|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
4-482 |
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: 775.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 4 LGHFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNEL 83
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 84 AEMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPA 163
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 164 IACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKR 243
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 244 AQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVPVGEEtANRLIDKLVPMVESLRIGPYTDEKADMGP 323
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDE-ADEWIPKLVERAKKLKVGAGDDPGADMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 324 VVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSL 403
Cdd:cd07085 320 VISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550356027 404 PMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGGWKSSSFGDLNQHGTDSIKFWTRTKTITSRW 482
Cdd:cd07085 400 INANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
6-482 |
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: 583.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 6 HFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAE 85
Cdd:TIGR01722 3 HWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 86 MLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIA 165
Cdd:TIGR01722 83 LITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 166 CGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQ 245
Cdd:TIGR01722 163 CGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 246 CFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVPVGEetANRLIDKLVPMVESLRIGPYTDEKADMGPVV 325
Cdd:TIGR01722 243 ALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGA--ADEWVPEIRERAEKIRIGPGDDPGAEMGPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 326 TKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPM 405
Cdd:TIGR01722 321 TPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALIN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550356027 406 KHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGGWKSSSFGDLNQHGTDSIKFWTRTKTITSRW 482
Cdd:TIGR01722 401 ASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
3-482 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 557.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 3 ELGHFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNE 82
Cdd:COG1012 5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 83 LAEMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAP 162
Cdd:COG1012 85 LAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 163 AIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGD-KGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNG 241
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 242 KRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDEKADM 321
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLL-VHESIYDEFVERLVAAAKALKVGDPLDPGTDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 322 GPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLqgyENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEAL 401
Cdd:COG1012 324 GPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDG---EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 402 SLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGGWKSSSFGDlnQHGTDSIKFWTRTKTITSR 481
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGR--EGGREGLEEYTETKTVTIR 478
|
.
gi 1550356027 482 W 482
Cdd:COG1012 479 L 479
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
6-496 |
6.49e-162 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 471.92 E-value: 6.49e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 6 HFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAE 85
Cdd:PLN02419 116 NLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 86 MLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIA 165
Cdd:PLN02419 196 NITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 166 CGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQ 245
Cdd:PLN02419 276 CGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQ 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 246 CFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVPVGEetANRLIDKLVPMVESLRIGPYTDEKADMGPVV 325
Cdd:PLN02419 356 SNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGD--AKSWEDKLVERAKALKVTCGSEPDADLGPVI 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 326 TKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPM 405
Cdd:PLN02419 434 SKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIIN 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 406 KHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGGWKSSSFGDLNQHGTDSIKFWTRTKTITSRWPSg 485
Cdd:PLN02419 514 KNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQKD- 592
|
490
....*....|.
gi 1550356027 486 IKDGAEFSIPT 496
Cdd:PLN02419 593 IHSPFSLAIPI 603
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
13-478 |
3.32e-155 |
|
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: 449.67 E-value: 3.32e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 13 VAGTSGRVSNIfNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHG 92
Cdd:pfam00171 2 VDSESETIEVI-NPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 93 KTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAgPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFIL 172
Cdd:pfam00171 81 KPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSD-PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 173 KPSERDPSVPIRLAELMIEAGLPAGILNVVNGD-KGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAK 251
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 252 NHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQ 331
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLL-VHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 332 RIRSLIDSGIEQGAKLVVDGRDfklqGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGN 411
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEA----GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550356027 412 GVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGGWKSSSFGDLNqhGTDSIKFWTRTKTI 478
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
54-479 |
1.29e-135 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 398.50 E-value: 1.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 54 QPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVRGLEVCEFVIG-IPHLQKSEFTEGaGPGID 132
Cdd:cd07078 11 FKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGlARRLHGEVIPSP-DPGEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 133 MYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DA 211
Cdd:cd07078 90 AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVgAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 212 ILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVaVPVG 291
Cdd:cd07078 170 LASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASR-LLVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 292 EETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGrdfKLQGYENGHFIGGCLFD 371
Cdd:cd07078 249 ESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGG---KRLEGGKGYFVPPTVLT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 372 DVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFG 451
Cdd:cd07078 326 DVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPSAPFG 405
|
410 420
....*....|....*....|....*...
gi 1550356027 452 GWKSSSFGdlNQHGTDSIKFWTRTKTIT 479
Cdd:cd07078 406 GVKQSGIG--REGGPYGLEEYTEPKTVT 431
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-478 |
8.20e-129 |
|
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: 382.75 E-value: 8.20e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 6 HFIDGKRVAGTSGRVSniFNPA-TGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELA 84
Cdd:cd07097 3 NYIDGEWVAGGDGEEN--RNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 85 EMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAI 164
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 165 ACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKR 243
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 244 AQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDEKADMGP 323
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLI-VTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 324 VVTKEAEQRIRSLIDSGIEQGAKLVVDGRdfKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSL 403
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGE--RLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550356027 404 PMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIpVPLAYHS-FGGWKSSSFGDLNQhGTDSIKFWTRTKTI 478
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPT-AGVDYHVpFGGRKGSSYGPREQ-GEAALEFYTTIKTV 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
6-479 |
1.36e-116 |
|
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: 351.65 E-value: 1.36e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 6 HFIDGKRVAGTSGRVSNIFNPATG-EVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELA 84
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 85 EMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAI 164
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 165 ACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKR 243
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 244 AQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDEKADMGP 323
Cdd:cd07131 241 VALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLI-VHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 324 VVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSL 403
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550356027 404 PMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGGWKSSSFGdLNQHGTDSIKFWTRTKTIT 479
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHLPFGGVKKSGNG-HREAGTTALDAFTEWKAVY 474
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
54-479 |
1.71e-104 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 316.86 E-value: 1.71e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 54 QPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDM 133
Cdd:cd06534 7 FKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 134 YSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGD-KGAVDAI 212
Cdd:cd06534 87 YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGgDEVGAAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 213 LTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGE 292
Cdd:cd06534 167 LSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLL-VHE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 293 ETANRLIDKLVpmveslrigpytdekadmgpvvtkeaeqrirslidsgieqgaklvvdgrdfklqgyenghfiggCLFDD 372
Cdd:cd06534 246 SIYDEFVEKLV----------------------------------------------------------------TVLVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 373 VTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGG 452
Cdd:cd06534 262 VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFGG 341
|
410 420
....*....|....*....|....*..
gi 1550356027 453 WKSSSFGdlNQHGTDSIKFWTRTKTIT 479
Cdd:cd06534 342 VKNSGIG--REGGPYGLEEYTRTKTVV 366
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
23-459 |
6.25e-100 |
|
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: 307.82 E-value: 6.25e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDI 102
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 103 VRGLEVCEF-------VIGiphlqksEFTEGAGPGIDMYSIRQPVGIGAGITPFNFpgmiPMWMF----APAIACGNAFI 171
Cdd:cd07103 81 DYAASFLEWfaeearrIYG-------RTIPSPAPGKRILVIKQPVGVVAAITPWNF----PAAMItrkiAPALAAGCTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 172 LKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAqCF--G 248
Cdd:cd07103 150 LKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRV-SLelG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 249 GaknH--MIIMPDADLDQAANALIGAGYGSAGERCMA---ISVAVPVgeetANRLIDKLVPMVESLRIGPYTDEKADMGP 323
Cdd:cd07103 229 G---NapFIVFDDADLDKAVDGAIASKFRNAGQTCVCanrIYVHESI----YDEFVEKLVERVKKLKVGNGLDEGTDMGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 324 VVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSL 403
Cdd:cd07103 302 LINERAVEKVEALVEDAVAKGAKVLTGGKRLGLGGY----FYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIAR 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1550356027 404 PMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPvPLAYHSFGGWKSSSFG 459
Cdd:cd07103 378 ANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLI-SDAEAPFGGVKESGLG 432
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
6-479 |
5.72e-99 |
|
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: 306.41 E-value: 5.72e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 6 HFIDGKRVAGTSGRVSNIfNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAE 85
Cdd:cd07086 1 GVIGGEWVGSGGETFTSR-NPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 86 MLSREHGKTIDDAKGDIVRGLEVCEFVIG---------IPhlqkSEFtegagPGIDMYSIRQPVGIGAGITPFNFPGMIP 156
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGlsrmlygltIP----SER-----PGHRLMEQWNPLGVVGVITAFNFPVAVP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 157 MWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEA----GLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARY 232
Cdd:cd07086 151 GWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 233 VYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIG 312
Cdd:cd07086 231 VGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLI-VHESVYDEFLERLVKAYKQVRIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 313 PYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRdfKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVV 392
Cdd:cd07086 310 DPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGK--RIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 393 RARNYEEALSLPMKHEYGNGVAIYTRDGDAARDF--ASRINIGMVGVNVPI---PVPLAyhsFGGWKSSSFGdlNQHGTD 467
Cdd:cd07086 388 KFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTsgaEIGGA---FGGEKETGGG--RESGSD 462
|
490
....*....|..
gi 1550356027 468 SIKFWTRTKTIT 479
Cdd:cd07086 463 AWKQYMRRSTCT 474
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
54-479 |
1.13e-98 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 304.07 E-value: 1.13e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 54 QPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDM 133
Cdd:cd07104 13 QKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDVPGKES 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 134 YSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDP-SVPIRLAELMIEAGLPAGILNVVNGDKGAV-DA 211
Cdd:cd07104 93 MVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvTGGLLIAEIFEEAGLPKGVLNVVPGGGSEIgDA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 212 ILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAIS---VAV 288
Cdd:cd07104 173 LVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGrilVHE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 289 PVGEETANRLIDKlvpmVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRdfklqgyENGHFIGGC 368
Cdd:cd07104 253 SVYDEFVEKLVAK----AKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT-------YEGLFYQPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 369 LFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYH 448
Cdd:cd07104 322 VLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDEPHV 401
|
410 420 430
....*....|....*....|....*....|.
