSdakgeVMRGIEVVEFAcgipNLLK--TDFTDQIGGGIDN-------------WNLRQPLGVVAGITP 159
Cdd:cd07113 81 AQLETLCSGKSIH-----LSRAFEVGQSA----NFLRyfAGWATKINGETLApsipsmqgerytaFTRREPVGVVAGIVP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 160 FNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTP 239
Cdd:cd07113 152 WNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 240 IAEYIHTQAARRGKRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKAL 319
Cdd:cd07113 232 TGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 320 KIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhvVAGgeNGFFLGGTLFDDVTTDMSIYREEIFGPVL 399
Cdd:cd07113 312 QVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEA--LAG--EGYFVQPTLVLARSADSRLMREETFGPVV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 400 AVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGIN----VPIPVPmawhsFGGWKRSLFGdhHAYG 475
Cdd:cd07113 388 SFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmhtfLDPAVP-----FGGMKQSGIG--REFG 460
|
490
....*....|....*..
gi 490304777 476 EEGVRFYTRYKSVMQRW 492
Cdd:cd07113 461 SAFIDDYTELKSVMIRY 477
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
34-490 |
6.33e-97 |
|
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: 300.81 E-value: 6.33e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 34 VFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEV 113
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 114 MRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWN---LRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDP 190
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKarvRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 191 SASIRLAELLKEAGLPDGVFNVVHGDKTAVDA-LIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQALGGAKNHLVVMP 269
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGApLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 270 DANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDA 349
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 350 GVAAGAKLVVDGRRhvVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSD 429
Cdd:cd07110 321 GKEEGARLLCGGRR--PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490304777 430 GGIARAFARKIQVGMVGINVPIPVpMAWHSFGGWKRSLFGdhHAYGEEGVRFYTRYKSVMQ 490
Cdd:cd07110 399 AERCDRVAEALEAGIVWINCSQPC-FPQAPWGGYKRSGIG--RELGEWGLDNYLEVKQITR 456
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
34-488 |
4.01e-95 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 295.82 E-value: 4.01e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 34 VFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEV 113
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 114 MRGIEVVEFACGIPNLLKTDfTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSAS 193
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGE-TIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 194 IRLAELLKEAgLPDGVFNVVHGD-KTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQALGGAKNHLVVMPDAN 272
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDgATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 273 LDQAVDALV-GAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGV 351
Cdd:cd07107 239 PEAAADAAVaGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 352 AAGAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDgg 431
Cdd:cd07107 319 REGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND-- 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304777 432 IARAF--ARKIQVGMVGIN--------VPipvpmawhsFGGWKRSLFGDHHAYGEegVRFYTRYKSV 488
Cdd:cd07107 397 ISQAHrtARRVEAGYVWINgssrhflgAP---------FGGVKNSGIGREECLEE--LLSYTQEKNV 452
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
34-488 |
1.20e-94 |
|
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: 294.53 E-value: 1.20e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 34 VFDPALGTVTARVPLASGA-EVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGE 112
Cdd:cd07109 1 VFDPSTGEVFARIARGGAAdVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 113 VMRGIEVVEFACGIPNLLKTDfTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSA 192
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGE-TIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 193 SIRLAELLKEAGLPDGVFNVVHG-DKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQALGGAKNHLVVMPDA 271
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 272 NLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMnADVEMGPLVTAAHRAKVSAYIDAGV 351
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 352 AAGAKLVVDGRRhVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGG 431
Cdd:cd07109 319 ARGARIVAGGRI-AEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304777 432 IARAFARKIQVGMVGINV-----PIPVPmawhsFGGWKRSLFGdhHAYGEEGVRFYTRYKSV 488
Cdd:cd07109 398 RALRVARRLRAGQVFVNNygaggGIELP-----FGGVKKSGHG--REKGLEALYNYTQTKTV 452
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
34-489 |
2.16e-94 |
|
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: 293.67 E-value: 2.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 34 VFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEV 113
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 114 MRGIEVVEFACGI---PNLLKTDFTDQIGGgidnwnLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDP 190
Cdd:cd07106 81 GGAVAWLRYTASLdlpDEVIEDDDTRRVEL------RRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 191 SASIRLAELLKEAgLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQ-ALGGaKNHLVVMP 269
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTlELGG-NDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 270 DANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDA 349
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 350 GVAAGAKlvvdgrrhVVAGGE----NGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSC 425
Cdd:cd07106 313 AKAKGAK--------VLAGGEpldgPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASV 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490304777 426 FTSDGGIARAFARKIQVGMVGINVPIPV-PMAWhsFGGWKRSLFGdhHAYGEEGVRFYTRYKSVM 489
Cdd:cd07106 385 WSSDLERAEAVARRLEAGTVWINTHGALdPDAP--FGGHKQSGIG--VEFGIEGLKEYTQTQVIN 445
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
33-480 |
3.11e-94 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 293.87 E-value: 3.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 33 DVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGE 112
Cdd:cd07145 2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 113 VMRGIEVVEFACGIPNLLkTDFTDQIGGGIDNWN-----LRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSE 187
Cdd:cd07145 82 VERTIRLFKLAAEEAKVL-RGETIPVDAYEYNERriaftVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 188 RDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQ-ALGGAkNHL 265
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVAlELGGS-DPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 266 VVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSA 345
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 346 YIDAGVAAGAKLVVDGRRhvvaggENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSC 425
Cdd:cd07145 320 LVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 490304777 426 FTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGGWKRSlfgdhhAYGEEGVR 480
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKS------GIGREGVR 442
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
18-488 |
3.93e-94 |
|
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: 293.71 E-value: 3.93e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAA--FPAWSETSPLKRARVMFKFKELLDRHHDELA 95
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 96 ELITREHGK-VFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVA 174
Cdd:cd07139 82 RLWTAENGMpISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 175 IACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKR 254
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 255 VQ-ALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGP 333
Cdd:cd07139 242 VTlELGG-KSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 334 LVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhvVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVEL 413
Cdd:cd07139 321 LASARQRERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490304777 414 INAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPipvPMAWHS-FGGWKRSLFGdhHAYGEEGVRFYTRYKSV 488
Cdd:cd07139 399 ANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF---RLDFGApFGGFKQSGIG--REGGPEGLDAYLETKSI 469
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
18-492 |
2.48e-93 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 291.81 E-value: 2.48e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYgDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAEL 97
Cdd:PRK13473 6 LINGELVAGEGEKQ-PVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 98 ITREHGKVFSDAKGEVMRGI-EVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIA 176
Cdd:PRK13473 85 ESLNCGKPLHLALNDEIPAIvDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 177 CGNTFVLKPSERDPSASIRLAELLKEAgLPDGVFNVVHG-DKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRV 255
Cdd:PRK13473 165 AGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGrGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 256 Q-ALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPL 334
Cdd:PRK13473 244 HlELGG-KAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 335 VTAAHRAKVSAYIDAGVAAG-AKLVVDGRRHvvagGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVEL 413
Cdd:PRK13473 323 ISAAHRDRVAGFVERAKALGhIRVVTGGEAP----DGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRW 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 414 INAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIP-VPMAWHsfGGWKRSLFG-DHHAYGEEGvrfYTRYKSVMQR 491
Cdd:PRK13473 399 ANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMlVSEMPH--GGQKQSGYGkDMSLYGLED---YTVVRHVMVK 473
|
.
gi 490304777 492 W 492
Cdd:PRK13473 474 H 474
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
18-466 |
3.61e-93 |
|
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: 292.59 E-value: 3.61e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGaSDRYgDVFDPAL-GTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAE 96
Cdd:cd07124 36 VIGGKEVRT-EEKI-ESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 97 LITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKtDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIA 176
Cdd:cd07124 114 WMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLR-GFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 177 CGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIHTQAARRG--- 252
Cdd:cd07124 193 TGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQpgq 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 253 ---KRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADV 329
Cdd:cd07124 273 kwlKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 330 EMGPLVTAAHRAKVSAYIDAGVAAGaKLVVDGRrhVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFAS 409
Cdd:cd07124 353 YMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGE--VLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDE 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490304777 410 AVELINAHEFANGVSCFT-SDGGIARAFaRKIQVGMVGINVPIpvPMAW---HSFGGWKRS 466
Cdd:cd07124 430 ALEIANDTEYGLTGGVFSrSPEHLERAR-REFEVGNLYANRKI--TGALvgrQPFGGFKMS 487
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
18-469 |
1.65e-92 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 290.44 E-value: 1.65e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAEL 97
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 98 ITREHGKVFSDAKGEVMRGIEVVEFACG---------IPnllkTDFTD-QIgggidnWNLRQPLGVVAGITPFNFPMMVP 167
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEeakrvygdiIP----SPFPDrRL------LVLKQPVGVVGAITPWNFPLAMI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 168 CWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIHT 246
Cdd:PLN02278 178 TRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 247 QAARRGKRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMN 326
Cdd:PLN02278 258 GAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 327 ADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvvaggengfFLGGTLFD-----DVTTDMSIYREEIFGPVLAV 401
Cdd:PLN02278 338 EGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRH---------SLGGTFYEptvlgDVTEDMLIFREEVFGPVAPL 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 402 VRVPDFASAVELINAHEFANGVSCFTSDggIARA--FARKIQVGMVGINVPIpVPMAWHSFGGWKRSLFG 469
Cdd:PLN02278 409 TRFKTEEEAIAIANDTEAGLAAYIFTRD--LQRAwrVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLG 475
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
34-489 |
2.25e-92 |
|
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: 288.84 E-value: 2.25e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 34 VFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAK-GE 112
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 113 VMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSA 192
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 193 SIRLAELLKEaGLPDGVFNVVHGD-KTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQALGGAKNHLVVMPDA 271
Cdd:cd07092 161 TLLLAELAAE-VLPPGVVNVVCGGgASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 272 NLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDaGV 351
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE-RA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 352 AAGAKLVVDGRRhvvaGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGG 431
Cdd:cd07092 319 PAHARVLTGGRR----AEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490304777 432 IARAFARKIQVGMVGINVPIPVP--MAWhsfGGWKRSLFG-DHHAYGEEGvrfYTRYKSVM 489
Cdd:cd07092 395 RAMRLSARLDFGTVWVNTHIPLAaeMPH---GGFKQSGYGkDLSIYALED---YTRIKHVM 449
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
18-488 |
2.92e-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: 289.11 E-value: 2.92e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVPLASGA--EVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELA 95
Cdd:cd07091 7 FINNEFVDSVSGKTFPTINPATEEVICQVAEADEEdvDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 96 ELITREHGKVFSD-AKGEVMRGIEVVEFACGipnllktdFTDQIGG---GIDNWNL----RQPLGVVAGITPFNFPMMVP 167
Cdd:cd07091 87 ALESLDNGKPLEEsAKGDVALSIKCLRYYAG--------WADKIQGktiPIDGNFLaytrREPIGVCGQIIPWNFPLLML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 168 CWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHG-DKTAVDALIAHPDVAALSFVGSTPIAEYIHT 246
Cdd:cd07091 159 AWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIME 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 247 QAARRG-KRVQ-ALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNG 324
Cdd:cd07091 239 AAAKSNlKKVTlELGG-KSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 325 MNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvvagGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRV 404
Cdd:cd07091 318 FDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERH----GSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 405 PDFASAVELINAHEF--ANGVscFTSDGGIARAFARKIQVGMVGIN------VPIPvpmawhsFGGWKRSLFGdhHAYGE 476
Cdd:cd07091 394 KTEDEVIERANDTEYglAAGV--FTKDINKALRVSRALKAGTVWVNtynvfdAAVP-------FGGFKQSGFG--RELGE 462
|
490
....*....|..