gi 1550356027 449 SFGGWKSSSFGDLNqhGTDSIKFWTRTKTIT 479
Cdd:cd07104 402 PFGGVKASGGGRFG--GPASLEEFTEWQWIT 430
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
23-478 |
3.24e-98 |
|
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: 303.84 E-value: 3.24e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDI 102
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 103 VRGLEVCEFVIGI-PHLQKSEFTEGAGPGIdmYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSV 181
Cdd:cd07090 81 DSSADCLEYYAGLaPTLSGEHVPLPGGSFA--YTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 182 PIRLAELMIEAGLPAGILNVVNGDkGAVDAILT-HPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDA 260
Cdd:cd07090 159 ALLLAEILTEAGLPDGVFNVVQGG-GETGQLLCeHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 261 DLDQAANALIGAGYGSAGERCM-AISVAVPvgEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDS 339
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSnGTRVFVQ--RSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 340 GIEQGAKLVVDGRDFKLQ-GYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTR 418
Cdd:cd07090 316 AKQEGAKVLCGGERVVPEdGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550356027 419 DGDAARDFASRINIGMVGVN----VPIPVPlayhsFGGWKSSSFGDLNqhGTDSIKFWTRTKTI 478
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
23-478 |
2.78e-97 |
|
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: 301.39 E-value: 2.78e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPATGEVQGTVALASDADLAAAVESAKA--AQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKG 100
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAafEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 101 DIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPS 180
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 181 VPIRLAELMIEAGLPAGILNVVNGD-KGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPD 259
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 260 ADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDS 339
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLL-VQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 340 GIEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRD 419
Cdd:cd07114 320 AREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550356027 420 GDAARDFASRINIGMVGVNvpipvplAYHS------FGGWKSSSFGDLNqhGTDSIKFWTRTKTI 478
Cdd:cd07114 400 LARAHRVARAIEAGTVWVN-------TYRAlspsspFGGFKDSGIGREN--GIEAIREYTQTKSV 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
23-479 |
3.62e-97 |
|
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: 301.02 E-value: 3.62e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAK-GD 101
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 102 IVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDmYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSV 181
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALN-YVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 182 PIRLAELMIEAGLPAGILNVVNGD-KGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDA 260
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 261 DLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSG 340
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGS-RILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 341 IEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDG 420
Cdd:cd07093 319 RAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550356027 421 DAARDFASRINIGMVGVNVPI----PVPlayhsFGGWKSSSFGdlNQHGTDSIKFWTRTKTIT 479
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLvrdlRTP-----FGGVKASGIG--REGGDYSLEFYTELKNVC 454
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
25-478 |
2.61e-96 |
|
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: 298.58 E-value: 2.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 25 NPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKG-DIV 103
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 104 RGLEVCEFVIGIPHLQKSEFTEGAGPGIDmYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPI 183
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRGPFLN-YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 184 RLAELMIEAGLPAGILNVVNGdKGAV--DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDAD 261
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTG-FGEVagAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 262 LDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGI 341
Cdd:cd07115 241 LDAAVRAAATGIFYNQGQMCTAGS-RLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 342 EQGAKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGD 421
Cdd:cd07115 320 EEGARLLTGGKRPGARGF----FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLG 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550356027 422 AARDFASRINIGMVGVN----VPIPVPlayhsFGGWKSSSFGdlNQHGTDSIKFWTRTKTI 478
Cdd:cd07115 396 RAHRVAAALKAGTVWINtynrFDPGSP-----FGGYKQSGFG--REMGREALDEYTEVKSV 449
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
7-478 |
4.02e-94 |
|
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: 293.40 E-value: 4.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEM 86
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 87 LSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIAC 166
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 167 GNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDkGAV--DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRA 244
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGR-GSVvgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 245 QCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVaVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPV 324
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAER-VYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 325 VTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLqgyENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLP 404
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGGKRPEG---EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550356027 405 MKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPL-AYHSfgGWKSSSF-GDLNQHGtdsIKFWTRTKTI 478
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMqGFHA--GWKKSGLgGADGKHG---LEEYLQTKVV 466
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
6-478 |
1.21e-93 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 292.94 E-value: 1.21e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 6 HFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAE 85
Cdd:PRK13252 9 LYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 86 MLSREHGKTIDDAK-GDIVRGLEVCEFVIGI-PHLQKSEFTEGAGPGIdmYSIRQPVGIGAGITPFNFPGMIPMWMFAPA 163
Cdd:PRK13252 89 LETLDTGKPIQETSvVDIVTGADVLEYYAGLaPALEGEQIPLRGGSFV--YTRREPLGVCAGIGAWNYPIQIACWKSAPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 164 IACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDkGAVDAILT-HPDIAAVSFVGSTPIARYVYGTAAMNGK 242
Cdd:PRK13252 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGD-GRVGAWLTeHPDIAKVSFTGGVPTGKKVMAAAAASLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 243 RAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCM-AISVAVPvgEETANRLIDKLVPMVESLRIGPYTDEKADM 321
Cdd:PRK13252 246 EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVFVQ--KSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 322 GPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEAL 401
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 402 SLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNV----PIPVPlayhsFGGWKSSSFGDLNqhGTDSIKFWTRTKT 477
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgesPAEMP-----VGGYKQSGIGREN--GIATLEHYTQIKS 476
|
.
gi 1550356027 478 I 478
Cdd:PRK13252 477 V 477
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
24-479 |
4.16e-93 |
|
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: 290.39 E-value: 4.16e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 24 FNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIV 103
Cdd:cd07150 4 LNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 104 RGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPI 183
Cdd:cd07150 84 FTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 184 RLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADL 262
Cdd:cd07150 164 KIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 263 DQAANAligAGYGS---AGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDS 339
Cdd:cd07150 244 DYAVRA---AAFGAfmhQGQICMSAS-RIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 340 GIEQGAKLVVDgrdfklqGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRD 419
Cdd:cd07150 320 AVAKGAKLLTG-------GKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 420 GDAARDFASRINIGMVGVNVPIPVPLAYHSFGGWKSSSFGdlNQHGTDSIKFWTRTKTIT 479
Cdd:cd07150 393 LQRAFKLAERLESGMVHINDPTILDEAHVPFGGVKASGFG--REGGEWSMEEFTELKWIT 450
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
7-478 |
4.42e-90 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 283.43 E-value: 4.42e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAA--QPKWAATNPQRRARVFMKFVQLLNDNMNELA 84
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 85 EMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDmYSIRQPVGIGAGITPFNFPGMIPMWMFAPAI 164
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHVIS-RTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 165 ACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKR 243
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 244 AQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDEKADMGP 323
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLL-VEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 324 VVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSL 403
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 404 PMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNvpipvplAYH------SFGGWKSSSFG-DLNQHGTDSikfWTRTK 476
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN-------DYHpyfaeaPWGGYKQSGIGrELGPTGLEE---YQETK 468
|
..
gi 1550356027 477 TI 478
Cdd:cd07119 469 HI 470
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
5-482 |
9.57e-89 |
|
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: 279.71 E-value: 9.57e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 5 GHFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAA-QPKWAATNPQRRARVFMKFVQLLNDNMNEL 83
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 84 AEMLSREHGKTIDdakgdIVRGLEVCEFVI-------------------GIPHLQKSEFTEgagpgidmYSIRQPVGIGA 144
Cdd:cd07113 81 AQLETLCSGKSIH-----LSRAFEVGQSANflryfagwatkingetlapSIPSMQGERYTA--------FTRREPVGVVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 145 GITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGdKGAVDAILT-HPDIAAVSF 223
Cdd:cd07113 148 GIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNG-KGAVGAQLIsHPDVAKVSF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 224 VGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCmAISVAVPVGEETANRLIDKLV 303
Cdd:cd07113 227 TGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVC-AAPERFYVHRSKFDELVTKLK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 304 PMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKTE 383
Cdd:cd07113 306 QALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGY----FVQPTLVLARSADSRLMREE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 384 IFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVN----VPIPVPlayhsFGGWKSSSFG 459
Cdd:cd07113 382 TFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmhtfLDPAVP-----FGGMKQSGIG 456
|
490 500
....*....|....*....|...
gi 1550356027 460 dlNQHGTDSIKFWTRTKTITSRW 482
Cdd:cd07113 457 --REFGSAFIDDYTELKSVMIRY 477
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
57-478 |
1.09e-88 |
|
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: 279.10 E-value: 1.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 57 WAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVRGL--------EVCEFVIG-IPHlqkseftegA 127
Cdd:cd07112 42 WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAVDVPSAantfrwyaEAIDKVYGeVAP---------T 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 128 GPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGD-K 206
Cdd:cd07112 113 GPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFgH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 207 GAVDAILTHPDIAAVSFVGSTPIARYVYGTAA-MNGKRAQCFGGAKNHMIIMPDA-DLDQAANALIGAGYGSAGERCMAI 284
Cdd:cd07112 193 TAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 285 SvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRdfKLQGYENGHF 364
Cdd:cd07112 273 S-RLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLVAGGK--RVLTETGGFF 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 365 IGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVN----VP 440
Cdd:cd07112 350 VEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNcfdeGD 429
|
410 420 430
....*....|....*....|....*....|....*....