gi 490304777 477 EGVRFYTRYKSV 488
Cdd:cd07091 463 EGLEEYTQVKAV 474
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
34-488 |
2.64e-90 |
|
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: 283.48 E-value: 2.64e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 34 VFDPALGTVTARVPLASGAEVDAAVAAAAAAFpawSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEV 113
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALAASYR---STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 114 MRGIEVVEFACGIPN-----LLKTDFTDQiGGGIDNWNLRQPLGVVAGITPFNFPM-MVPCWMFPvAIACGNTFVLKPSE 187
Cdd:cd07146 80 GRAADVLRFAAAEALrddgeSFSCDLTAN-GKARKIFTLREPLGVVLAITPFNHPLnQVAHKIAP-AIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 188 RDPSASIRLAELLKEAGLPDGVFNVVHGD-KTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRgKRVQALGGaKNHLV 266
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK-RQLLELGG-NDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 267 VMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAY 346
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 347 IDAGVAAGAKLVVDGRRhvvaggeNGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCF 426
Cdd:cd07146 316 VEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVC 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490304777 427 TSDGGIARAFARKIQVGMVGIN-VP------IPvpmawhsFGGWKRSLFGdhhayGEEGVR----FYTRYKSV 488
Cdd:cd07146 389 TNDLDTIKRLVERLDVGTVNVNeVPgfrselSP-------FGGVKDSGLG-----GKEGVReamkEMTNVKTY 449
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
21-469 |
5.19e-90 |
|
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: 283.04 E-value: 5.19e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 21 GRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITR 100
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 101 EHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNT 180
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 181 FVLKPSERDP-SASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQAL 258
Cdd:cd07151 161 VVLKPASDTPiTGGLLLAKIFEEAGLPKGVLNVVVGAGSEIgDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 259 GGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAA 338
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 339 HRAKVSAYIDAGVAAGAKLVVDGRRhvvaggeNGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHE 418
Cdd:cd07151 321 QVDGLLDKIEQAVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 490304777 419 FANGVSCFTSDGGIARAFARKIQVGMVGINvPIPVPMAWH-SFGGWKRSLFG 469
Cdd:cd07151 394 YGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVNDEPHvPFGGEKNSGLG 444
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
33-481 |
9.51e-90 |
|
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: 282.01 E-value: 9.51e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 33 DVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGE 112
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 113 VMRGIEVVEFACG---------IPNLLKTDFTDQIGggidnWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVL 183
Cdd:cd07094 82 VDRAIDTLRLAAEeaerirgeeIPLDATQGSDNRLA-----WTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 184 KPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIHTQAArrGKRVQALGGAK 262
Cdd:cd07094 157 KPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLgDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 263 NHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAK 342
Cdd:cd07094 235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 343 VSAYIDAGVAAGAKLVVDGRRhvvaggeNGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANG 422
Cdd:cd07094 315 VERWVEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQ 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 490304777 423 VSCFTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGGWKRSlfgdhhAYGEEGVRF 481
Cdd:cd07094 388 AGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKES------GVGREGVPY 440
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
33-481 |
7.95e-89 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 279.48 E-value: 7.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 33 DVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGE 112
Cdd:cd07149 2 EVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 113 VMRGIEVVEFAC---------GIPnllktdfTDQIGGGIDN--WNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTF 181
Cdd:cd07149 82 VDRAIETLRLSAeeakrlageTIP-------FDASPGGEGRigFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 182 VLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGD-KTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARrgKRVQALGG 260
Cdd:cd07149 155 VLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSgETVGDALVTDPRVRMISFTGSPAVGEAIARKAGL--KKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 261 AKNHLVVMPDANLDQAVDALVGAAYGSAGERCmaISVA-VAV-GGVADALVERLAERAKALKIGNGMNADVEMGPLVTAA 338
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVC--ISVQrIFVhEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 339 HRAKVSAYIDAGVAAGAKLVVDGRRhvvaggeNGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHE 418
Cdd:cd07149 311 EAERIEEWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSP 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490304777 419 FANGVSCFTSDGGIARAFARKIQVGMVGINvPIPVPMAWH-SFGGWKRSlfgdhhAYGEEGVRF 481
Cdd:cd07149 384 YGLQAGVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHmPYGGVKES------GTGREGPRY 440
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
68-488 |
2.20e-88 |
|
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: 278.74 E-value: 2.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSeTSPLKRARVMFKFKELLDRHHDELAELITREHGK-VFSDAKGEVMRGIEVVEFacgiPNLLKTDFTDQIGGGIDNWN 146
Cdd:cd07089 37 WS-TDAEERARCLRQLHEALEARKEELRALLVAEVGApVMTARAMQVDGPIGHLRY----FADLADSFPWEFDLPVPALR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 147 L--------RQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHG-DK 217
Cdd:cd07089 112 GgpgrrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGsDN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 218 TAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQ-ALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAIS 296
Cdd:cd07089 192 AVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLlELGG-KSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 297 VAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhvVAGGENGFFLG 376
Cdd:cd07089 271 RLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLVTGGGR--PAGLDKGFYVE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 377 GTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINvpipvPMA 456
Cdd:cd07089 349 PTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN-----GGG 423
|
410 420 430
....*....|....*....|....*....|....*.
gi 490304777 457 WHS----FGGWKRSLFGdhHAYGEEGVRFYTRYKSV 488
Cdd:cd07089 424 GYGpdapFGGYKQSGLG--RENGIEGLEEFLETKSI 457
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
18-488 |
2.16e-87 |
|
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: 276.98 E-value: 2.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAA-FPAWSETSPLKRARVMFKFKELLDRHHDELAE 96
Cdd:cd07144 11 FINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 97 LITREHGKVF-SDAKGEVMRGIEVVEFACGipnllktdFTDQI-GGGIDN------WNLRQPLGVVAGITPFNFPMMVPC 168
Cdd:cd07144 91 IEALDSGKPYhSNALGDLDEIIAVIRYYAG--------WADKIqGKTIPTspnklaYTLHEPYGVCGQIIPWNYPLAMAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 169 WMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVV--HGDKTAvDALIAHPDVAALSFVGSTPIAEYIHT 246
Cdd:cd07144 163 WKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIpgYGAVAG-SALAEHPDVDKIAFTGSTATGRLVMK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 247 QAARRGKRVQALGGAKNHLVVMPDANLDQAVD-ALVGAAYGSaGERCMAISVAVAVGGVADALVERLAERAK-ALKIGNG 324
Cdd:cd07144 242 AAAQNLKAVTLECGGKSPALVFEDADLDQAVKwAAAGIMYNS-GQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 325 MNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRV 404
Cdd:cd07144 321 FDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKA-PEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 405 PDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVP----IPVPmawhsFGGWKRSLFGdhHAYGEEGVR 480
Cdd:cd07144 400 KTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMSGIG--RELGEYGLE 472
|
....*...
gi 490304777 481 FYTRYKSV 488
Cdd:cd07144 473 TYTQTKAV 480
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
33-488 |
4.27e-87 |
|
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: 275.60 E-value: 4.27e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 33 DVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPL-KRARVMFKFKELLDRHHDELAELITREHGKVFSDAKG 111
Cdd:cd07082 19 EVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLeERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 112 EVMRGIEVVEFAcgIPNLLKTDfTDQIGGGIDNWNL-------RQPLGVVAGITPFNFPMMVP-CWMFPVAIAcGNTFVL 183
Cdd:cd07082 99 EVDRTIDYIRDT--IEELKRLD-GDSLPGDWFPGTKgkiaqvrREPLGVVLAIGPFNYPLNLTvSKLIPALIM-GNTVVF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 184 KPSERDPSASIRLAELLKEAGLPDGVFNVVHGD-KTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARrgKRVQaLG-GA 261
Cdd:cd07082 175 KPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPM--KRLV-LElGG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 262 KNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRA 341
Cdd:cd07082 252 KDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSAD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 342 KVSAYIDAGVAAGAKLVVDGRRhvvaggENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFAN 421
Cdd:cd07082 332 FVEGLIDDAVAKGATVLNGGGR------EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGL 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490304777 422 GVSCFTSDGGIARAFARKIQVGMVGINV-----PIPVPmawhsFGGWKRSlfgdhhAYGEEGV----RFYTRYKSV 488
Cdd:cd07082 406 QASIFTKDINKARKLADALEVGTVNINSkcqrgPDHFP-----FLGRKDS------GIGTQGIgdalRSMTRRKGI 470
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
68-469 |
1.63e-86 |
|
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: 272.80 E-value: 1.63e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEF-ACGIPNLLKTDFTDQIGGgiDNWN 146
Cdd:cd07100 15 WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyAENAEAFLADEPIETDAG--KAYV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 147 LRQPLGVVAGITPFNFPMmvpcW-MFPVAIAC---GNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDA 222
Cdd:cd07100 93 RYEPLGVVLGIMPWNFPF----WqVFRFAAPNlmaGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 223 LIAHPDVAALSFVGSTPIAEYIHTQAARRGKR-VQALGGAkNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAV 301
Cdd:cd07100 169 IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKsVLELGGS-DPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVH 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 302 GGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvvagGENGFFLGGTLFD 381
Cdd:cd07100 248 EDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRP----DGPGAFYPPTVLT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 382 DVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVP------IPvpm 455
Cdd:cd07100 324 DVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMvksdprLP--- 400
|
410
....*....|....
gi 490304777 456 awhsFGGWKRSLFG 469
Cdd:cd07100 401 ----FGGVKRSGYG 410
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
40-466 |
1.31e-84 |
|
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: 268.39 E-value: 1.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 40 GTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEV 119
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 120 VEFACGIPN-----LLKTdftdqiGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDP-SAS 193
Cdd:cd07152 81 LHEAAGLPTqpqgeILPS------APGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 194 IRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQALGGAKNHLVVMPDANL 273
Cdd:cd07152 155 VVIARLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 274 DQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAA 353
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 354 GAKLVVDGRRhvvaggeNGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIA 433
Cdd:cd07152 315 GARLEAGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRA 387
|
410 420 430
....*....|....*....|....*....|...
gi 490304777 434 RAFARKIQVGMVGINVPIPVPMAWHSFGGWKRS 466
Cdd:cd07152 388 MALADRLRTGMLHINDQTVNDEPHNPFGGMGAS 420
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
36-488 |
4.36e-83 |
|
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: 264.85 E-value: 4.36e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 36 DPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMR 115
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 116 GIEVVEFACG-IPNLLKTDF--TDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSA 192
Cdd:cd07099 82 ALEAIDWAARnAPRVLAPRKvpTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 193 SIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPdVAALSFVGSTPIAEYIHTQAARRGKRVQA-LGGaKNHLVVMPDA 271
Cdd:cd07099 162 GELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLeLGG-KDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 272 NLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGV 351
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 352 AAGAKLVVDGRRhvvaGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGG 431
Cdd:cd07099 320 AKGAKALTGGAR----SNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490304777 432 IARAFARKIQVGMVGIN-----VPIP-VPmawhsFGGWKRSLFGDHHayGEEGVRFYTRYKSV 488
Cdd:cd07099 396 RAEAIARRLEAGAVSINdvlltAGIPaLP-----FGGVKDSGGGRRH--GAEGLREFCRPKAI 451
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
34-488 |
5.97e-83 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 264.61 E-value: 5.97e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 34 VFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVF-SDAKGE 112
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 113 VMRGIEVVEFACGIPNLLKTDfTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSA 192
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGE-TLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 193 SIRLAELLKEAgLPDGVFNVVHG-DKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQALGGAKNHLVVMPDA 271
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 272 NLDQAVD-ALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAG 350
Cdd:cd07108 239 DLDDAVDgAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 351 VAA-GAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSD 429
Cdd:cd07108 319 LSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 490304777 430 GGIARAFARKIQVGMVGINVPIpVPMAWHSFGGWKRSLFGDHHAYgEEGVRFYTRYKSV 488
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLGREASL-EGMLEHFTQKKTV 455
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
18-488 |
4.41e-80 |
|
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: 257.81 E-value: 4.41e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVplASGAEVDAAVAAAAAAFP----AWSETSPLKRARVMFKFKELLDRHHDE 93
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHV--AEGDAEDVDRAVKAARKAfdegPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 94 LAELITREHGKVFSDAK-GEVMRGIEVVEF----ACGIPNL-LKTDftdqigGGIDNWNLRQPLGVVAGITPFNFPMMVP 167
Cdd:cd07142 85 LAALETWDNGKPYEQARyAEVPLAARLFRYyagwADKIHGMtLPAD------GPHHVYTLHEPIGVVGQIIPWNFPLLMF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 168 CWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHG-DKTAVDALIAHPDVAALSFVGSTPIAEYIHT 246
Cdd:cd07142 159 AWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 247 QAARRG-KRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGM 325
Cdd:cd07142 239 LAAKSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 326 NADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvvagGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVP 405
Cdd:cd07142 319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRI----GSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 406 DFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGIN------VPIPvpmawhsFGGWKRSLFGDHHayGEEGV 479
Cdd:cd07142 395 TVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcydvfdASIP-------FGGYKMSGIGREK--GIYAL 465
|
....*....
gi 490304777 480 RFYTRYKSV 488
Cdd:cd07142 466 NNYLQVKAV 474
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
68-488 |
2.55e-79 |
|
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: 255.74 E-value: 2.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAK-GEVMRGIEVVEFACGipnllktdFTDQIGGG---ID 143
Cdd:cd07141 63 WRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYlVDLPGAIKVLRYYAG--------WADKIHGKtipMD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 144 N----WNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHG-DKT 218
Cdd:cd07141 135 GdfftYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 219 AVDALIAHPDVAALSFVGSTPIAEYIHTQAARRG-KRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISV 297
Cdd:cd07141 215 AGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNlKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 298 AVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvvagGENGFFLGG 377
Cdd:cd07141 295 TFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRH----GDKGYFIQP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 378 TLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPV-PMA 456
Cdd:cd07141 371 TVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVsPQA 450
|
410 420 430
....*....|....*....|....*....|..
gi 490304777 457 whSFGGWKRSLFGdhHAYGEEGVRFYTRYKSV 488
Cdd:cd07141 451 --PFGGYKMSGNG--RELGEYGLQEYTEVKTV 478
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
68-488 |
3.70e-79 |
|
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: 253.65 E-value: 3.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNL 147
Cdd:cd07105 16 WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIPSDKPGTLAMVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 148 RQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDK----TAVDAL 223
Cdd:cd07105 96 KEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSPedapEVVEAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 224 IAHPDVAALSFVGSTPIAEYIHTQAARRGKRV-QALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVG 302
Cdd:cd07105 176 IAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVlLELGG-KAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 303 GVADALVERLAERAKALKIGngmnaDVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhvvAGGENGFFLGGTLFDD 382
Cdd:cd07105 255 SIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLA---DESPSGTSMPPTILDN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 383 VTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVP-------IPvpm 455
Cdd:cd07105 327 VTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMtvhdeptLP--- 403
|
410 420 430
....*....|....*....|....*....|...
gi 490304777 456 awhsFGGWKRSLFGDHHayGEEGVRFYTRYKSV 488
Cdd:cd07105 404 ----HGGVKSSGYGRFN--GKWGIDEFTETKWI 430
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
11-492 |
8.70e-78 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 252.88 E-value: 8.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 11 RVRALAhfigGRALDGASDRYgDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRH 90
Cdd:PRK09407 18 RLRRLT----ARVDGAAGPTR-EVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 91 HDELAELITREHGKVFSDAKGEVMrgiEVV----EFACGIPNLLKTDftdQIGGGI----DNWNLRQPLGVVAGITPFNF 162
Cdd:PRK09407 93 REELLDLVQLETGKARRHAFEEVL---DVAltarYYARRAPKLLAPR---RRAGALpvltKTTELRQPKGVVGVISPWNY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 163 PM------MVPcwmfpvAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVaaLSFV 235
Cdd:PRK09407 167 PLtlavsdAIP------ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVgTALVDNADY--LMFT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 236 GSTPIAEYIHTQAARRGKRVQA-LGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAE 314
Cdd:PRK09407 239 GSTATGRVLAEQAGRRLIGFSLeLGG-KNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 315 RAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGGengFFLGGTLFDDVTTDMSIYREEI 394
Cdd:PRK09407 318 AVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGP---LFYEPTVLTGVTPDMELAREET 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 395 FGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVP-------IPVPMawhsfGGWKRSL 467
Cdd:PRK09407 395 FGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGyaaawgsVDAPM-----GGMKDSG 469
|
490 500
....*....|....*....|....*.
gi 490304777 468 FGDHHayGEEGVRFYTRYKSV-MQRW 492
Cdd:PRK09407 470 LGRRH--GAEGLLKYTESQTIaTQRV 493
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
18-488 |
1.79e-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: 250.91 E-value: 1.79e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAA-FPAWS-ETSPLKRARVMFKFKELLDRHHDELA 95
Cdd:cd07143 10 FINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGlKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 96 ELITREHGKVFSDAKG-EVMRGIEVVEFACGipnllktdFTDQI-GGGIDN------WNLRQPLGVVAGITPFNFPMMVP 167
Cdd:cd07143 90 SIEALDNGKTFGTAKRvDVQASADTFRYYGG--------WADKIhGQVIETdikkltYTRHEPIGVCGQIIPWNFPLLMC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 168 CWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGD-KTAVDALIAHPDVAALSFVGSTPIAEYIHT 246
Cdd:cd07143 162 AWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYgRTCGNAISSHMDIDKVAFTGSTLVGRKVME 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 247 QAARRG-KRVQALGGAKNHLVVMPDANLDQAVdalVGAAYG---SAGERCMAISVAVAVGGVADALVERLAERAKALKIG 322
Cdd:cd07143 242 AAAKSNlKKVTLELGGKSPNIVFDDADLESAV---VWTAYGiffNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 323 NGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvvagGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVV 402
Cdd:cd07143 319 DPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRH----GNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 403 RVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGIN----VPIPVPmawhsFGGWKRSLFGdhHAYGEEG 478
Cdd:cd07143 395 KFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcynlLHHQVP-----FGGYKQSGIG--RELGEYA 467
|
490
....*....|
gi 490304777 479 VRFYTRYKSV 488
Cdd:cd07143 468 LENYTQIKAV 477
|
|
| lactal_redase_Meth |
NF040648 |
lactaldehyde dehydrogenase; |
18-481 |
3.65e-77 |
|
lactaldehyde dehydrogenase;
Pssm-ID: 468615 [Multi-domain] Cd Length: 463 Bit Score: 249.52 E-value: 3.65e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDgaSDRYgDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAEL 97
Cdd:NF040648 2 FINGKWID--REDI-DVINPYNLEVIDKIPSLSREEVKEAIEIANEAKEVMKNLSPRKRYNILMDIAEELKKNKEELAKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 98 ITREHGKVFSDAKGEVMRGIEVVEFAC---------GIPNLLKTDFTdqigggidnwnLRQPLGVVAGITPFNFPMMVPC 168
Cdd:NF040648 79 ITIDAGKPIKQSIIEVDRSIETFKLAAfyakeirgeTIPSDAGLIFT-----------KKEPLGVVGAITPFNYPLNLAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 169 WMFPVAIACGNTFVLKPSERDPSASIRLAEL----LKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEY 243
Cdd:NF040648 148 HKIAPAIATGNSVVLHPSSKAPLAAIELAKIiekvLKKMNIPLGVFNLVTGYGEVVgDEIVKNEKVNKISFTGSVEVGES 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 244 IhTQAARRGKRVQALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGN 323
Cdd:NF040648 228 I-SKKAGMKKITLELGG-NNPLIVLKDADIEKAVESAVKGSFLNSGQVCISVGRVIVEEEIADEFIKKLVEETKKLKVGN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 324 GMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhvvaggENGFFLGGTLfdDVTTDMSIYREEIFGPVLAVVR 403
Cdd:NF040648 306 PLDEKTDIGPLITEEAAIRVENLVNEAIEEGAKLLCGGNR------EGSLFYPTVL--DVDEDNILVKVETFGPVLPIIR 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490304777 404 VPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGGWKRSlfgdhhAYGEEGVRF 481
Cdd:NF040648 378 VKDIDEAIEIANNTKYGLQAGVFTNDINKALKFADELEYGGVIINKSSTFRTDNMPFGGFKKS------GLGKEGIKY 449
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
9-484 |
4.14e-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: 250.01 E-value: 4.14e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 9 DSRVRALAHFIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLD 88
Cdd:cd07111 16 DAHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 89 RHHDELAELITREHGKVFSDAK-GEVMRGIEVVEFACGIPNLLKTDFTdqigggidNWnlrQPLGVVAGITPFNFPMMVP 167
Cdd:cd07111 96 KHQRLFAVLESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLLDTELA--------GW---KPVGVVGQIVPWNFPLLML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 168 CWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQ 247
Cdd:cd07111 165 AWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 248 AARRGKRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNA 327
Cdd:cd07111 245 TAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 328 DVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGrrhvVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVV--RVP 405
Cdd:cd07111 325 AIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPG----ADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLtfRTA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 406 DfaSAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGIN--------VPipvpmawhsFGGWKRSLFGDHHayGEE 477
Cdd:cd07111 401 K--EAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINghnlfdaaAG---------FGGYRESGFGREG--GKE 467
|
....*..
gi 490304777 478 GVRFYTR 484
Cdd:cd07111 468 GLYEYLR 474
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
33-481 |
1.70e-76 |
|
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: 247.54 E-value: 1.70e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 33 DVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGE 112
Cdd:cd07147 2 EVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 113 VMRGIEVVEFACG--------IPNLlktdftDQIGGGIDNWNL--RQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFV 182
Cdd:cd07147 82 VARAIDTFRIAAEeatriygeVLPL------DISARGEGRQGLvrRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 183 LKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRgKRVQALGGAK 262
Cdd:cd07147 156 LKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKK-KVVLELGGNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 263 NhLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAK 342
Cdd:cd07147 235 A-VIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 343 VSAYIDAGVAAGAKLVVDGRRhvvaggeNGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANG 422
Cdd:cd07147 314 VEGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQ 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490304777 423 VSCFTSD-GGIARAFaRKIQVGMVGIN-VPipvpmAWHS----FGGWKRSLFgdhhayGEEGVRF 481
Cdd:cd07147 387 AGVFTRDlEKALRAW-DELEVGGVVINdVP-----TFRVdhmpYGGVKDSGI------GREGVRY 439
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
18-488 |
2.02e-76 |
|
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: 248.56 E-value: 2.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAA--FPAWSETSPLKRARVMFKFKELLDRHHDELA 95
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 96 ELITREHGKVFSDA-KGEVMRGIEVVEFACGipnllktdFTDQIGGGI-------DNWNL----RQPLGVVAGITPFNFP 163
Cdd:cd07140 89 TIESLDSGAVYTLAlKTHVGMSIQTFRYFAG--------WCDKIQGKTipinqarPNRNLtltkREPIGVCGIVIPWNYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 164 MMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAE 242
Cdd:cd07140 161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 243 YIHTQAARRG-KRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKI 321
Cdd:cd07140 241 HIMKSCAVSNlKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 322 GNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvvagGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAV 401
Cdd:cd07140 321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQV----DRPGFFFEPTVFTDVEDHMFIAKEESFGPIMII 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 402 VRVP--DFASAVELINAHEF--ANGVscFTSDGGIARAFARKIQVGMVGINVPIPVPMAwHSFGGWKRSLFGDHhaYGEE 477
Cdd:cd07140 397 SKFDdgDVDGVLQRANDTEYglASGV--FTKDINKALYVSDKLEAGTVFVNTYNKTDVA-APFGGFKQSGFGKD--LGEE 471
|
490
....*....|.
gi 490304777 478 GVRFYTRYKSV 488
Cdd:cd07140 472 ALNEYLKTKTV 482
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
18-495 |
2.95e-76 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 248.58 E-value: 2.95e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAA--FPAWSETSPLKRARVMFKFKELLDRHHDELA 95
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 96 ELITREHGKVFSDAKG-EVMRGIEVVEFACGIPNLLKTDfTDQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVA 174
Cdd:PLN02766 104 ALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGE-TLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 175 IACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHG-DKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRG- 252
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNl 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 253 KRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMG 332
Cdd:PLN02766 263 KQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 333 PLVTAAHRAKVSAYIDAGVAAGAKLVVDGRrhvvAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVE 412
Cdd:PLN02766 343 PQVDKQQFEKILSYIEHGKREGATLLTGGK----PCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIK 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 413 LINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPMAWhSFGGWKRSLFGDHhaYGEEGVRFYTRYKSVMQRW 492
Cdd:PLN02766 419 KANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDC-PFGGYKMSGFGRD--QGMDALDKYLQVKSVVTPL 495
|
...
gi 490304777 493 PDS 495
Cdd:PLN02766 496 YNS 498
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
68-492 |
4.00e-76 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 248.31 E-value: 4.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGI--------EVVEFACGIPNLLKTdftdqig 139
Cdd:PRK03137 89 WKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIdfleyyarQMLKLADGKPVESRP------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 140 gGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTA 219
Cdd:PRK03137 162 -GEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 220 V-DALIAHPDVAALSFVGSTPIAEYIHTQAARRG------KRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERC 292
Cdd:PRK03137 241 VgDYLVDHPKTRFITFTGSREVGLRIYERAAKVQpgqiwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 293 MAISVAVAVGGVADALVERLAERAKALKIGNGMNADVeMGPLVTAAHRAKVSAYIDAGVAAGaKLVVDGRRhvvaGGENG 372
Cdd:PRK03137 321 SACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAY-MGPVINQASFDKIMSYIEIGKEEG-RLVLGGEG----DDSKG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 373 FFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFA-NGVSCFTSDGGIARA----------FARKIQ 441
Cdd:PRK03137 395 YFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGlTGAVISNNREHLEKArrefhvgnlyFNRGCT 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 490304777 442 VGMVGinvpipvpmaWHSFGGWKRSlfG-DHHAYGEEGVRFYTRYKSVMQRW 492
Cdd:PRK03137 475 GAIVG----------YHPFGGFNMS--GtDSKAGGPDYLLLFLQAKTVSEMF 514
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
68-490 |
1.36e-75 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 245.33 E-value: 1.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSeTSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFACGipnLLKTDF--TDQIGGGIDNW 145
Cdd:cd07120 37 WA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAG---LARTEAgrMIEPEPGSFSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 146 NLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEA-GLPDGVFNVVHGDKTAV-DAL 223
Cdd:cd07120 113 VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGaAHL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 224 IAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGG 303
Cdd:cd07120 193 VASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 304 VADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhVVAGGENGFFLGGTLFDDV 383
Cdd:cd07120 273 IADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGGP-VTEGLAKGAFLRPTLLEVD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 384 TTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGgiARAF--ARKIQVGMVGINVPIPVpMAWHSFG 461
Cdd:cd07120 352 DPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL--ARAMrvARAIRAGTVWINDWNKL-FAEAEEG 428
|
410 420
....*....|....*....|....*....