gi 1550356027 441 IPVPlayhsFGGWKSSSFG-DLNQHGTDSikfWTRTKTI 478
Cdd:cd07112 430 ITTP-----FGGFKQSGNGrDKSLHALDK---YTELKTT 460
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
23-479 |
2.66e-87 |
|
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: 275.39 E-value: 2.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPATGEVQGTVALASDADLAAAVESAKAAQPKwaaTNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDI 102
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALAASYRST---LTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 103 VRGLEVCEFVIG-IPHLQKSEF----TEGAGPGIdMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSER 177
Cdd:cd07146 80 GRAADVLRFAAAeALRDDGESFscdlTANGKARK-IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 178 DPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVygtAAMNGKRAQCFG-GAKNHMI 255
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIgDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLElGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 256 IMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRS 335
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVK-RILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 336 LIDSGIEQGAKLVVDGRdfklqgyENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAI 415
Cdd:cd07146 315 RVEEAIAQGARVLLGNQ-------RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550356027 416 YTRDGDAARDFASRINIGMVGVN-VP------IPvplayhsFGGWKSSSFGdLNQHGTDSIKFWTRTKTIT 479
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTVNVNeVPgfrselSP-------FGGVKDSGLG-GKEGVREAMKEMTNVKTYS 450
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
23-481 |
7.77e-87 |
|
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: 274.25 E-value: 7.77e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDI 102
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 103 VRGLEVCEFVIGIPHLQKSEfTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVP 182
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGE-TIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 183 IRLAELMIEAgLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDAD 261
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 262 LDQAANALI-GAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSG 340
Cdd:cd07107 239 PEAAADAAVaGMNFTWCGQSCGSTSRLF-VHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 341 IEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDG 420
Cdd:cd07107 318 KREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550356027 421 DAARDFASRINIGMVGVN--------VPipvplayhsFGGWKSSSFGdlNQHGTDSIKFWTRTKTITSR 481
Cdd:cd07107 398 SQAHRTARRVEAGYVWINgssrhflgAP---------FGGVKNSGIG--REECLEELLSYTQEKNVNVR 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
10-479 |
8.14e-87 |
|
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: 274.57 E-value: 8.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 10 GKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSR 89
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 90 EHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNA 169
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 170 FILKPSERDPSVP-IRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCF 247
Cdd:cd07151 161 VVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIgDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 248 GGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAIS---VAVPVGEETANRLIDKlvpmVESLRIGPYTDEKADMGPV 324
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINriiVHEDVYDEFVEKFVER----VKALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 325 VTKEAEQRIRSLIDSGIEQGAKLVVDGRdfklqgyENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLP 404
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGGE-------AEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELA 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550356027 405 MKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNvPIPV---PLAyhSFGGWKSSSFGDLNqhGTDSIKFWTRTKTIT 479
Cdd:cd07151 390 NDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVndePHV--PFGGEKNSGLGRFN--GEWALEEFTTDKWIS 462
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
6-456 |
4.59e-86 |
|
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: 272.45 E-value: 4.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 6 HFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAE 85
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 86 MLSREHGKTIDDAKGDIVrGLEVCEFVIGIPHLQKSEFTEGAGPGIdmySIRQPVGIGAGITPFNFPGMIPMWMFAPAIA 165
Cdd:cd07138 81 AITLEMGAPITLARAAQV-GLGIGHLRAAADALKDFEFEERRGNSL---VVREPIGVCGLITPWNWPLNQIVLKVAPALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 166 CGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDkGAV--DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKR 243
Cdd:cd07138 157 AGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGD-GPVvgEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 244 -AQCFGGaKNHMIIMPDADLDQAANALIGAGYGSAGERCMAIS-VAVPvgEETANRLIDKLVPMVESLRIGPYTDEKADM 321
Cdd:cd07138 236 vALELGG-KSANIILDDADLEKAVPRGVAACFANSGQSCNAPTrMLVP--RSRYAEAEEIAAAAAEAYVVGDPRDPATTL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 322 GPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDfKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEAL 401
Cdd:cd07138 313 GPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAI 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1550356027 402 SLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAyhSFGGWKSS 456
Cdd:cd07138 392 AIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGA--PFGGYKQS 444
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
7-482 |
9.05e-86 |
|
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: 273.33 E-value: 9.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVaGTSGRVSNIfNPA-TGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAE 85
Cdd:cd07124 36 VIGGKEV-RTEEKIESR-NPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 86 MLSREHGKTIDDAKGDIVRGLEVCEFVIGipHLQK-SEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAI 164
Cdd:cd07124 114 WMVLEVGKNWAEADADVAEAIDFLEYYAR--EMLRlRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 165 ACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAM---- 239
Cdd:cd07124 192 VTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERAAKvqpg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 240 --NGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDE 317
Cdd:cd07124 272 qkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVI-VHESVYDEFLERLVERTKALKVGDPEDP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 318 KADMGPVVTKEAEQRIRSLIDSGIEQGaKLVVDGRdfKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNY 397
Cdd:cd07124 351 EVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGE--VLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 398 EEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPL-AYHSFGGWKSSSFGDLNQhGTDSIKFWTRTK 476
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALvGRQPFGGFKMSGTGSKAG-GPDYLLQFMQPK 506
|
....*.
gi 1550356027 477 TITSRW 482
Cdd:cd07124 507 TVTENF 512
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
23-459 |
9.33e-85 |
|
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: 268.83 E-value: 9.33e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDI 102
Cdd:cd07145 3 VRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 103 VRGLEVCEFVIgiphlQKSEFTEGAGPGIDMY---------SIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILK 173
Cdd:cd07145 83 ERTIRLFKLAA-----EEAKVLRGETIPVDAYeynerriafTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 174 PSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKN 252
Cdd:cd07145 158 PSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 253 HMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQR 332
Cdd:cd07145 238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVK-RILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 333 IRSLIDSGIEQGAKLVVDGRDfklqgyENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNG 412
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQ 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1550356027 413 VAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGGWKSSSFG 459
Cdd:cd07145 391 ASVFTNDINRALKVARELEAGGVVINDSTRFRWDNLPFGGFKKSGIG 437
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
23-474 |
1.31e-84 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 268.45 E-value: 1.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDI 102
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 103 VRGLEVCEFVIGI---PHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDP 179
Cdd:cd07110 81 DDVAGCFEYYADLaeqLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 180 SVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-HPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMP 258
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAaHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 259 DADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLID 338
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATS-RLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 339 SGIEQGAKLVVDGRdfKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTR 418
Cdd:cd07110 320 RGKEEGARLLCGGR--RPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 419 DGDAARDFASRINIGMVGVNVPIPVpLAYHSFGGWKSSSFG-DLNQHGTD---SIKFWTR 474
Cdd:cd07110 398 DAERCDRVAEALEAGIVWINCSQPC-FPQAPWGGYKRSGIGrELGEWGLDnylEVKQITR 456
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
5-479 |
2.31e-84 |
|
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: 268.31 E-value: 2.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 5 GHFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDA--DLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNE 82
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEdvDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 83 LAEMLSREHGKTIDD-AKGDIVRGLEVCEFVIG---------IPhLQKSEFTegagpgidmYSIRQPVGIGAGITPFNFP 152
Cdd:cd07091 85 LAALESLDNGKPLEEsAKGDVALSIKCLRYYAGwadkiqgktIP-IDGNFLA---------YTRREPIGVCGQIIPWNFP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 153 GMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGdKGAV--DAILTHPDIAAVSFVGSTPIA 230
Cdd:cd07091 155 LLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPG-FGPTagAAISSHMDVDKIAFTGSTAVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 231 RYVYGTAA-MNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESL 309
Cdd:cd07091 234 RTIMEAAAkSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGS-RIFVQESIYDEFVEKFKARAEKR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 310 RIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKTEIFGPVL 389
Cdd:cd07091 313 VVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGY----FIQPTVFTDVKDDMKIAKEEIFGPVV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 390 SVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVN------VPIPvplayhsFGGWKSSSFG-DLn 462
Cdd:cd07091 389 TILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNtynvfdAAVP-------FGGFKQSGFGrEL- 460
|
490
....*....|....*..
gi 1550356027 463 qhGTDSIKFWTRTKTIT 479
Cdd:cd07091 461 --GEEGLEEYTQVKAVT 475
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
4-478 |
2.91e-84 |
|
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: 268.51 E-value: 2.91e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 4 LGHFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAA-QPKWAATNPQRRARVFMKFVQLLNDNMNE 82
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 83 LAEMLSREHGKTID-DAKGDIVRGLEVCEFVIGIPHLQKSEfTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFA 161
Cdd:cd07144 88 LAAIEALDSGKPYHsNALGDLDEIIAVIRYYAGWADKIQGK-TIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 162 PAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGdKGAV--DAILTHPDIAAVSFVGSTPIARYVYGTAAM 239
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPG-YGAVagSALAEHPDVDKIAFTGSTATGRLVMKAAAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 240 NGKRAQCFGGAKNHMIIMPDADLDQAAN-ALIGAGYGSaGERCMAISvAVPVGEETANRLIDKLVPMV-ESLRIGPYTDE 317
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVKwAAAGIMYNS-GQNCTATS-RIYVQESIYDKFVEKFVEHVkQNYKVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 318 KADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGrDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNY 397
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGG-EKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 398 EEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVP----IPVPlayhsFGGWKSSSFG-DLNQHGTDSikfW 472
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMSGIGrELGEYGLET---Y 474
|
....*.
gi 1550356027 473 TRTKTI 478
Cdd:cd07144 475 TQTKAV 480
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
25-479 |
4.82e-84 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 266.99 E-value: 4.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 25 NPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVR 104
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 105 glevcefVIGIPHLQKSEFTEGAGPGIDM-----------YSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILK 173
Cdd:cd07094 85 -------AIDTLRLAAEEAERIRGEEIPLdatqgsdnrlaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 174 PSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVygTAAMNGKRAQCFGGAKN 252
Cdd:cd07094 158 PASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLgDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 253 HMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQR 332
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIY-VHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 333 IRSLIDSGIEQGAKLVvdgrdfkLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNG 412
Cdd:cd07094 315 VERWVEEAVEAGARLL-------CGGERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQ 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550356027 413 VAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGGWKSSSFgdlnqhGTDSIKF----WTRTKTIT 479
Cdd:cd07094 388 AGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKESGV------GREGVPYameeMTEEKTVV 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
7-478 |
9.95e-84 |
|
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: 266.74 E-value: 9.95e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVaGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNP-QRRARVFMKFVQLLNDNMNELAE 85
Cdd:cd07082 5 LINGEWK-ESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 86 MLSREHGKTIDDAKGDIVRGLEVCEFVIG-----IPHLQKSEFTEGAGPGIDMYSiRQPVGIGAGITPFNFPGMIPMWMF 160
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRDTIEelkrlDGDSLPGDWFPGTKGKIAQVR-REPLGVVLAIGPFNYPLNLTVSKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 161 APAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGdKGAV--DAILTHPDIAAVSFVGSTPIARYVYGTAA 238
Cdd:cd07082 163 IPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTG-RGREigDPLVTHGRIDVISFTGSTEVGNRLKKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 239 MngKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVaVPVGEETANRLIDKLVPMVESLRIGPYTDEK 318
Cdd:cd07082 242 M--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-VLVHESVADELVELLKEEVAKLKVGMPWDNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 319 ADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGrdfklqGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYE 398
Cdd:cd07082 319 VDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 399 EALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNvpipvplAYHS-------FGGWKSSSFGDLNQHgtDSIKF 471
Cdd:cd07082 393 EAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN-------SKCQrgpdhfpFLGRKDSGIGTQGIG--DALRS 463
|
....*..
gi 1550356027 472 WTRTKTI 478
Cdd:cd07082 464 MTRRKGI 470
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
23-479 |
1.93e-82 |
|
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: 262.94 E-value: 1.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPATGEVQGTVALASDADLAAAVESAKAAQPKWA-ATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGD 101
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 102 IV---RGLE----VCEFVIG--IPhlqkseftegAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFIL 172
Cdd:cd07109 81 VEaaaRYFEyyggAADKLHGetIP----------LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 173 KPSERDPSVPIRLAELMIEAGLPAGILNVVNG---DKGAvdAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGG 249
Cdd:cd07109 151 KPAEDAPLTALRLAELAEEAGLPAGALNVVTGlgaEAGA--ALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 250 AKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPyTDEKADMGPVVTKEA 329
Cdd:cd07109 229 GKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGS-RLLVHRSIYDEVLERLVERFRALRVGP-GLEDPDLGPLISAKQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 330 EQRIRSLIDSGIEQGAKLVVDGRdfKLQG-YENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHE 408
Cdd:cd07109 307 LDRVEGFVARARARGARIVAGGR--IAEGaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTD 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550356027 409 YGNGVAIYTRDGDAARDFASRINIGMVGVN-------VPIPvplayhsFGGWKSSSFGdlNQHGTDSIKFWTRTKTIT 479
Cdd:cd07109 385 YGLVAGVWTRDGDRALRVARRLRAGQVFVNnygagggIELP-------FGGVKKSGHG--REKGLEALYNYTQTKTVA 453
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
23-479 |
5.30e-81 |
|
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: 259.22 E-value: 5.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTI-DDAKGD 101
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 102 IVRGLEVCEFVIGIPHLQKSEfTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSV 181
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGE-TLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 182 PIRLAELMIEAgLPAGILNVVNGdKGAV--DAILTHPDIAAVSFVGSTPIARYVYGTAAmnGKRAQC---FGGaKNHMII 256
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITG-YGEEcgAALVDHPDVDKVTFTGSTEVGKIIYRAAA--DRLIPVsleLGG-KSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 257 MPDADLDQAANALI-GAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRS 335
Cdd:cd07108 235 FPDADLDDAVDGAIaGMRFTRQGQSCTAGS-RLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 336 LIDSGIE-QGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVA 414
Cdd:cd07108 314 YIDLGLStSGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAY 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550356027 415 IYTRDGDAARDFASRINIGMVGVNVPIpVPLAYHSFGGWKSSSFGdlNQHGTDS-IKFWTRTKTIT 479
Cdd:cd07108 394 VWTRDLGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLG--REASLEGmLEHFTQKKTVN 456
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
23-478 |
2.28e-80 |
|
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: 257.07 E-value: 2.28e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDI 102
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 103 VRGLEVCEFVIGIP----HLQKSEftegagpgiDMYSI--RQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSE 176
Cdd:cd07106 81 GGAVAWLRYTASLDlpdeVIEDDD---------TRRVElrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 177 RDPSVPIRLAELMIEAgLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMII 256
Cdd:cd07106 152 FTPLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 257 MPDADLDQAANALIGAGYGSAGERCMAIS-VAVPvgEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRS 335
Cdd:cd07106 231 LPDVDIDAVAPKLFWGAFINSGQVCAAIKrLYVH--ESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 336 LIDSGIEQGAKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAI 415
Cdd:cd07106 309 LVEDAKAKGAKVLAGGEPLDGPGY----FIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASV 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550356027 416 YTRDGDAARDFASRINIGMVGVN----VPIPVPlayhsFGGWKSSSFGdlNQHGTDSIKFWTRTKTI 478
Cdd:cd07106 385 WSSDLERAEAVARRLEAGTVWINthgaLDPDAP-----FGGHKQSGIG--VEFGIEGLKEYTQTQVI 444
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
7-479 |
4.22e-80 |
|
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: 257.12 E-value: 4.22e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVES--AKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELA 84
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAarRAFDNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 85 EMLSREHGKTIDDAK-GDIVRGLEVCEFVIGI-PHLQKSEFTEGAGPGiDMYSIRQPVGIGAGITPFNFPGMIPMWMFAP 162
Cdd:cd07139 82 RLWTAENGMPISWSRrAQGPGPAALLRYYAALaRDFPFEERRPGSGGG-HVLVRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 163 AIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGK 242
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 243 RAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAIS-VAVPvgeetANR---LIDKLVPMVESLRIGPYTDEK 318
Cdd:cd07139 241 RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTrILVP-----RSRydeVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 319 ADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKlqGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYE 398
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPA--GLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 399 EALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAyhSFGGWKSSSFGdlNQHGTDSIKFWTRTKTI 478
Cdd:cd07139 394 DAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFGA--PFGGFKQSGIG--REGGPEGLDAYLETKSI 469
|
.
gi 1550356027 479 T 479
Cdd:cd07139 470 Y 470
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
25-478 |
1.24e-78 |
|
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: 252.93 E-value: 1.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 25 NPATGEVQGTVALASDADLAAAVESAKAAQPKWA-ATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTI-------D 96
Cdd:cd07089 3 NPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVmtaramqV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 97 DAKGDIVRG-LEVCEFvigipHLQKSEFTEGAGPGIDMYSI--RQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILK 173
Cdd:cd07089 83 DGPIGHLRYfADLADS-----FPWEFDLPVPALRGGPGRRVvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 174 PSERDPSVPIRLAELMIEAGLPAGILNVVNG-DKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKN 252
Cdd:cd07089 158 PAPDTPLSALLLGEIIAETDLPAGVVNVVTGsDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 253 HMIIMPDADLDQAANALIGAGYGSAGERCmAISVAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQR 332
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGC-ALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 333 IRSLIDSGIEQGAKLVVDGRdfKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNG 412
Cdd:cd07089 317 VEGYIARGRDEGARLVTGGG--RPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550356027 413 VAIYTRDGDAARDFASRINIGMVGVNvPIPVPLAYHSFGGWKSSSFGdlNQHGTDSIKFWTRTKTI 478
Cdd:cd07089 395 GGVWSADVDRAYRVARRIRTGSVGIN-GGGGYGPDAPFGGYKQSGLG--RENGIEGLEEFLETKSI 457
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
23-459 |
1.39e-78 |
|
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: 252.52 E-value: 1.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDI 102
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 103 VRGLEVCEFvigiphlQKSEFTEGAGPGIDM-----------YSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFI 171
Cdd:cd07149 83 DRAIETLRL-------SAEEAKRLAGETIPFdaspggegrigFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 172 LKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAMngKRAQCFGGA 250
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKAGL--KKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 251 KNHMIIMPDADLDQAANALIGAGYGSAGERCmaISVA-VPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEA 329
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVC--ISVQrIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 330 EQRIRSLIDSGIEQGAKLVvdgrdfkLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEY 409
Cdd:cd07149 312 AERIEEWVEEAVEGGARLL-------TGGKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPY 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1550356027 410 GNGVAIYTRDGDAARDFASRINIGMVGVNvPIPVPLAYH-SFGGWKSSSFG 459
Cdd:cd07149 385 GLQAGVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHmPYGGVKESGTG 434
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
57-479 |
3.67e-78 |
|
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: 251.49 E-value: 3.67e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 57 WAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSI 136
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 137 RQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTH 215
Cdd:cd07118 117 REPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVgQAMTEH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 216 PDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETA 295
Cdd:cd07118 197 PDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLL-VHESIA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 296 NRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGrdfKLQGYENGHFIGGCLFDDVTP 375
Cdd:cd07118 276 DAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGG---ERLASAAGLFYQPTIFTDVTP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 376 DMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPI----PVPlayhsFG 451
Cdd:cd07118 353 DMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLdgspELP-----FG 427
|
410 420
....*....|....*....|....*....