gi 490304777 462 GWKRSLFGDHHayGEEGVRFYTRYKSVMQ 490
Cdd:cd07120 429 GYRQSGLGRLH--GVAALEDFIEYKHIYL 455
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
35-483 |
3.54e-75 |
|
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: 244.14 E-value: 3.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 35 FDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVM 114
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 115 RGIEVVEF-ACGIPNLLKTDftdQIGGGI----DNWNLRQPLGVVAGITPFNFPM------MVPcwmfpvAIACGNTFVL 183
Cdd:cd07101 81 DVAIVARYyARRAERLLKPR---RRRGAIpvltRTTVNRRPKGVVGVISPWNYPLtlavsdAIP------ALLAGNAVVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 184 KPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVaaLSFVGSTPIAEYIHTQAARRGKRVQALGGAK 262
Cdd:cd07101 152 KPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVgGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 263 NHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAK 342
Cdd:cd07101 230 NPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 343 VSAYIDAGVAAGAKLVVDGRRHVVAGgenGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANG 422
Cdd:cd07101 310 VTAHVDDAVAKGATVLAGGRARPDLG---PYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLN 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490304777 423 VSCFTSDGGIARAFARKIQVGMVGIN-------VPIPVPMawhsfGGWKRSlfGDHHAYGEEGVRFYT 483
Cdd:cd07101 387 ASVWTRDGARGRRIAARLRAGTVNVNegyaaawASIDAPM-----GGMKDS--GLGRRHGAEGLLKYT 447
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
18-469 |
9.47e-75 |
|
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: 243.79 E-value: 9.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAEL 97
Cdd:cd07559 4 FINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 98 ITREHGKVFSDAKG--------------EVMRGIEvvefacGIPNLLKTDFTDQIgggidnwnLRQPLGVVAGITPFNFP 163
Cdd:cd07559 84 ETLDNGKPIRETLAadiplaidhfryfaGVIRAQE------GSLSEIDEDTLSYH--------FHEPLGVVGQIIPWNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 164 MMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAgLPDGVFNVVHG-DKTAVDALIAHPDVAALSFVGSTPIAE 242
Cdd:cd07559 150 LLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGfGSEAGKPLASHPRIAKLAFTGSTTVGR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 243 YIHTQAARRGKRVQ-ALGGaKNHLVVMPDA--NLDQAVDALVGAAYGSA---GERCMAISVAVAVGGVADALVERLAERA 316
Cdd:cd07559 229 LIMQYAAENLIPVTlELGG-KSPNIFFDDAmdADDDFDDKAEEGQLGFAfnqGEVCTCPSRALVQESIYDEFIERAVERF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 317 KALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFG 396
Cdd:cd07559 308 EAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490304777 397 PVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPmAWHSFGGWKRSLFG 469
Cdd:cd07559 388 PVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYP-AHAPFGGYKKSGIG 459
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
37-489 |
1.06e-74 |
|
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: 242.92 E-value: 1.06e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 37 PALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRG 116
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 117 IEVVEFACGI--------PNLLKTDFTDQIgggidnwnLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSER 188
Cdd:cd07102 83 LERARYMISIaeealadiRVPEKDGFERYI--------RREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 189 DPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRVQ-ALGGaKNHLVV 267
Cdd:cd07102 155 TPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGlELGG-KDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 268 MPDANLDQAVDALV-GAAYGSaGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAY 346
Cdd:cd07102 234 RPDADLDAAAESLVdGAFFNS-GQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 347 IDAGVAAGAKLVVDGrRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCF 426
Cdd:cd07102 313 IADAIAKGARALIDG-ALFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVW 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490304777 427 TSDGGIARAFARKIQVGMVGIN---VPIPVpMAWhsfGGWKRSlfGDHHAYGEEGVRFYTRYKSVM 489
Cdd:cd07102 392 TKDIARAEALGEQLETGTVFMNrcdYLDPA-LAW---TGVKDS--GRGVTLSRLGYDQLTRPKSYH 451
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
18-469 |
1.01e-71 |
|
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: 235.81 E-value: 1.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAEL 97
Cdd:cd07117 4 FINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 98 ITREHGKVFSDAKG--------------EVMRGIEvvefacGIPNLLKTDFTDQIgggidnwnLRQPLGVVAGITPFNFP 163
Cdd:cd07117 84 ETLDNGKPIRETRAvdiplaadhfryfaGVIRAEE------GSANMIDEDTLSIV--------LREPIGVVGQIIPWNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 164 MMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAgLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAE 242
Cdd:cd07117 150 FLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSgEYLLNHPGLDKLAFTGSTEVGR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 243 YIHTQAARRgkRVQA---LGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKAL 319
Cdd:cd07117 229 DVAIAAAKK--LIPAtleLGG-KSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 320 KIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVL 399
Cdd:cd07117 306 KVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVA 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 400 AVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPmAWHSFGGWKRSLFG 469
Cdd:cd07117 386 TVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIP-AGAPFGGYKKSGIG 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
17-489 |
1.01e-71 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 237.40 E-value: 1.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 17 HFIGGRALDGASDRYGDVFDPALGTVTARVplASGAEVDAAVAAAAAAFP----AWSETSPLKRARVMFKFKELLDRHHD 92
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHV--AEGDAEDVNRAVAAARKAfdegPWPKMTAYERSRILLRFADLLEKHND 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 93 ELAELITREHGKVFSD-AKGEVMRGIEVVEFACGipnllktdFTDQIGG------GIDN-WNLRQPLGVVAGITPFNFPM 164
Cdd:PLN02466 138 ELAALETWDNGKPYEQsAKAELPMFARLFRYYAG--------WADKIHGltvpadGPHHvQTLHEPIGVAGQIIPWNFPL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 165 MVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHG-DKTAVDALIAHPDVAALSFVGSTPIAEY 243
Cdd:PLN02466 210 LMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKI 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 244 IHTQAARRG-KRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIG 322
Cdd:PLN02466 290 VLELAAKSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 323 NGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvvagGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVV 402
Cdd:PLN02466 370 DPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRF----GSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSIL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 403 RVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVpIPVPMAWHSFGGWKRSlfGDHHAYGEEGVRFY 482
Cdd:PLN02466 446 KFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNC-FDVFDAAIPFGGYKMS--GIGREKGIYSLNNY 522
|
....*..
gi 490304777 483 TRYKSVM 489
Cdd:PLN02466 523 LQVKAVV 529
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
18-490 |
2.45e-70 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 233.09 E-value: 2.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVPLASG-----AEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHD 92
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAedvdaAVEAARKAFKRNKGKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 93 ELAELITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWN---LRQPLGVVAGITPFNFPMMVPCW 169
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKgyvLKEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 170 MFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKT-AVDALIAHPDVAALSFVGSTPIAEYIHTQA 248
Cdd:PLN02467 171 KVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTeAGAPLASHPGVDKIAFTGSTATGRKIMTAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 249 ARRGKRVQALGGAKNHLVVMPDANLDQAVD-ALVGaAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNA 327
Cdd:PLN02467 251 AQMVKPVSLELGGKSPIIVFDDVDLDKAVEwAMFG-CFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 328 DVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvvAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDF 407
Cdd:PLN02467 330 GCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRP--EHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 408 ASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVpMAWHSFGGWKRSLFGdhHAYGEEGVRFYTRYKS 487
Cdd:PLN02467 408 DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPC-FCQAPWGGIKRSGFG--RELGEWGLENYLSVKQ 484
|
...
gi 490304777 488 VMQ 490
Cdd:PLN02467 485 VTK 487
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
18-466 |
6.57e-70 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 231.71 E-value: 6.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVplASGAEVDAAVAAAAAAFP----AWSETSPLKRARVMFKFKELLDRHHDE 93
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKI--ARGKSVDIDRAVSAARGVfergDWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 94 LAELITREHGK-VFSDAKGEVMRGIEVVEFAcgipnllkTDFTDQIGGGI---DNWNL----RQPLGVVAGITPFNFPMM 165
Cdd:PRK09847 101 LALLETLDTGKpIRHSLRDDIPGAARAIRWY--------AEAIDKVYGEVattSSHELamivREPVGVIAAIVPWNFPLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 166 VPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHG-DKTAVDALIAHPDVAALSFVGSTPIAEYI 244
Cdd:PRK09847 173 LTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 245 HTQAARRG-KRVQALGGAKNHLVVMPDA-NLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIG 322
Cdd:PRK09847 253 LKDAGDSNmKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 323 NGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGaKLVVDGRRHVVAGgengfFLGGTLFDDVTTDMSIYREEIFGPVLAVV 402
Cdd:PRK09847 333 HPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-----AIGPTIFVDVDPNASLSREEIFGPVLVVT 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490304777 403 RVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINV----PIPVPmawhsFGGWKRS 466
Cdd:PRK09847 407 RFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMTVP-----FGGYKQS 469
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
8-477 |
8.23e-70 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 230.95 E-value: 8.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 8 NDSRVRALAHFIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELL 87
Cdd:PRK11241 4 NDSTLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 88 DRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFacgIPNLLKTDFTDQIGGGIDNWNL---RQPLGVVAGITPFNFPM 164
Cdd:PRK11241 84 MEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEW---FAEEGKRIYGDTIPGHQADKRLiviKQPIGVTAAITPWNFPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 165 MVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDA-LIAHPDVAALSFVGSTPIAEY 243
Cdd:PRK11241 161 AMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGeLTSNPLVRKLSFTGSTEIGRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 244 IHTQAARRGKRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGN 323
Cdd:PRK11241 241 LMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 324 GMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGGengfFLGGTLFDDVTTDMSIYREEIFGPVLAVVR 403
Cdd:PRK11241 321 GLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGN----FFQPTILVDVPANAKVAKEETFGPLAPLFR 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304777 404 VPDFASAVELINAHEFanGVSCFTSDGGIARAF--ARKIQVGMVGINVPIpVPMAWHSFGGWKRSLFG-DHHAYGEE 477
Cdd:PRK11241 397 FKDEADVIAQANDTEF--GLAAYFYARDLSRVFrvGEALEYGIVGINTGI-ISNEVAPFGGIKASGLGrEGSKYGIE 470
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
68-471 |
2.79e-68 |
|
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: 225.61 E-value: 2.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFAcgIPNLLKTDFTDQIGGGIDNWNL 147
Cdd:cd07095 16 WAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDIS--IKAYHERTGERATPMAQGRAVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 148 RQ-PLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAH 226
Cdd:cd07095 94 RHrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRETGEALAAH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 227 PDVAALSFVGSTPIAEYIHTQAARRGKRVQALG-GAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAIS-VAVAVGGV 304
Cdd:cd07095 174 EGIDGLLFTGSAATGLLLHRQFAGRPGKILALEmGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARrLIVPDGAV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 305 ADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhVVAGGenGFFLGGTLfdDVT 384
Cdd:cd07095 254 GDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMER-LVAGT--AFLSPGII--DVT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 385 TDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFanGVSC--FTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGG 462
Cdd:cd07095 329 DAADVPDEEIFGPLLQVYRYDDFDEAIALANATRF--GLSAglLSDDEALFERFLARIRAGIVNWNRPTTGASSTAPFGG 406
|
....*....
gi 490304777 463 WKRSlfGDH 471
Cdd:cd07095 407 VGLS--GNH 413
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
71-488 |
2.59e-65 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 218.45 E-value: 2.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 71 TSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEF-ACGIPNLLKTDFTDQIGGGIDNWNLR- 148
Cdd:PRK09406 42 TTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYyAEHAEALLADEPADAAAVGASRAYVRy 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 149 QPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPD 228
Cdd:PRK09406 122 QPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 229 VAALSFVGSTPIAEYIHTQAARRGKR-VQALGGAkNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADA 307
Cdd:PRK09406 202 VAAATLTGSEPAGRAVAAIAGDEIKKtVLELGGS-DPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 308 LVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhvVAGgeNGFFLGGTLFDDVTTDM 387
Cdd:PRK09406 281 FAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKR--PDG--PGWFYPPTVITDITPDM 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 388 SIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGIN---VPIP-VPmawhsFGGW 463
Cdd:PRK09406 357 RLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINgmtVSYPeLP-----FGGV 431
|
410 420
....*....|....*....|....*....