gi 1550356027 452 GWKSSSFG-DLNQHGTDSikfWTRTKTIT 479
Cdd:cd07118 428 GFKQSGIGrELGRYGVEE---YTELKTVH 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
55-479 |
4.21e-78 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 250.96 E-value: 4.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 55 PKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMY 134
Cdd:cd07105 14 PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIPSDKPGTLAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 135 SIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDK----GAVD 210
Cdd:cd07105 94 VVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSPedapEVVE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 211 AILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPV 290
Cdd:cd07105 174 ALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTE-RIIV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 291 GEETANRLIDKLVPMVESLRIGPytdekADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDfklQGYENGHFIGGCLF 370
Cdd:cd07105 253 HESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLA---DESPSGTSMPPTIL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 371 DDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVP-------IPv 443
Cdd:cd07105 325 DNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMtvhdeptLP- 403
|
410 420 430
....*....|....*....|....*....|....*.
gi 1550356027 444 playhsFGGWKSSSFGDLNqhGTDSIKFWTRTKTIT 479
Cdd:cd07105 404 ------HGGVKSSGYGRFN--GKWGIDEFTETKWIT 431
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-459 |
9.77e-78 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 251.92 E-value: 9.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEM 86
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 87 LSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFP-GMIPMwMFAPAIA 165
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITR-KVGPALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 166 CGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRA 244
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 245 QCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPV 324
Cdd:PLN02278 267 SLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCAN-RILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 325 VTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLqgyeNGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLP 404
Cdd:PLN02278 346 INEAAVQKVESHVQDAVSKGAKVLLGGKRHSL----GGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIA 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1550356027 405 MKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIpVPLAYHSFGGWKSSSFG 459
Cdd:PLN02278 422 NDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLG 475
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
54-460 |
1.59e-77 |
|
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: 249.52 E-value: 1.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 54 QPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEgAGPGIDM 133
Cdd:cd07152 26 QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQGEILP-SAPGRLS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 134 YSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDP-SVPIRLAELMIEAGLPAGILNVVNGDKGAVDAI 212
Cdd:cd07152 105 LARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvSGGVVIARLFEEAGLPAGVLHVLPGGADAGEAL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 213 LTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAiSVAVPVGE 292
Cdd:cd07152 185 VEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMA-AGRHLVHE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 293 ETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRdfklqgYEnGHFIGGCLFDD 372
Cdd:cd07152 264 SVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGT------YD-GLFYRPTVLSG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 373 VTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGG 452
Cdd:cd07152 337 VKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDEPHNPFGG 416
|
....*...
gi 1550356027 453 WKSSSFGD 460
Cdd:cd07152 417 MGASGNGS 424
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
23-480 |
6.92e-76 |
|
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: 245.70 E-value: 6.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGD- 101
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 102 IVRGLEVCEFVIG-IPHLQKSEFTEGAgPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPS 180
Cdd:cd07092 81 LPGAVDNFRFFAGaARTLEGPAAGEYL-PGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 181 VPIRLAELMIEaGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPD 259
Cdd:cd07092 160 TTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 260 ADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDs 339
Cdd:cd07092 239 ADLDAAVAGIATAGYYNAGQDCTAAC-RVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 340 GIEQGAKLVVDGRdfklQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRD 419
Cdd:cd07092 317 RAPAHARVLTGGR----RAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550356027 420 GDAARDFASRINIGMVGVNVPIPVPlAYHSFGGWKSSSFG-DLNQHGTDSikfWTRTKTITS 480
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLA-AEMPHGGFKQSGYGkDLSIYALED---YTRIKHVMV 450
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
7-465 |
8.50e-76 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 245.97 E-value: 8.50e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGtSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEM 86
Cdd:PRK13473 6 LINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 87 LSREHGKTIDDAKGDIVRG-LEVCEFVIGIP-HLQKS---EFTEGAGPGIDmysiRQPVGIGAGITPFNFPGMIPMWMFA 161
Cdd:PRK13473 85 ESLNCGKPLHLALNDEIPAiVDVFRFFAGAArCLEGKaagEYLEGHTSMIR----RDPVGVVASIAPWNYPLMMAAWKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 162 PAIACGNAFILKPSERDPSVPIRLAELMIEAgLPAGILNVVNGdKGAV--DAILTHPDIAAVSFVGSTPIARYVYGTAAM 239
Cdd:PRK13473 161 PALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTG-RGATvgDALVGHPKVRMVSLTGSIATGKHVLSAAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 240 NGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDEKA 319
Cdd:PRK13473 239 SVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIY-AQRGIYDDLVAKLAAAVATLKVGDPDDEDT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 320 DMGPVVTKEAEQRIRSLIDSGIEQG-AKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYE 398
Cdd:PRK13473 318 ELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGY----YYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550356027 399 EALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPV----PlayHsfGGWKSSSFG-DLNQHG 465
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLvsemP---H--GGQKQSGYGkDMSLYG 460
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
25-479 |
3.04e-75 |
|
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: 244.05 E-value: 3.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 25 NPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVR 104
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 105 GLEVCEFVigIPHLQKSEFTEGAGPGIDMYSIR-----QPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDP 179
Cdd:cd07099 82 ALEAIDWA--ARNAPRVLAPRKVPTGLLMPNKKatveyRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 180 SVPIRLAELMIEAGLPAGILNVVNGDkGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPD 259
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGD-GATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 260 ADLDQAANALIGAGYGSAGERCMAISVaVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDS 339
Cdd:cd07099 239 ADLERAAAAAVWGAMVNAGQTCISVER-VYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 340 GIEQGAKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRD 419
Cdd:cd07099 318 AVAKGAKALTGGARSNGGGP----FYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550356027 420 GDAARDFASRINIGMVGVN-----VPIP-VPlayhsFGGWKSSSFGdlNQHGTDSIKFWTRTKTIT 479
Cdd:cd07099 394 LARAEAIARRLEAGAVSINdvlltAGIPaLP-----FGGVKDSGGG--RRHGAEGLREFCRPKAIA 452
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
4-465 |
1.99e-73 |
|
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: 239.99 E-value: 1.99e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 4 LGHFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNEL 83
Cdd:cd07111 22 FGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 84 AEMLSREHGKTIDDAKGdivrglevCEFVIGIPHLQK----SEFTEGAGPGidmysiRQPVGIGAGITPFNFPGMIPMWM 159
Cdd:cd07111 102 AVLESLDNGKPIRESRD--------CDIPLVARHFYHhagwAQLLDTELAG------WKPVGVVGQIVPWNFPLLMLAWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 160 FAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAM 239
Cdd:cd07111 168 ICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 240 NGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDEKA 319
Cdd:cd07111 248 TGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLL-VQESVAEELIRKLKERMSHLRVGDPLDKAI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 320 DMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKlqgyENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEE 399
Cdd:cd07111 327 DMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLP----SKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKE 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550356027 400 ALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVN--------VPipvplayhsFGGWKSSSFG-DLNQHG 465
Cdd:cd07111 403 AVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINghnlfdaaAG---------FGGYRESGFGrEGGKEG 468
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
54-478 |
7.16e-73 |
|
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: 236.97 E-value: 7.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 54 QPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVRGLEVCEF-VIGIPHLQKSEFTEGAGPgiD 132
Cdd:cd07100 12 FLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyAENAEAFLADEPIETDAG--K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 133 MYSIRQPVGIGAGITPFNFPgmipMW----MFAPAIACGNAFILKPSerdPSVP---IRLAELMIEAGLPAGILNVVNGD 205
Cdd:cd07100 90 AYVRYEPLGVVLGIMPWNFP----FWqvfrFAAPNLMAGNTVLLKHA---SNVPgcaLAIEELFREAGFPEGVFQNLLID 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 206 KGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQC-FGGAkNHMIIMPDADLDQAANALIGAGYGSAGERCMA- 283
Cdd:cd07100 163 SDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLeLGGS-DPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAa 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 284 ---IsvavpVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYe 360
Cdd:cd07100 242 krfI-----VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGA- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 361 nghFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVP 440
Cdd:cd07100 316 ---FYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGM 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1550356027 441 ------IPvplayhsFGGWKSSSFG-DLNQHGtdsIKFWTRTKTI 478
Cdd:cd07100 393 vksdprLP-------FGGVKRSGYGrELGRFG---IREFVNIKTV 427
|
|
| lactal_redase_Meth |
NF040648 |
lactaldehyde dehydrogenase; |
7-478 |
2.45e-72 |
|
lactaldehyde dehydrogenase;
Pssm-ID: 468615 [Multi-domain] Cd Length: 463 Bit Score: 236.81 E-value: 2.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGTSgrvSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEM 86
Cdd:NF040648 2 FINGKWIDRED---IDVINPYNLEVIDKIPSLSREEVKEAIEIANEAKEVMKNLSPRKRYNILMDIAEELKKNKEELAKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 87 LSREHGKTIDDAKGDIVRGLEVCEfvigiphLQKSEFTEGAGPGIDM-----YSIRQPVGIGAGITPFNFPGMIPMWMFA 161
Cdd:NF040648 79 ITIDAGKPIKQSIIEVDRSIETFK-------LAAFYAKEIRGETIPSdagliFTKKEPLGVVGAITPFNYPLNLAAHKIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 162 PAIACGNAFILKPSERDPSVPIRLAELMIEA----GLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGT 236
Cdd:NF040648 152 PAIATGNSVVLHPSSKAPLAAIELAKIIEKVlkkmNIPLGVFNLVTGYGEVVgDEIVKNEKVNKISFTGSVEVGESISKK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 237 AAMngKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTD 316
Cdd:NF040648 232 AGM--KKITLELGGNNPLIVLKDADIEKAVESAVKGSFLNSGQVCISVG-RVIVEEEIADEFIKKLVEETKKLKVGNPLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 317 EKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDG-RDfklqgyenghfigGCLFD----DVTPDMDIYKTEIFGPVLSV 391
Cdd:NF040648 309 EKTDIGPLITEEAAIRVENLVNEAIEEGAKLLCGGnRE-------------GSLFYptvlDVDEDNILVKVETFGPVLPI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 392 VRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVP-------IPvplayhsFGGWKSSSFgdlnqh 464
Cdd:NF040648 376 IRVKDIDEAIEIANNTKYGLQAGVFTNDINKALKFADELEYGGVIINKSstfrtdnMP-------FGGFKKSGL------ 442
|
490
....*....|....*...
gi 1550356027 465 GTDSIKF----WTRTKTI 478
Cdd:NF040648 443 GKEGIKYaveeMTEIKTI 460
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
3-482 |
8.99e-72 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 236.76 E-value: 8.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 3 ELGH----FIDGKRVAgTSGRVSNIfNPA-TGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLN 77
Cdd:PRK03137 32 ELGQdyplIIGGERIT-TEDKIVSI-NPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 78 DNMNELAEMLSREHGKTIDDAKGDIVRGLEVCEFVIgiphLQKSEFTEGAG----PGIDMYSIRQPVGIGAGITPFNFPG 153
Cdd:PRK03137 110 RRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYA----RQMLKLADGKPvesrPGEHNRYFYIPLGVGVVISPWNFPF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 154 MIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARY 232
Cdd:PRK03137 186 AIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFITFTGSREVGLR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 233 VYGTAA--MNG----KRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMV 306
Cdd:PRK03137 266 IYERAAkvQPGqiwlKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAI-VHEDVYDEVLEKVVELT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 307 ESLRIGPyTDEKADMGPVVTKEAEQRIRSLIDSGIEQGaKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKTEIFG 386
Cdd:PRK03137 345 KELTVGN-PEDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGY----FIQPTIFADVDPKARIMQEEIFG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 387 PVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGD----AARDFAS---RINIGMVGVNVpipvplAYHSFGGWKSSsfg 459
Cdd:PRK03137 419 PVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREhlekARREFHVgnlYFNRGCTGAIV------GYHPFGGFNMS--- 489
|
490 500 510
....*....|....*....|....*....|
gi 1550356027 460 dlnqhGTDS-------IKFWTRTKTITSRW 482
Cdd:PRK03137 490 -----GTDSkaggpdyLLLFLQAKTVSEMF 514
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
24-479 |
2.48e-71 |
|
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: 233.77 E-value: 2.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 24 FNPATGEVQGTVALASDADLAAAVESAKA--AQPKWAaTNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGD 101
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRafDETDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 102 IVRGLEVCEFVIGiphLQKSEFTEGAGPGIDMYSI--RQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDP 179
Cdd:cd07120 81 ISGAISELRYYAG---LARTEAGRMIEPEPGSFSLvlREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 180 SVPIRLAELMIEA-GLPAGILNVVNGDKGAVDAIL-THPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIM 257
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLvASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 258 PDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLI 337
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGS-RVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 338 DSGIEQGAKLVVDGRDFKlQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYT 417
Cdd:cd07120 317 ERAIAAGAEVVLRGGPVT-EGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550356027 418 RDGDAARDFASRINIGMVGVNVPIPVpLAYHSFGGWKSSSFGDLnqHGTDSIKFWTRTKTIT 479
Cdd:cd07120 396 RDLARAMRVARAIRAGTVWINDWNKL-FAEAEEGGYRQSGLGRL--HGVAALEDFIEYKHIY 454
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
5-459 |
1.00e-70 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 233.00 E-value: 1.00e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 5 GHFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELA 84
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 85 EMLSREHGKTIDDAKG-DIVRGLEVCEFVIGIPHLQkseftEGAGPGID----MYSIRQPVGIGAGITPFNFPGMIPMWM 159
Cdd:cd07559 82 VAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQ-----EGSLSEIDedtlSYHFHEPLGVVGQIIPWNFPLLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 160 FAPAIACGNAFILKPSERDPSVPIRLAELmIEAGLPAGILNVVNGdKGAV--DAILTHPDIAAVSFVGSTPIARYVYGTA 237
Cdd:cd07559 157 LAPALAAGNTVVLKPASQTPLSILVLMEL-IGDLLPKGVVNVVTG-FGSEagKPLASHPRIAKLAFTGSTTVGRLIMQYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 238 AMNGKRAQCFGGAKNHMIIMPDADLDQAA--NALIGAGYGSA---GERCMAISVAVpVGEETANRLIDKLVPMVESLRIG 312
Cdd:cd07559 235 AENLIPVTLELGGKSPNIFFDDAMDADDDfdDKAEEGQLGFAfnqGEVCTCPSRAL-VQESIYDEFIERAVERFEAIKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 313 PYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVV 392
Cdd:cd07559 314 NPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVI 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550356027 393 RARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPlAYHSFGGWKSSSFG 459
Cdd:cd07559 394 TFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYP-AHAPFGGYKKSGIG 459
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
2-459 |
1.19e-70 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 233.63 E-value: 1.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 2 YELGHFIDGKRVAGTSGRVsnIFNPATGEVQ-GTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNM 80
Cdd:cd07125 31 WEAIPIINGEETETGEGAP--VIDPADHERTiGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 81 NELAEMLSREHGKTIDDAKGDIVRGLEVCEFVigiPHLQKSEFTEGAGPGIDMYS---IRQPVGIGAGITPFNFPGMIPM 157
Cdd:cd07125 109 GELIALAAAEAGKTLADADAEVREAIDFCRYY---AAQARELFSDPELPGPTGELnglELHGRGVFVCISPWNFPLAIFT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 158 WMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARyvygt 236
Cdd:cd07125 186 GQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAK----- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 237 aAMNGKRAQCFG---------GAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVE 307
Cdd:cd07125 261 -LINRALAERDGpilpliaetGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLY-LQEEIAERFIEMLKGAMA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 308 SLRIGPYTDEKADMGPVVTKEAEQRIRSLIDsgIEQGAKLVVdgrdFKLQ-GYENGHFIGGCLFDDVTPdmDIYKTEIFG 386
Cdd:cd07125 339 SLKVGDPWDLSTDVGPLIDKPAGKLLRAHTE--LMRGEAWLI----APAPlDDGNGYFVAPGIIEIVGI--FDLTTEVFG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 387 PVLSVVRARNY--EEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPI--------PvplayhsFGGWKSS 456
Cdd:cd07125 411 PILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNItgaivgrqP-------FGGWGLS 483
|
...
gi 1550356027 457 SFG 459
Cdd:cd07125 484 GTG 486
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
4-478 |
3.28e-70 |
|
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: 231.65 E-value: 3.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 4 LGHFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAA-QPKWAAT-NPQRRARVFMKFVQLLNDNMN 81
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 82 ELAEMLSREHGKTIDDAKG-DIVRGLEVCEFVIGIPHLQKSEFTEgAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMF 160
Cdd:cd07143 87 YLASIEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVIE-TDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 161 APAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAM 239
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 240 -NGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEK 318
Cdd:cd07143 246 sNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGS-RIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 319 ADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGrdfKLQGYEnGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYE 398
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGG---KRHGNE-GYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 399 EALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVN----VPIPVPlayhsFGGWKSSSFGdlNQHGTDSIKFWTR 474
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcynlLHHQVP-----FGGYKQSGIG--RELGEYALENYTQ 473
|
....