gi 490304777 464 KRSlfgdhhAYGEE----GVRFYTRYKSV 488
Cdd:PRK09406 432 KRS------GYGRElsahGIREFCNIKTV 454
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
33-469 |
1.71e-64 |
|
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: 217.83 E-value: 1.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 33 DVFDPA-LGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKG 111
Cdd:cd07125 49 PVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 112 EVMrgiEVVEFACGIPNLLKTDFTDQIGGGID--NWNLR-QPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSER 188
Cdd:cd07125 129 EVR---EAIDFCRYYAAQARELFSDPELPGPTgeLNGLElHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 189 DPSASIRLAELLKEAGLPDGVFNVVHGD-KTAVDALIAHPDVAALSFVGSTPIAEYIH-TQAARRGKRVQ--ALGGAKNH 264
Cdd:cd07125 206 TPLIAARAVELLHEAGVPRDVLQLVPGDgEEIGEALVAHPRIDGVIFTGSTETAKLINrALAERDGPILPliAETGGKNA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 265 LVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVS 344
Cdd:cd07125 286 MIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 345 AYIDAGVAAgAKLVvdgrRHVVAGGENGFFLGGTLFDDVTTdmSIYREEIFGPVLAVVR--VPDFASAVELINAHEFAng 422
Cdd:cd07125 366 AHTELMRGE-AWLI----APAPLDDGNGYFVAPGIIEIVGI--FDLTTEVFGPILHVIRfkAEDLDEAIEDINATGYG-- 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304777 423 vscFTSdgGI-------ARAFARKIQVGMVGINVPI--------PvpmawhsFGGWKRSLFG 469
Cdd:cd07125 437 ---LTL--GIhsrdereIEYWRERVEAGNLYINRNItgaivgrqP-------FGGWGLSGTG 486
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
80-482 |
2.46e-62 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 209.21 E-value: 2.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 80 MFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDF--TDQIGGGIdnWNLRQPLGVVAGI 157
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIiqSDRPGENI--LLFKRALGVTTGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 158 TPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVG 236
Cdd:PRK10090 79 LPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 237 STPIAEYIHTQAARRGKRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERA 316
Cdd:PRK10090 159 SVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 317 KALKIGN-GMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHvvagGENGFFLGGTLFDDVTTDMSIYREEIF 395
Cdd:PRK10090 239 QAVQFGNpAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAV----EGKGYYYPPTLLLDVRQEMSIMHEETF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 396 GPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPM-AWHSfgGWKRSLFGDhhAY 474
Cdd:PRK10090 315 GPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMqGFHA--GWRKSGIGG--AD 390
|
....*...
gi 490304777 475 GEEGVRFY 482
Cdd:PRK10090 391 GKHGLHEY 398
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
33-450 |
7.81e-62 |
|
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: 209.76 E-value: 7.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 33 DVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGE 112
Cdd:cd07130 15 TSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 113 VMRGIEVVEFACGIpnllktdfTDQIGGGI-----------DNWNlrqPLGVVAGITPFNFPMMVPCWMFPVAIACGNTF 181
Cdd:cd07130 95 VQEMIDICDFAVGL--------SRQLYGLTipserpghrmmEQWN---PLGVVGVITAFNFPVAVWGWNAAIALVCGNVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 182 VLKPSERDPSASIR----LAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYI-HTQAARRGKRVQ 256
Cdd:cd07130 164 VWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVgQAVAARFGRSLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 257 ALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVT 336
Cdd:cd07130 244 ELGG-NNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 337 AAHRAKVSAYIDAGVAAGAKLVVDGRRhvVAGGenGFFLGGTLFdDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINa 416
Cdd:cd07130 323 KAAVDNYLAAIEEAKSQGGTVLFGGKV--IDGP--GNYVEPTIV-EGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNN- 396
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 490304777 417 hEFANGVSC--FTSDggIARAF----ARKIQVGMVGINVP 450
Cdd:cd07130 397 -EVPQGLSSsiFTTD--LRNAFrwlgPKGSDCGIVNVNIG 433
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
35-489 |
2.54e-61 |
|
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: 207.92 E-value: 2.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 35 FDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAK-GEV 113
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 114 MRGIEvvefacgipnllKTDFTDQIG----------GGIDNWNLR-----QPLGVVAGITPFNFPM------MVPcwmfp 172
Cdd:cd07098 81 LVTCE------------KIRWTLKHGekalrpesrpGGLLMFYKRarveyEPLGVVGAIVSWNYPFhnllgpIIA----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 173 vAIACGNTFVLKPSERDPSASIR----LAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQA 248
Cdd:cd07098 144 -ALFAGNAIVVKVSEQVAWSSGFflsiIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 249 ARRGKRVQA-LGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNA 327
Cdd:cd07098 223 AESLTPVVLeLGG-KDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 328 DVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDF 407
Cdd:cd07098 302 DVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 408 ASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGIN--------VPIPvpmawhsFGGWKRSLFGDHHayGEEGV 479
Cdd:cd07098 382 EEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINdfgvnyyvQQLP-------FGGVKGSGFGRFA--GEEGL 452
|
490
....*....|
gi 490304777 480 RFYTRYKSVM 489
Cdd:cd07098 453 RGLCNPKSVT 462
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
68-448 |
9.21e-60 |
|
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: 204.73 E-value: 9.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIG-GGIDNWN 146
Cdd:cd07083 71 WKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPyPGEDNES 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 147 LRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIA 225
Cdd:cd07083 151 FYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 226 HPDVAALSFVGSTPIAEYIHTQAARRG------KRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAV 299
Cdd:cd07083 231 HERIRGINFTGSLETGKKIYEAAARLApgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLI 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 300 AVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGaKLVVDGRRhvVAGgeNGFFLGGTL 379
Cdd:cd07083 311 LTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKR--LEG--EGYFVAPTV 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490304777 380 FDDVTTDMSIYREEIFGPVLAVVRVP--DFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGIN 448
Cdd:cd07083 386 VEEVPPKARIAQEEIFGPVLSVIRYKddDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYIN 456
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
36-469 |
1.40e-59 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 203.55 E-value: 1.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 36 DPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMR 115
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 116 GIEVVE-FACGIPNLLKTDFTDqigggIDNWNL---RQPLGVVAGITPFNFPM-MVPCWMFPVAIAcGNTFVLKPSERDP 190
Cdd:PRK13968 93 SANLCDwYAEHGPAMLKAEPTL-----VENQQAvieYRPLGTILAIMPWNFPLwQVMRGAVPILLA-GNGYLLKHAPNVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 191 SASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKR-VQALGGAkNHLVVMP 269
Cdd:PRK13968 167 GCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKcVLELGGS-DPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 270 DANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDA 349
Cdd:PRK13968 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 350 GVAAGAKLVVDGRRhvVAGGENgfFLGGTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSD 429
Cdd:PRK13968 326 TLAEGARLLLGGEK--IAGAGN--YYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTD 401
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 490304777 430 GGIARAFARKIQVGMVGINvPIPVPMAWHSFGGWKRSLFG 469
Cdd:PRK13968 402 ETQARQMAARLECGGVFIN-GYCASDARVAFGGVKKSGFG 440
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
18-469 |
1.11e-55 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 193.44 E-value: 1.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 18 FIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAEL 97
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 98 ITREHGKVFSDAKG-EVMRGIEVVEFACGIPNLLKTDFTdQIGGGIDNWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIA 176
Cdd:cd07116 84 ETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSIS-EIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 177 CGNTFVLKPSERDPSASIRLAELLKEAgLPDGVFNVVHG-DKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRV 255
Cdd:cd07116 163 AGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 256 Q-ALGGAKNHLV---VMP--DANLDQAVDALVGAAYGSaGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADV 329
Cdd:cd07116 242 TlELGGKSPNIFfadVMDadDAFFDKALEGFVMFALNQ-GEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 330 EMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGGENGFFLGGTLFDDvTTDMSIYREEIFGPVLAVVRVPDFAS 409
Cdd:cd07116 321 MIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEE 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 410 AVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPmAWHSFGGWKRSLFG 469
Cdd:cd07116 400 ALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYP-AHAAFGGYKQSGIG 458
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
73-469 |
9.06e-55 |
|
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: 190.32 E-value: 9.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 73 PLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLK-----TDFTdQIGGGIDNWNL 147
Cdd:cd07148 43 AHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGgreipMGLT-PASAGRIAFTT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 148 RQPLGVVAGITPFNFPM------MVPcwmfpvAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVD 221
Cdd:cd07148 122 REPIGVVVAISAFNHPLnlivhqVAP------AIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 222 ALIAHPDVAALSFVGSTPIAEYIHTQAARrGKRVqAL--GGAKNhLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAV 299
Cdd:cd07148 196 KLVTDPRVAFFSFIGSARVGWMLRSKLAP-GTRC-ALehGGAAP-VIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 300 AVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhvvaggengffLGGTL 379
Cdd:cd07148 273 VPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKR-----------LSDTT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 380 FD-----DVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVP 454
Cdd:cd07148 342 YAptvllDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFR 421
|
410
....*....|....*
gi 490304777 455 MAWHSFGGWKRSLFG 469
Cdd:cd07148 422 VDWMPFAGRRQSGYG 436
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
68-450 |
1.18e-49 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 177.64 E-value: 1.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFAC--GIPNLLKTDF--TDQI-GGGI 142
Cdd:PLN00412 69 WAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFlvSDSFpGNER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 143 DNWNL--RQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV 220
Cdd:PLN00412 149 NKYCLtsKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 221 -DALIAHPDVAALSFVG-STPIAeyihtqAARRGKRV--QALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAIS 296
Cdd:PLN00412 229 gDFLTMHPGVNCISFTGgDTGIA------ISKKAGMVplQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 297 VAVAVGGVADALVERLAERAKALKIGNGmNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRRhvvaggeNGFFLG 376
Cdd:PLN00412 303 VVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIW 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490304777 377 GTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVP 450
Cdd:PLN00412 375 PLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA 448
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
17-473 |
9.14e-48 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 172.06 E-value: 9.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 17 HFIGGRALDGASDRYgDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAE 96
Cdd:PRK09457 3 LWINGDWIAGQGEAF-ESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 97 LITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGidNWNLR-QPLGVVAGITPFNFPMMVPCWMFPVAI 175
Cdd:PRK09457 82 VIARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKRSEMADG--AAVLRhRPHGVVAVFGPYNFPGHLPNGHIVPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 176 ACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQAARRGKRV 255
Cdd:PRK09457 160 LAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 256 QALG-GAKNHLVVMPDANLDQAVDALVGAAYGSAGERCM-AISVAVAVGGVADALVERLAERAKALKIGnGMNADVE--M 331
Cdd:PRK09457 240 LALEmGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTcARRLLVPQGAQGDAFLARLVAVAKRLTVG-RWDAEPQpfM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 332 GPLVT-AAHRAKVSAYIDAgVAAGAKLVVDgRRHVVAGGenGFFLGGTLfdDVTTDMSIYREEIFGPVLAVVRVPDFASA 410
Cdd:PRK09457 319 GAVISeQAAQGLVAAQAQL-LALGGKSLLE-MTQLQAGT--GLLTPGII--DVTGVAELPDEEYFGPLLQVVRYDDFDEA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490304777 411 VELINAHEFanGVSC--FTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGGWKRSlfGDHHA 473
Cdd:PRK09457 393 IRLANNTRF--GLSAglLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAAPFGGVGAS--GNHRP 453
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
24-448 |
5.00e-43 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 163.83 E-value: 5.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 24 LDGASDRYGDVFDPA-LGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREH 102
Cdd:PRK11904 556 IINGEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREA 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 103 GKVFSDAKGEVmRgiEVVEFaC-----------GIPNLLkTDFTdqiggGIDNWNLRQPLGVVAGITPFNFPMMVPCWMF 171
Cdd:PRK11904 636 GKTLQDAIAEV-R--EAVDF-CryyaaqarrlfGAPEKL-PGPT-----GESNELRLHGRGVFVCISPWNFPLAIFLGQV 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 172 PVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIH-TQAA 249
Cdd:PRK11904 706 AAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIAGVAFTGSTETARIINrTLAA 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 250 RRGKRVQ--ALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNA 327
Cdd:PRK11904 786 RDGPIVPliAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLL 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 328 DVEMGPLVTAAHRAKVSAYIDAgVAAGAKLVVdgRRHVVAGGENGFFLGGTLFDdvTTDMSIYREEIFGPVLAVVRVP-- 405
Cdd:PRK11904 866 STDVGPVIDAEAKANLDAHIER-MKREARLLA--QLPLPAGTENGHFVAPTAFE--IDSISQLEREVFGPILHVIRYKas 940
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 490304777 406 DFASAVELINAhefangvscfTSDG---GI-------ARAFARKIQVGMVGIN 448
Cdd:PRK11904 941 DLDKVIDAINA----------TGYGltlGIhsrieetADRIADRVRVGNVYVN 983
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
148-490 |
1.04e-42 |
|
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: 156.92 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 148 RQPLGVVAGITPFNFPM------MVPcwmfpvAIACGNTFVLKPSERDPSASIRLAELLKEAgLPDGVFNVVHGDKTAVD 221
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLqlalapLIG------AIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 222 ALIAHP-DVaaLSFVGSTPIAEYIHTQAARRGKRVQ-ALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAV 299
Cdd:cd07087 171 ALLAEPfDH--IFFTGSPAVGKIVMEAAAKHLTPVTlELGG-KSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 300 AVGGVADALVERLAERAKALkIGNGMNADVEMGPLVTAAHRAKVSAYIDAGvaagaKLVVDGRRHvvaggENGFFLGGTL 379
Cdd:cd07087 248 VHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGGQVD-----KEERYIAPTI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 380 FDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIpVPMAWHS 459
Cdd:cd07087 317 LDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVL-LHAAIPN 395
|
330 340 350
....*....|....*....|....*....|...
gi 490304777 460 --FGGWKRSLFGDHHayGEEGVRFYTRYKSVMQ 490
Cdd:cd07087 396 lpFGGVGNSGMGAYH--GKAGFDTFSHLKSVLK 426
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
68-448 |
3.87e-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: 156.99 E-value: 3.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFacgipnllktdFTDQIGGGIDNWNL 147
Cdd:TIGR01238 90 WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRY-----------YAKQVRDVLGEFSV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 148 RqPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAH 226
Cdd:TIGR01238 159 E-SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVgAALTSD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 227 PDVAALSFVGSTPIAEYIHTQAARRGK---RVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGG 303
Cdd:TIGR01238 238 PRIAGVAFTGSTEVAQLINQTLAQREDapvPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQED 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 304 VADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAgVAAGAKLVVDGRRHVVAGGENGFFLGGTLFDdv 383
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEH-MSQTQKKIAQLTLDDSRACQHGTFVAPTLFE-- 394
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304777 384 TTDMSIYREEIFGPVLAVVR--VPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGIN 448
Cdd:TIGR01238 395 LDDIAELSEEVFGPVLHVVRykARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN 461
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
68-464 |
5.52e-40 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 151.14 E-value: 5.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFACGIpnllktdfTDQIGGGI----- 142
Cdd:PLN02315 72 WMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGL--------SRQLNGSIipser 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 143 ------DNWNlrqPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRL----AELLKEAGLPDGVFNV 212
Cdd:PLN02315 144 pnhmmmEVWN---PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 213 VHGDKTAVDALIAHPDVAALSFVGSTPIAEYIHTQA-ARRGKRVQALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGER 291
Cdd:PLN02315 221 FCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVnARFGKCLLELSG-NNAIIVMDDADIQLAVRSVLFAAVGTAGQR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 292 CMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVDGRrhVVAGGEN 371
Cdd:PLN02315 300 CTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGS--AIESEGN 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 372 gfFLGGTLFdDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAF--ARKIQVGMVGINV 449
Cdd:PLN02315 378 --FVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWigPLGSDCGIVNVNI 454
|
410
....*....|....*
gi 490304777 450 PIPVPMAWHSFGGWK 464
Cdd:PLN02315 455 PTNGAEIGGAFGGEK 469
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
28-416 |
2.14e-39 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 153.10 E-value: 2.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 28 SDRYGDVFDPALGTVTARVPLASGAevdaavaaaaaaFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFS 107
Cdd:PRK11905 578 DDVVGTVTEASAEDVERALAAAQAA------------FPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLA 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 108 DAKGEVmRgiEVVEF----ACGIPNLLKTDftdqigggidnwnLRQPLGVVAGITPFNFPMMVpcwmF----PVAIACGN 179
Cdd:PRK11905 646 NAIAEV-R--EAVDFlryyAAQARRLLNGP-------------GHKPLGPVVCISPWNFPLAI----FtgqiAAALVAGN 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 180 TFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIH-TQAARRGKRVQ- 256
Cdd:PRK11905 706 TVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLIQrTLAKRSGPPVPl 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 257 -ALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLV 335
Cdd:PRK11905 786 iAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVI 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 336 TAAHRAKVSAYIDAGVAAGAKLvvdgrrHVVA---GGENGFFLGGTLFDdvTTDMSIYREEIFGPVLAVVRVP--DFASA 410
Cdd:PRK11905 866 DAEAQANIEAHIEAMRAAGRLV------HQLPlpaETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKadELDRV 937
|
....*.
gi 490304777 411 VELINA 416
Cdd:PRK11905 938 IDDINA 943
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
65-403 |
1.23e-37 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 147.78 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 65 FPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVmRgiEVVEF----AcgipNLLKTDFtdqigg 140
Cdd:COG4230 606 FPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEV-R--EAVDFcryyA----AQARRLF------ 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 141 giDNWNLRQPLGVVAGITPfnfpmmvpcWMFPVAI---------ACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFN 211
Cdd:COG4230 673 --AAPTVLRGRGVFVCISP---------WNFPLAIftgqvaaalAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQ 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 212 VVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIH-TQAARRGKRVqAL----GGaKNHLVVMPDANLDQAVDALVGAAY 285
Cdd:COG4230 742 LLPGDGETVgAALVADPRIAGVAFTGSTETARLINrTLAARDGPIV-PLiaetGG-QNAMIVDSSALPEQVVDDVLASAF 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 286 GSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKLvvdGRRHV 365
Cdd:COG4230 820 DSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLV---HQLPL 896
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 490304777 366 VAGGENGFFLGGTLF-----DDVTtdmsiyrEEIFGPVLAVVR 403
Cdd:COG4230 897 PEECANGTFVAPTLIeidsiSDLE-------REVFGPVLHVVR 932
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
148-489 |
4.61e-36 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 138.89 E-value: 4.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 148 RQPLGVVAGITPFNFPMMVPcwMFPV--AIACGNTFVLKPSERDPSASIRLAELLKEAgLPDGVFNVVHGDKTAVDALIA 225
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLA--LSPLvgAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 226 HP-DvaALSFVGSTPIAEYIHTQAARRGKRVQ-ALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGG 303
Cdd:cd07135 183 QKfD--KIFYTGSGRVGRIIAEAAAKHLTPVTlELGG-KSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 304 VADALVERLAeraKALK--IGNGMNADVEMGPLVTAAHRAKVSAYIDAgvaAGAKLVVDGRRhvvagGENGFFLGGTLFD 381
Cdd:cd07135 260 VYDEFVEELK---KVLDefYPGGANASPDYTRIVNPRHFNRLKSLLDT---TKGKVVIGGEM-----DEATRFIPPTIVS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 382 DVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGIN-----VPIP-VPm 455
Cdd:cd07135 329 DVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdtlihVGVDnAP- 407
|
330 340 350
....*....|....*....|....*....|....
gi 490304777 456 awhsFGGWKRSLFGDHHayGEEGVRFYTRYKSVM 489
Cdd:cd07135 408 ----FGGVGDSGYGAYH--GKYGFDTFTHERTVV 435
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
145-415 |
1.78e-35 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 138.87 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 145 WNLRQ--PL-GVVAGITPFNFpmmvpcwmfpVAIA---------CGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNV 212
Cdd:cd07123 162 WNRLEyrPLeGFVYAVSPFNF----------TAIGgnlagapalMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINF 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 213 VHGD-KTAVDALIAHPDVAALSFVGSTP--------IAEYIHTQaaRRGKRVQALGGAKNHLVVMPDANLDQAVDALVGA 283
Cdd:cd07123 232 VPGDgPVVGDTVLASPHLAGLHFTGSTPtfkslwkqIGENLDRY--RTYPRIVGETGGKNFHLVHPSADVDSLVTATVRG 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 284 AYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYID-AGVAAGAKlvvdgr 362
Cdd:cd07123 310 AFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDhAKSDPEAE------ 383
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490304777 363 rhVVAGGE----NGFFLGGTLFddVTTDMS--IYREEIFGPVLAVVRVPD--FASAVELIN 415
Cdd:cd07123 384 --IIAGGKcddsVGYFVEPTVI--ETTDPKhkLMTEEIFGPVLTVYVYPDsdFEETLELVD 440
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
19-416 |
2.60e-34 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 137.80 E-value: 2.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 19 IGGRALDGASDrygDVFDPA-LGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKELLDRHHDELAEL 97
Cdd:PRK11809 651 LEDPVAAGEMS---PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGL 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 98 ITREHGKVFSDAKGEVMrgiEVVEFacgipnlLKTdFTDQIGGGIDNWNLRqPLGVVAGITPFNFPMMVPCWMFPVAIAC 177
Cdd:PRK11809 728 LVREAGKTFSNAIAEVR---EAVDF-------LRY-YAGQVRDDFDNDTHR-PLGPVVCISPWNFPLAIFTGQVAAALAA 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 178 GNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDA-LIAHPDVAALSFVGSTPIAEYIHTQAARR----G 252
Cdd:PRK11809 796 GNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAaLVADARVRGVMFTGSTEVARLLQRNLAGRldpqG 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 253 KRVQ--ALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNADVE 330
Cdd:PRK11809 876 RPIPliAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTD 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 331 MGPLVTAAHRAKVSAYIDAGVAAGAKlVVDGRRHVVAGGENGFFLGGTL-----FDDVTtdmsiyrEEIFGPVLAVVRVP 405
Cdd:PRK11809 956 IGPVIDAEAKANIERHIQAMRAKGRP-VFQAARENSEDWQSGTFVPPTLieldsFDELK-------REVFGPVLHVVRYN 1027
|
410
....*....|...
gi 490304777 406 --DFASAVELINA 416
Cdd:PRK11809 1028 rnQLDELIEQINA 1040
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
144-490 |
1.64e-32 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 128.76 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 144 NWNLRQPLGVVAGITPFNFPMMVPcwMFPV--AIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVfNVVHGDktavd 221
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYLA--LGPLiaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV-AVVTGG----- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 222 aliahPDVAA---------LSFVGSTPIaeyihtqaarrGKRVQA------------LGGaKNHLVVMPDANLDQAVDAL 280
Cdd:cd07133 167 -----ADVAAafsslpfdhLLFTGSTAV-----------GRHVMRaaaenltpvtleLGG-KSPAIIAPDADLAKAAERI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 281 VGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALkIGNGMNADvEMGPLVTAAHRAKVSAYIDAGVAAGAKLVVD 360
Cdd:cd07133 230 AFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-YPTLADNP-DYTSIINERHYARLQGLLEDARAKGARVIEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 361 GRRHVVAGGENGFFLggTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKI 440
Cdd:cd07133 308 NPAGEDFAATRKLPP--TLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRT 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490304777 441 QVGMVGINVPIpvpmaWH------SFGGWKRSLFGDHHayGEEGVRFYTRYKSVMQ 490
Cdd:cd07133 386 HSGGVTINDTL-----LHvaqddlPFGGVGASGMGAYH--GKEGFLTFSHAKPVFK 434
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
149-490 |
3.34e-32 |
|
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: 128.11 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 149 QPLGVVAGITPFNFPMMVPcwMFPV--AIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFnVVHGDKTAVDALIAH 226
Cdd:cd07134 99 EPKGVCLIISPWNYPFNLA--FGPLvsAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEGDAEVAQALLEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 227 PdVAALSFVGSTPIAEYIHTQAARRGKRVQ-ALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVA 305
Cdd:cd07134 176 P-FDHIFFTGSPAVGKIVMAAAAKHLASVTlELGG-KSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 306 DALVERL-AERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAGVAAGAKlvvdgrrhVVAGGE---NGFFLGGTLFD 381
Cdd:cd07134 254 DAFVEHLkAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAK--------VEFGGQfdaAQRYIAPTVLT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 382 DVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDggiaRAFARKI----QVGMVGIN------VPI 451
Cdd:cd07134 326 NVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD----KANVNKVlartSSGGVVVNdvvlhfLNP 401
|
330 340 350
....*....|....*....|....*....|....*....