gi 1550356027 475 TKTI 478
Cdd:cd07143 474 IKAV 477
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
25-478 |
4.52e-69 |
|
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: 227.90 E-value: 4.52e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 25 NPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVR 104
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 105 GLEVCEFVIGI--------PHLQKSEFTEgagpgidmYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSE 176
Cdd:cd07102 82 MLERARYMISIaeealadiRVPEKDGFER--------YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 177 RDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMII 256
Cdd:cd07102 154 QTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 257 MPDADLDQAANALI-GAGYGSaGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRS 335
Cdd:cd07102 234 RPDADLDAAAESLVdGAFFNS-GQSCCSIE-RIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 336 LIDSGIEQGAKLVVDGRDFKlQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAI 415
Cdd:cd07102 312 QIADAIAKGARALIDGALFP-EDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550356027 416 YTRDGDAARDFASRINIGMVGVNvPIPVPLAYHSFGGWKSSSFG-DLNQHGTDSIkfwTRTKTI 478
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMN-RCDYLDPALAWTGVKDSGRGvTLSRLGYDQL---TRPKSY 450
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
7-479 |
1.86e-68 |
|
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: 227.23 E-value: 1.86e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDA---DLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNEL 83
Cdd:cd07141 10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKAdvdKAVKAARAAFKLGSPWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 84 AEMLSREHGKTIDDAK-GDIVRGLEVCEFVIG---------IPhLQKSEFTegagpgidmYSIRQPVGIGAGITPFNFPG 153
Cdd:cd07141 90 ASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGwadkihgktIP-MDGDFFT---------YTRHEPVGVCGQIIPWNFPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 154 MIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNG-DKGAVDAILTHPDIAAVSFVGSTPIARY 232
Cdd:cd07141 160 LMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 233 VYGTAA-MNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRI 311
Cdd:cd07141 240 IQQAAGkSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGS-RTFVQESIYDEFVKRSVERAKKRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 312 GPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKTEIFGPVLSV 391
Cdd:cd07141 319 GNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 392 VRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPlAYHSFGGWKSSSFGdlNQHGTDSIKF 471
Cdd:cd07141 395 FKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNG--RELGEYGLQE 471
|
....*...
gi 1550356027 472 WTRTKTIT 479
Cdd:cd07141 472 YTEVKTVT 479
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
12-482 |
2.06e-68 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 228.22 E-value: 2.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 12 RVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREH 91
Cdd:PRK09407 25 RVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 92 GKTIDDAKgdivrgLEVCEFVIG-------IPHLQKSEFTEGAGPGI-DMYSIRQPVGIGAGITPFNFPGMIPMWMFAPA 163
Cdd:PRK09407 105 GKARRHAF------EEVLDVALTaryyarrAPKLLAPRRRAGALPVLtKTTELRQPKGVVGVISPWNYPLTLAVSDAIPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 164 IACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDkGAV--DAILTHPDIaaVSFVGSTPIARYVYGTAamnG 241
Cdd:PRK09407 179 LLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGP-GPVvgTALVDNADY--LMFTGSTATGRVLAEQA---G 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 242 KRAQCFG---GAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEK 318
Cdd:PRK09407 253 RRLIGFSlelGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIE-RIYVHESIYDEFVRAFVAAVRAMRLGAGYDYS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 319 ADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGR---DFklqgyenghfigGCLF------DDVTPDMDIYKTEIFGPVL 389
Cdd:PRK09407 332 ADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKarpDL------------GPLFyeptvlTGVTPDMELAREETFGPVV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 390 SVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVplAYHSF----GGWKSSSFGdlNQHG 465
Cdd:PRK09407 400 SVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAA--AWGSVdapmGGMKDSGLG--RRHG 475
|
490
....*....|....*...
gi 1550356027 466 TDSIKFWTRTKTI-TSRW 482
Cdd:PRK09407 476 AEGLLKYTESQTIaTQRV 493
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
7-478 |
1.25e-65 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 220.08 E-value: 1.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAA--QPKWAATNPQRRARVFMKFVQLLNDNMNELA 84
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 85 EMLSREHGKTIDDAKG-DIVRGLEVCEFVIGIPHLQKSEFTEGAGPgIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPA 163
Cdd:PLN02766 104 ALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQ-LQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 164 IACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNG---DKGAvdAILTHPDIAAVSFVGSTPIARYVYGTAAM- 239
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfgpTAGA--AIASHMDVDKVSFTGSTEVGRKIMQAAATs 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 240 NGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKA 319
Cdd:PLN02766 261 NLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASS-RVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 320 DMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFklqgYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEE 399
Cdd:PLN02766 340 RQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPC----GDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 400 ALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNvpipVPLAYHS---FGGWKSSSFGdlNQHGTDSIKFWTRTK 476
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN----CYFAFDPdcpFGGYKMSGFG--RDQGMDALDKYLQVK 489
|
..
gi 1550356027 477 TI 478
Cdd:PLN02766 490 SV 491
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
24-480 |
1.36e-65 |
|
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: 219.09 E-value: 1.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 24 FNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAK-GDI 102
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 103 VRGLEVCEFVI--GIPHLQksefTEGAGPGIDMYSIR-----QPVGIGAGITPFNFP---GMIPMwmfAPAIACGNAFIL 172
Cdd:cd07098 81 LVTCEKIRWTLkhGEKALR----PESRPGGLLMFYKRarveyEPLGVVGAIVSWNYPfhnLLGPI---IAALFAGNAIVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 173 KPSER-----DPSVPIrLAELMIEAGLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCF 247
Cdd:cd07098 154 KVSEQvawssGFFLSI-IRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 248 GGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTK 327
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIE-RVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 328 EAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKH 407
Cdd:cd07098 312 ARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANST 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 408 EYGNGVAIYTRDGDAARDFASRINIGMVGVN--------VPIPvplayhsFGGWKSSSFGDLNqhGTDSIKFWTRTKTIT 479
Cdd:cd07098 392 EYGLGASVFGKDIKRARRIASQLETGMVAINdfgvnyyvQQLP-------FGGVKGSGFGRFA--GEEGLRGLCNPKSVT 462
|
.
gi 1550356027 480 S 480
Cdd:cd07098 463 E 463
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
7-474 |
2.59e-65 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 219.22 E-value: 2.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGTSGRVSNIFNPATGEVQG-----TVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMN 81
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGdipaaTAEDVDAAVEAARKAFKRNKGKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 82 ELAEMLSREHGKTIDDAKGDI--VRGL-----EVCEFVIGIPH----LQKSEFtegagpgiDMYSIRQPVGIGAGITPFN 150
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMddVAGCfeyyaDLAEALDAKQKapvsLPMETF--------KGYVLKEPLGVVGLITPWN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 151 FPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNG---DKGAvdAILTHPDIAAVSFVGST 227
Cdd:PLN02467 163 YPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGlgtEAGA--PLASHPGVDKIAFTGST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 228 PIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAAN-ALIGAgYGSAGERCMAISvAVPVGEETANRLIDKLVPMV 306
Cdd:PLN02467 241 ATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEwAMFGC-FWTNGQICSATS-RLLVHERIASEFLEKLVKWA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 307 ESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRdfKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFG 386
Cdd:PLN02467 319 KNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGK--RPEHLKKGFFIEPTIITDVTTSMQIWREEVFG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 387 PVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVpLAYHSFGGWKSSSFG-DLNQHG 465
Cdd:PLN02467 397 PVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPC-FCQAPWGGIKRSGFGrELGEWG 475
|
490
....*....|..
gi 1550356027 466 TD---SIKFWTR 474
Cdd:PLN02467 476 LEnylSVKQVTK 487
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
7-478 |
4.57e-65 |
|
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: 218.13 E-value: 4.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAA--QPKWAATNPQRRARVFMKFVQLLNDNMNELA 84
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 85 EMLSREHGKTIDDAK-GDIVRGLEVCEFVIGIPHLQKSEFTEGAGPgIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPA 163
Cdd:cd07142 87 ALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGP-HHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 164 IACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNG---DKGAvdAILTHPDIAAVSFVGSTPIARYVYGTAA-M 239
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGfgpTAGA--AIASHMDVDKVAFTGSTEVGKIIMQLAAkS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 240 NGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKA 319
Cdd:cd07142 244 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGS-RTFVHESIYDEFVEKAKARALKRVVGDPFRKGV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 320 DMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEE 399
Cdd:cd07142 323 EQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGY----YIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 400 ALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVN------VPIPvplayhsFGGWKSSSFGdlNQHGTDSIKFWT 473
Cdd:cd07142 399 VIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcydvfdASIP-------FGGYKMSGIG--REKGIYALNNYL 469
|
....*
gi 1550356027 474 RTKTI 478
Cdd:cd07142 470 QVKAV 474
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
17-481 |
1.42e-64 |
|
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: 217.45 E-value: 1.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 17 SGRVSNIFNP-ATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTI 95
Cdd:cd07083 30 TKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 96 DDAKGDIVRGLEVCEF--VIGIPHLQKSEFTEGAgPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILK 173
Cdd:cd07083 110 VEAIDDVAEAIDFIRYyaRAALRLRYPAVEVVPY-PGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 174 PSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-HPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCF----- 247
Cdd:cd07083 189 PAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTeHERIRGINFTGSLETGKKIYEAAARLAPGQTWFkrlyv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 248 -GGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVT 326
Cdd:cd07083 269 eTGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLI-LTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVID 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 327 KEAEQRIRSLIDSGIEQGaKLVVDGRdfKLQGyeNGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVR--ARNYEEALSLP 404
Cdd:cd07083 348 AEQEAKVLSYIEHGKNEG-QLVLGGK--RLEG--EGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRykDDDFAEALEVA 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550356027 405 MKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPL-AYHSFGGWKSSSFGDlNQHGTDSIKFWTRTKTITSR 481
Cdd:cd07083 423 NSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALvGVQPFGGFKLSGTNA-KTGGPHYLRRFLEMKAVAER 499
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
26-480 |
5.01e-64 |
|
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: 214.48 E-value: 5.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 26 PATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKgdivrg 105
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAF------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 106 LEVCEFVIGI-------PHLQKSEFTEGAGPGI-DMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSER 177
Cdd:cd07101 77 EEVLDVAIVAryyarraERLLKPRRRRGAIPVLtRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 178 DPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIaaVSFVGSTPIARYVYGTAAMN--GKRAQCfgGAKNHM 254
Cdd:cd07101 157 TALTALWAVELLIEAGLPRDLWQVVTGPGSEVgGAIVDNADY--VMFTGSTATGRVVAERAGRRliGCSLEL--GGKNPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 255 IIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIR 334
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIE-RIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 335 SLIDSGIEQGAKLVVDGR---DFKLQGYENghfiggCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGN 411
Cdd:cd07101 312 AHVDDAVAKGATVLAGGRarpDLGPYFYEP------TVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1550356027 412 GVAIYTRDGDAARDFASRINIGMVGVN-------VPIPVPLayhsfGGWKSSSFGdlNQHGTDSIKFWTRTKTITS 480
Cdd:cd07101 386 NASVWTRDGARGRRIAARLRAGTVNVNegyaaawASIDAPM-----GGMKDSGLG--RRHGAEGLLKYTETQTVAV 454
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
6-477 |
1.39e-63 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 214.62 E-value: 1.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 6 HFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAE 85
Cdd:PLN00412 18 YYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 86 MLSREHGKTIDDAKGDIVRGLEVCEFVI--GIPHLQKSEF-TEGAGPGID-----MYSiRQPVGIGAGITPFNFPGMIPM 157
Cdd:PLN00412 98 CLVKEIAKPAKDAVTEVVRSGDLISYTAeeGVRILGEGKFlVSDSFPGNErnkycLTS-KIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 158 WMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGdKGAV--DAILTHPDIAAVSFV-GSTPIAryVY 234
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTG-KGSEigDFLTMHPGVNCISFTgGDTGIA--IS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 235 GTAAMngKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVaVPVGEETANRLIDKLVPMVESLRIGPY 314
Cdd:PLN00412 254 KKAGM--VPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKV-VLVMESVADALVEKVNAKVAKLTVGPP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 315 TDEkADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRdfklqgyENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRA 394
Cdd:PLN00412 331 EDD-CDITPVVSESSANFIEGLVMDAKEKGATFCQEWK-------REGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 395 RNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGGWKSSSFGdlNQHGTDSIKFWTR 474
Cdd:PLN00412 403 NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDHFPFQGLKDSGIG--SQGITNSINMMTK 480
|
...