gi 490304777 452 PVPmawhsFGGWKRSLFGDHHayGEEGVRFYTRYKSVMQ 490
Cdd:cd07134 402 NLP-----FGGVNNSGIGSYH--GVYGFKAFSHERAVLR 433
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
147-491 |
5.82e-30 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 122.44 E-value: 5.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 147 LRQPLGVVAGITPFNFPM---MVPCwmfPVAIACGNTFVLKPSERDPSASIRLAELLKEAgLPDGVFNVVHGDKTAVDAL 223
Cdd:PTZ00381 106 IPEPLGVVLVIGAWNYPLnltLIPL---AGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 224 IAHP-DVaaLSFVGSTPIAEYIHTQAARrgKRVQA---LGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAV 299
Cdd:PTZ00381 182 LKEPfDH--IFFTGSPRVGKLVMQAAAE--NLTPCtleLGG-KSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 300 AVGGVADALVERLAERAKALkIGNGMNADVEMGPLVTAAHRAKVSAYIDAgvaAGAKLVVDGRrhvvaGGENGFFLGGTL 379
Cdd:PTZ00381 257 VHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGGE-----VDIENKYVAPTI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 380 FDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGIN------VPIPV 453
Cdd:PTZ00381 328 IVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcvfhlLNPNL 407
|
330 340 350
....*....|....*....|....*....|....*...
gi 490304777 454 PmawhsFGGWKRSLFGDHHayGEEGVRFYTRYKSVMQR 491
Cdd:PTZ00381 408 P-----FGGVGNSGMGAYH--GKYGFDTFSHPKPVLNK 438
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
148-491 |
8.53e-29 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 118.38 E-value: 8.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 148 RQPLGVVAGITPFNFPMMVPcwMFPV--AIACGNTFVLKPSERDPSASIRLAELLKEAgLPDGVFNVVHGDKTAVDALIA 225
Cdd:cd07136 98 YEPYGVVLIIAPWNYPFQLA--LAPLigAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELLD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 226 HP-DvaALSFVGSTPIAEYIHTQAARRGKRVQ-ALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVAVAVGG 303
Cdd:cd07136 175 QKfD--YIFFTGSVRVGKIVMEAAAKHLTPVTlELGG-KSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 304 VADALVERLAErakALKIGNGMNA--DVEMGPLVTAAHRAKVSAYIDAGvaagaklvvdgrrHVVAGG---ENGFFLGGT 378
Cdd:cd07136 252 VKEKFIKELKE---EIKKFYGEDPleSPDYGRIINEKHFDRLAGLLDNG-------------KIVFGGntdRETLYIEPT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 379 LFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGIN---------- 448
Cdd:cd07136 316 ILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtimhlanpy 395
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 490304777 449 VPipvpmawhsFGGWKRSLFGDHHayGEEGVRFYTRYKSVMQR 491
Cdd:cd07136 396 LP---------FGGVGNSGMGSYH--GKYSFDTFSHKKSILKK 427
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
149-472 |
9.49e-28 |
|
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: 115.20 E-value: 9.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 149 QPLGVVAGITPFNFPMMVPcwMFPV--AIACGNTFVLKPSERDPSASIRLAELLKEAgLPDGVFNVVHGDKTAVDALIAH 226
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLS--LEPVigAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEGGVPETTALLEQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 227 P-DvaALSFVGSTPIAEYIHTQAARRGKRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGS-AGERCMAISVAVAVGGV 304
Cdd:cd07137 177 KwD--KIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEESF 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 305 ADALVERLAERAKALKIGNGMNADvEMGPLVTAAHRAKVSAYIDAGVAAgAKLVVDGRRHvvaggENGFFLGGTLFDDVT 384
Cdd:cd07137 255 APTLIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGGERD-----EKNLYIEPTILLDPP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 385 TDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIpVPMAWHS--FGG 462
Cdd:cd07137 328 LDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTV-VQYAIDTlpFGG 406
|
330
....*....|
gi 490304777 463 WKRSLFGDHH 472
Cdd:cd07137 407 VGESGFGAYH 416
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
149-491 |
7.66e-22 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 98.19 E-value: 7.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 149 QPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLkEAGLPDGVFNVVHGDKTAVDALIAHpD 228
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQ-K 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 229 VAALSFVGSTPIAEYIHTQAARRGKRVQALGGAKNHLVVMPDANLDQAVDALVGAAYG-SAGERCMAISVAVAVGGVADA 307
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYAPK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 308 LVERLAERAKALKIGNGMNADvEMGPLVTAAHRAKVSAYIDagvaagAKLVVDgrrHVVAGGEN---GFFLGGTLFDDVT 384
Cdd:PLN02174 269 VIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLD------EKEVSD---KIVYGGEKdreNLKIAPTILLDVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 385 TDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINvPIPVPMAWHS--FGG 462
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVN-DIAVHLALHTlpFGG 417
|
330 340
....*....|....*....|....*....
gi 490304777 463 WKRSLFGDHHayGEEGVRFYTRYKSVMQR 491
Cdd:PLN02174 418 VGESGMGAYH--GKFSFDAFSHKKAVLYR 444
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
149-491 |
1.86e-20 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 94.02 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 149 QPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKeAGLPDGVFNVVHGDKTAVDALIAHPD 228
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP-KYLDSKAVKVIEGGPAVGEQLLQHKW 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 229 VAALsFVGSTPIAEYIHTQAARRGKRVQ-ALGGAKNHLVVMPDANLDQ--AVDALVGAAYGS-AGERCMAISVAVAVGGV 304
Cdd:PLN02203 186 DKIF-FTGSPRVGRIIMTAAAKHLTPVAlELGGKCPCIVDSLSSSRDTkvAVNRIVGGKWGScAGQACIAIDYVLVEERF 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 305 ADALVERLAERAKALKIGNGMNADvEMGPLVTAAHRAKVSAYI-DAGVAAGaklvvdgrrhVVAGG---ENGFFLGGTLF 380
Cdd:PLN02203 265 APILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLkDPRVAAS----------IVHGGsidEKKLFIEPTIL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 381 DDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIpVPMAWHS- 459
Cdd:PLN02203 334 LNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAI-IQYACDSl 412
|
330 340 350
....*....|....*....|....*....|...
gi 490304777 460 -FGGWKRSLFGDHHayGEEGVRFYTRYKSVMQR 491
Cdd:PLN02203 413 pFGGVGESGFGRYH--GKYSFDTFSHEKAVLRR 443
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
15-437 |
2.63e-20 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 94.00 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 15 LAHFIGGRALDGASDryGDV-FDPALGTVTARVP-----LASGAEVDAAVAAAAAAFPAWSETSPLKRARVmfkfkELLD 88
Cdd:PRK11903 5 LANYVAGRWQAGSGA--GTPlFDPVTGEELVRVSatgldLAAAFAFAREQGGAALRALTYAQRAALLAAIV-----KVLQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 89 RHHDELAELITREHGKVFSDAKGEVMRGIEVVEF------ACGIPNLLKTDFTDQIGggidnwnlRQPL----------- 151
Cdd:PRK11903 78 ANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYyaklgaALGDARLLRDGEAVQLG--------KDPAfqgqhvlvptr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 152 GVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAG-LPDGVFNVVHGDKTAVDALIAHPDVa 230
Cdd:PRK11903 150 GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHLQPFDV- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 231 aLSFVGSTPIAEYI--HTQAARRGKRVQALGGAKNHLVVMPDANLD-QAVDALVGAAYGS----AGERCMAISVAVAVGG 303
Cdd:PRK11903 229 -VSFTGSAETAAVLrsHPAVVQRSVRVNVEADSLNSALLGPDAAPGsEAFDLFVKEVVREmtvkSGQKCTAIRRIFVPEA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 304 VADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAgVAAGAKLVVDGRRHVVAGGEN--GFFLGGTLF- 380
Cdd:PRK11903 308 LYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGFALVDADPavAACVGPTLLg 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 490304777 381 -DDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFA 437
Cdd:PRK11903 387 aSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAA 444
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
148-491 |
2.59e-19 |
|
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: 90.36 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 148 RQPLGVVAGITPFNFPMMVPcwMFPV--AIACGNTFVLKPSERDPSASIRLAELL-----KEAglpdgvFNVVHGDKTAV 220
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQLT--LVPLvgAIAAGNCVVIKPSEVSPATAKLLAELIpkyldKEC------YPVVLGGVEET 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 221 DALIAHP-DVaaLSFVGSTPIAEYIHTQAARRGKRVQ-ALGGaKNHLVVMPDANLDQAVDALVGAAYGSAGERCMAISVA 298
Cdd:cd07132 170 TELLKQRfDY--IFYTGSTSVGKIVMQAAAKHLTPVTlELGG-KSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 299 VAVGGVADALVERLAeraKALK--IGNGMNADVEMGPLVTAAHRAKVSAYIDAGvaagaKLVVDGRrhvvaGGENGFFLG 376
Cdd:cd07132 247 LCTPEVQEKFVEALK---KTLKefYGEDPKESPDYGRIINDRHFQRLKKLLSGG-----KVAIGGQ-----TDEKERYIA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 377 GTLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIpVPMA 456
Cdd:cd07132 314 PTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTI-MHYT 392
|
330 340 350
....*....|....*....|....*....|....*..
gi 490304777 457 WHS--FGGWKRSLFGDHHayGEEGVRFYTRYKSVMQR 491
Cdd:cd07132 393 LDSlpFGGVGNSGMGAYH--GKYSFDTFSHKRSCLVK 427
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
68-418 |
3.74e-19 |
|
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: 89.91 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 68 WSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDAKGEVMRGI--------EVVEfacGIPNLLKTDFTDQIG 139
Cdd:cd07129 15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTgqlrlfadLVRE---GSWLDARIDPADPDR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 140 GGIDNWNLRQ---PLGVVAGITPFNFPMMvpcwmFPV-------AIACGNTFVLKPSERDPSASIRLAEL----LKEAGL 205
Cdd:cd07129 92 QPLPRPDLRRmlvPLGPVAVFGASNFPLA-----FSVaggdtasALAAGCPVVVKAHPAHPGTSELVARAiraaLRATGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 206 PDGVFNVVHGDKTAV-DALIAHPDVAALSFVGSTPIAEYIHTQAARR--GKRVQALGGAKNHLVVMPDA---NLDQAVDA 279
Cdd:cd07129 167 PAGVFSLLQGGGREVgVALVKHPAIKAVGFTGSRRGGRALFDAAAARpePIPFYAELGSVNPVFILPGAlaeRGEAIAQG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 280 LVGAAYGSAGERCMAISVAVAVGGVA-DALVERLAERAkalkigngmnADVEMGPLVTAAHRAkvsAYiDAGVAAGAKlv 358
Cdd:cd07129 247 FVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEAL----------AAAPAQTMLTPGIAE---AY-RQGVEALAA-- 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490304777 359 VDGRRHVVAGG--ENGFFLGGTLFddvTTDMSIYR------EEIFGPVLAVVRVPDFASAVELINAHE 418
Cdd:cd07129 311 APGVRVLAGGAaaEGGNQAAPTLF---KVDAAAFLadpalqEEVFGPASLVVRYDDAAELLAVAEALE 375
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
75-414 |
1.11e-18 |
|
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: 88.45 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 75 KRARVMFKFKELLDRHHDELAelitreHGKVFSDAKGEVM-----------RGIEVVEFACGIPNllKTDFTDQIGGGID 143
Cdd:cd07084 22 KRADFLARIIQRLAAKSYDIA------AGAVLVTGKGWMFaenicgdqvqlRARAFVIYSYRIPH--EPGNHLGQGLKQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 144 NWNLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAG-LPDGVFNVVHGDKTAVDA 222
Cdd:cd07084 94 SHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKTMQA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 223 LIAHPDVAALSFVGSTPIAEYIHTQAARrgKRVQALGGAKNHLVVMPDAN-LDQAVDALVGAAYGSAGERCMAISVAVAv 301
Cdd:cd07084 174 LLLHPNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFV- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 302 ggVADALVERLAERAKALkIGNGMNADVEMGPLVTAAHRAKVSAyidAGVAAGAKLVVDGR-RHVVAGGEN-GFFLGGTL 379
Cdd:cd07084 251 --PENWSKTPLVEKLKAL-LARRKLEDLLLGPVQTFTTLAMIAH---MENLLGSVLLFSGKeLKNHSIPSIyGACVASAL 324
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 490304777 380 F---DDVTTDMSIYREEIFGPV--LAVVRVPDFASAVELI 414
Cdd:cd07084 325 FvpiDEILKTYELVTEEIFGPFaiVVEYKKDQLALVLELL 364
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
152-444 |
8.64e-17 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 83.09 E-value: 8.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 152 GVVAGITPFNFPmmvpCW----MFPVAIACGNTFVLKPSERDPSASIRLAELLKEAG-LPDGVFNVVHGDKTAVDALIAH 226
Cdd:cd07128 146 GVAVHINAFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 227 PDVaaLSFVGSTPIAEYIHTQAA--RRGKRVQALGGAKNHLVVMPDANLDQA-----VDALVGAAYGSAGERCMAISVAV 299
Cdd:cd07128 222 QDV--VAFTGSAATAAKLRAHPNivARSIRFNAEADSLNAAILGPDATPGTPefdlfVKEVAREMTVKAGQKCTAIRRAF 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 300 AVGGVADALVERLAERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYIDAgVAAGAKLVVDGRRHVVAGG---ENGFFLG 376
Cdd:cd07128 300 VPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDRFEVVGadaEKGAFFP 378
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 377 GTLF--DDVTTDMSIYREEIFGPVLAVVRVPDFASAVELINAHEFANGVSCFTSDggiaRAFARKIQVGM 444
Cdd:cd07128 379 PTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND----PAFARELVLGA 444
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
125-450 |
9.78e-15 |
|
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: 76.15 E-value: 9.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 125 GIPNLLKTDFTDQIGGGIDNW---NLRQPLGVVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLK 201
Cdd:cd07081 67 YIYNVYKDEKTCGVLTGDENGgtlIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 202 EA----GLPDGVFNVV-HGDKTAVDALIAHPDVAALSFVGSTPIAEyihtQAARRGKRVQALGGAKNHLVVMPDANLDQA 276
Cdd:cd07081 147 QAavaaGAPENLIGWIdNPSIELAQRLMKFPGIGLLLATGGPAVVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 277 VDALVGAAYGSAGERCMAISVAVAVGGVADALVERLAERAKALKIGNGMNA-------DVEMGPLVTAAHRAKVSAYIDA 349
Cdd:cd07081 223 VQSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQvqpvilkNGDVNRDIVGQDAYKIAAAAGL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 350 GVAAGAKLVVDgrrHVVAGGENGFFLggtlfddvttdmsiyrEEIFGPVLAVVRVPDFASAVELINAHEFANGV---SCF 426
Cdd:cd07081 303 KVPQETRILIG---EVTSLAEHEPFA----------------HEKLSPVLAMYRAANFADADAKALALKLEGGCghtSAM 363
|
330 340
....*....|....*....|....*...
gi 490304777 427 TSDGGIARA----FARKIQVGMVGINVP 450
Cdd:cd07081 364 YSDNIKAIEnmnqFANAMKTSRFVKNGP 391
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
79-424 |
1.41e-14 |
|
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: 76.00 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 79 VMFKFKELLDRHHDE--LAELITREHGKVFSDAKGEVMRGIEVVE-FACGIPNLLKTDFTdqIGG---GIDNWNLRQPLG 152
Cdd:cd07126 67 VSHRVAHELRKPEVEdfFARLIQRVAPKSDAQALGEVVVTRKFLEnFAGDQVRFLARSFN--VPGdhqGQQSSGYRWPYG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 153 VVAGITPFNFPMMVPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAAL 232
Cdd:cd07126 145 PVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 233 SFVGSTPIAEYIHTQAARRGKRVQALGGAKnhlVVMPD-ANLDQAVDALVGAAYGSAGERCMAISVAVAVGGVADA-LVE 310
Cdd:cd07126 225 LFTGSSKVAERLALELHGKVKLEDAGFDWK---ILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAgILD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 311 RLAERAKALKIgngmnADVEMGPLVT------AAHRAKVSAYIDAGVAAGAKLVVDGRRHVVAGG--------------- 369
Cdd:cd07126 302 KLKALAEQRKL-----EDLTIGPVLTwtteriLDHVDKLLAIPGAKVLFGGKPLTNHSIPSIYGAyeptavfvpleeiai 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490304777 370 -ENgfflggtlFDDVTTdmsiyreEIFGPVLAVV-----RVPDFASAVELINAHEFANGVS 424
Cdd:cd07126 377 eEN--------FELVTT-------EVFGPFQVVTeykdeQLPLVLEALERMHAHLTAAVVS 422
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
150-313 |
8.42e-11 |
|
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: 63.78 E-value: 8.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 150 PLGVVAGITPFNFPMMVPCWMFpVAIACGNTFVLKPSERDPsASIRLAELLKEAGLPDG-----VFNVVHGDKTAVDALI 224
Cdd:cd07077 100 PIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHgpkilVLYVPHPSDELAEELL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 225 AHPDVAALSFVGSTPIAEYIhtQAARRGKRVQALGGAKNHLVVMPDANLDQAVDALVGAA--YGSAgerCMAISVAVAVG 302
Cdd:cd07077 178 SHPKIDLIVATGGRDAVDAA--VKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKffDQNA---CASEQNLYVVD 252
|
170
....*....|.
gi 490304777 303 GVADALVERLA 313
Cdd:cd07077 253 DVLDPLYEEFK 263
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
148-422 |
6.57e-09 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 58.02 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 148 RQPLGVVAGITPF---------NFPMMvpcwmfpvaIACGNTFVLKPSERDPSASIRLAELL----KEAGLPDGVFNVVH 214
Cdd:cd07121 95 YAPFGVIGAITPStnptetiinNSISM---------LAAGNAVVFNPHPGAKKVSAYAVELInkaiAEAGGPDNLVVTVE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 215 G-DKTAVDALIAHPDVAALSFVGSTPIAEyihtQAARRGKRVQAlGGAKNHLVVMPD-ANLDQAVDALVGAAYGSAGERC 292
Cdd:cd07121 166 EpTIETTNELMAHPDINLLVVTGGPAVVK----AALSSGKKAIG-AGAGNPPVVVDEtADIEKAARDIVQGASFDNNLPC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 293 MAISVAVAVGGVADALVERLaERAKALKIGNGMNADVEMGPLVTAAHRAKVSAYI--DAGVAAGAKLVVDGRRHVVagge 370
Cdd:cd07121 241 IAEKEVIAVDSVADYLIAAM-QRNGAYVLNDEQAEQLLEVVLLTNKGATPNKKWVgkDASKILKAAGIEVPADIRL---- 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490304777 371 ngfflggtLFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVELinAHEFANG 422
Cdd:cd07121 316 --------IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIEL--AVELEHG 357
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
149-462 |
9.86e-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: 57.50 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 149 QPLGVVAGITPFNFPMMVPcwMFPVAIA--CGNTFVLKPSERDPSASIRLAELLKEA----GLPDGVFNVV-HGDKTAVD 221
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTA--IFKALIAlkTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIeEPSIELTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 222 ALIAHPDVAALSFVGSTPIaeyihTQAARR-GKrvQALG-GAKNHLVVM-PDANLDQAVDALVGAA---YGSAgerCMAI 295
Cdd:cd07122 172 ELMKHPDVDLILATGGPGM-----VKAAYSsGK--PAIGvGPGNVPAYIdETADIKRAVKDIILSKtfdNGTI---CASE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 296 SVAVAVGGVADALVERLAER--------------AKALKIGNGMNADVeMGplVTAAHRAKVsayidAG--VAAGAKLVV 359
Cdd:cd07122 242 QSVIVDDEIYDEVRAELKRRgayflneeekekleKALFDDGGTLNPDI-VG--KSAQKIAEL-----AGieVPEDTKVLV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 360 DGRRHVvagGENgfflggtlfddvttdmSIYREEIFGPVLAVVRVPDFASAVEL---INAHEFAnGVSC--FTSDGGIAR 434
Cdd:cd07122 314 AEETGV---GPE----------------EPLSREKLSPVLAFYRAEDFEEALEKareLLEYGGA-GHTAviHSNDEEVIE 373
|
330 340
....*....|....*....|....*...
gi 490304777 435 AFARKIQVGMVGINVPipvpmawHSFGG 462
Cdd:cd07122 374 EFALRMPVSRILVNTP-------SSLGG 394
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
150-413 |
1.87e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 56.45 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 150 PLGVVAGITPFNFP---------MMvpcwmfpvaIACGNTFVLKPSERDPSASIRLAELLKEA----GLPDGVFNVV-HG 215
Cdd:PRK15398 129 PFGVIGAVTPSTNPtetiinnaiSM---------LAAGNSVVFSPHPGAKKVSLRAIELLNEAivaaGGPENLVVTVaEP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 216 DKTAVDALIAHPDVAALSFVGSTPIAEyihtQAARRGKRVQAlGGAKNHLVVMPD-ANLDQAVDALV-GAAYGSaGERCM 293
Cdd:PRK15398 200 TIETAQRLMKHPGIALLVVTGGPAVVK----AAMKSGKKAIG-AGAGNPPVVVDEtADIEKAARDIVkGASFDN-NLPCI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 294 AISVAVAVGGVADALVERLaERAKALkigngmnadvemgpLVTAAHRAKV-SAYIDAGVAAGAKLVvdGRRHVVAGGENG 372
Cdd:PRK15398 274 AEKEVIVVDSVADELMRLM-EKNGAV--------------LLTAEQAEKLqKVVLKNGGTVNKKWV--GKDAAKILEAAG 336
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490304777 373 FFLGGT---LFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVEL 413
Cdd:PRK15398 337 INVPKDtrlLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIAL 380
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
6-484 |
3.56e-08 |
|
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440272 [Multi-domain] Cd Length: 975 Bit Score: 56.21 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 6 HSNDSRVRALAHFIGGRALDGASDRYGDVFDPALGTVTARVPLASGAEVDAAVAAAAAAFPAWSETSPLKRARVMFKFKE 85
Cdd:COG0506 480 LAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 86 LLDRHHDELAELITREHGKVFSDAKGEVMRGIEVVEFACGIPNLLKTDFTDQIGGGIDNWNLRQPLGVVAGITPFNFPMM 165
Cdd:COG0506 560 AEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAAAAAAAA 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 166 VPCWMFPVAIACGNTFVLKPSERDPSASIRLAELLKEAGLPDGVFNVVHGDKTAVDALIAHPDVAALSFVGSTPIaeyih 245
Cdd:COG0506 640 AAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAA----- 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 246 TQAARRGKRVQALGGAKNHLVVMPDANLDQAVDALVGAAYGSAGERCmAISVAVAVGGVADALVERLAERAKALKIGNGM 325
Cdd:COG0506 715 AAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAA-ASASASASLLSLLALLLLDADLVILLLALAAA 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 326 NADVEMGPLVTAAHRAKVSAYIDA-----GVAAGAKLVVDGRRHVVAGGENGFFLGGTLFDDVTTDMSIYREEIFGPVLA 400
Cdd:COG0506 794 AAALLVGGPGAAALALGIVEDAAAaalllALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLAL 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 401 VVRVPDFASAVELINAHEFANGVSCFTSDGGIARAFARKIQVGMVGINVPIPVPMAWHSFGGWKRSLFGDHHAYGEEGVR 480
Cdd:COG0506 874 VLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAG 953
|
....
gi 490304777 481 FYTR 484
Cdd:COG0506 954 TLAL 957
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
64-413 |
6.29e-04 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 42.47 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 64 AFPAWSETSPLKRARVMFKFKELLDRHHDELAELITREHGKVFSDA-----KGEVMRGIEVVEFA----CGIPnllKTDF 134
Cdd:cd07127 96 AMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAfqaggPHAQDRGLEAVAYAwremSRIP---PTAE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 135 TDQIGGGIDNWNLRQPLGVVagitPFNFPMMVPCWMFPV---------AIACGNTFVLKPSerdPSASIRLA-------E 198
Cdd:cd07127 173 WEKPQGKHDPLAMEKTFTVV----PRGVALVIGCSTFPTwngypglfaSLATGNPVIVKPH---PAAILPLAitvqvarE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 199 LLKEAGL-PDGVFNVVH--GDKTAvDALIAHPDVAALSFVGSTPIAEYIHTQAarRGKRVQALGGAKNHLVVMPDANLDQ 275
Cdd:cd07127 246 VLAEAGFdPNLVTLAADtpEEPIA-QTLATRPEVRIIDFTGSNAFGDWLEANA--RQAQVYTEKAGVNTVVVDSTDDLKA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304777 276 AVDALVGAAYGSAGERCMAI-SVAVAVGGVA--------DALVERLAERAKALkIGNGMNADVEMGPLVTAAHRAKVsay 346
Cdd:cd07127 323 MLRNLAFSLSLYSGQMCTTPqNIYVPRDGIQtddgrksfDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARI--- 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304777 347 idAGVAAGAKLVVDGRRHvvaggENGFFLGGT-----LFDDVTTDMSIYREEIFGPVLAVVRVPDFASAVEL 413
Cdd:cd07127 399 --AEARQLGEVLLASEAV-----AHPEFPDARvrtplLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIEL 463
|
|
| |