gi 1550356027 475 TKT 477
Cdd:PLN00412 481 VKS 483
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
7-459 |
2.19e-63 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 213.61 E-value: 2.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEM 86
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 87 LSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIAC 166
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 167 GNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-HPDIAAVSFVGSTPIARYVYGTAAMNGKRAQ 245
Cdd:PRK11241 174 GCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTsNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 246 CFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVV 325
Cdd:PRK11241 254 LELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCAN-RLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 326 TKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQgyenGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPM 405
Cdd:PRK11241 333 DEKAVAKVEEHIADALEKGARVVCGGKAHELG----GNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1550356027 406 KHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIpVPLAYHSFGGWKSSSFG 459
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLG 461
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
7-478 |
4.65e-63 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 213.22 E-value: 4.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAA--QPKWAATNPQRRARVFMKFVQLLNDNMNELA 84
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 85 EMLSREHGKTI-----DDAKGDIvRGL----EVCEFVIGiphlqksEFTEGAGPGIDMYsIRQPVGIGAGITPFNFPGMI 155
Cdd:PRK09847 103 LLETLDTGKPIrhslrDDIPGAA-RAIrwyaEAIDKVYG-------EVATTSSHELAMI-VREPVGVIAAIVPWNFPLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 156 PMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNG-DKGAVDAILTHPDIAAVSFVGSTPIARYVY 234
Cdd:PRK09847 174 TCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 235 GTAA-MNGKRAQCFGGAKNHMIIMPDA-DLDQAANALIGAGYGSAGERCMAiSVAVPVGEETANRLIDKLVPMVESLRIG 312
Cdd:PRK09847 254 KDAGdSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIA-GTRLLLEESIADEFLALLKQQAQNWQPG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 313 PYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGaKLVVDGRdfklqgyENGH--FIGGCLFDDVTPDMDIYKTEIFGPVLS 390
Cdd:PRK09847 333 HPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGR-------NAGLaaAIGPTIFVDVDPNASLSREEIFGPVLV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 391 VVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNV----PIPVPlayhsFGGWKSSSFG-DLNQHG 465
Cdd:PRK09847 405 VTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMTVP-----FGGYKQSGNGrDKSLHA 479
|
490
....*....|...
gi 1550356027 466 TDsiKFwTRTKTI 478
Cdd:PRK09847 480 LE--KF-TELKTI 489
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
5-459 |
1.09e-61 |
|
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: 209.23 E-value: 1.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 5 GHFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELA 84
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 85 EMLSREHGKTIDDAKG-DIVRGLEVCEFVIGIPHLQkseftEGAGPGID--MYSI--RQPVGIGAGITPFNFPGMIPMWM 159
Cdd:cd07117 82 MVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAE-----EGSANMIDedTLSIvlREPIGVVGQIIPWNFPFLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 160 FAPAIACGNAFILKPSErdpSVPIRLAELM--IEAGLPAGILNVVNGdKGAV--DAILTHPDIAAVSFVGSTPIARYVYG 235
Cdd:cd07117 157 LAPALAAGNTVVIKPSS---TTSLSLLELAkiIQDVLPKGVVNIVTG-KGSKsgEYLLNHPGLDKLAFTGSTEVGRDVAI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 236 TAAMNGKRAQCFGGAKNHMIIMPDADLDQAanaLIGAGYG---SAGERCMAISvAVPVGEETANRLIDKLVPMVESLRIG 312
Cdd:cd07117 233 AAAKKLIPATLELGGKSANIIFDDANWDKA---LEGAQLGilfNQGQVCCAGS-RIFVQEGIYDEFVAKLKEKFENVKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 313 PYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVV 392
Cdd:cd07117 309 NPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVI 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550356027 393 RARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPlAYHSFGGWKSSSFG 459
Cdd:cd07117 389 KFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIP-AGAPFGGYKKSGIG 454
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
25-459 |
1.11e-61 |
|
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: 208.25 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 25 NPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVR 104
Cdd:cd07147 5 NPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 105 GLEVCEFV------IGIPHLQKSEFTEGAGP-GIDMysiRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSER 177
Cdd:cd07147 85 AIDTFRIAaeeatrIYGEVLPLDISARGEGRqGLVR---RFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 178 DPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAamnGKRAQCF---GGAKnhM 254
Cdd:cd07147 162 TPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARA---GKKKVVLelgGNAA--V 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 255 IIMPDADLDQAANALIGAGYGSAGERCmaISVA-VPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRI 333
Cdd:cd07147 237 IVDSDADLDFAAQRIIFGAFYQAGQSC--ISVQrVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 334 RSLIDSGIEQGAKLVVDGRdfklqgyENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGV 413
Cdd:cd07147 315 EGWVNEAVDAGAKLLTGGK-------RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1550356027 414 AIYTRDGDAARDFASRINIGMVGVN-VPI----PVPlayhsFGGWKSSSFG 459
Cdd:cd07147 388 GVFTRDLEKALRAWDELEVGGVVINdVPTfrvdHMP-----YGGVKDSGIG 433
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
7-479 |
4.32e-60 |
|
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: 205.04 E-value: 4.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAA--QPKWAATNPQRRARVFMKFVQLLNDNMNELA 84
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 85 EMLSREHGKTIDDA-KGDIVRGLEVCEFVIG---------IPHLQkseftegAGPGIDM-YSIRQPVGIGAGITPFNFPG 153
Cdd:cd07140 89 TIESLDSGAVYTLAlKTHVGMSIQTFRYFAGwcdkiqgktIPINQ-------ARPNRNLtLTKREPIGVCGIVIPWNYPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 154 MIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARY 232
Cdd:cd07140 162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGKH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 233 VYGTAAM-NGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVESLRI 311
Cdd:cd07140 242 IMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAG-RLFVEESIHDEFVRRVVEEVKKMKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 312 GPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKTEIFGPVLSV 391
Cdd:cd07140 321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFGPIMII 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 392 VRARN--YEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAyHSFGGWKSSSFG-DLnqhGTDS 468
Cdd:cd07140 397 SKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVA-APFGGFKQSGFGkDL---GEEA 472
|
490
....*....|.
gi 1550356027 469 IKFWTRTKTIT 479
Cdd:cd07140 473 LNEYLKTKTVT 483
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
71-465 |
5.38e-56 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 192.26 E-value: 5.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 71 KFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFN 150
Cdd:PRK10090 3 KIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 151 FPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGdKGAV--DAILTHPDIAAVSFVGSTP 228
Cdd:PRK10090 83 FPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLG-RGETvgQELAGNPKVAMVSMTGSVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 229 IARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISvAVPVGEETANRLIDKLVPMVES 308
Cdd:PRK10090 162 AGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAE-RVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 309 LRIG-PYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKTEIFGP 387
Cdd:PRK10090 241 VQFGnPAERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGY----YYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 388 VLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVP-IPVPLAYHSfgGWKSSSFGDLN-QHG 465
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINREnFEAMQGFHA--GWRKSGIGGADgKHG 394
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
5-464 |
2.44e-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: 192.28 E-value: 2.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 5 GHFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELA 84
Cdd:cd07116 2 DNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 85 EMLSREHGKTIDDAKG-DIVRGLEVCEFVIGIPHLQkseftEGAGPGID----MYSIRQPVGIGAGITPFNFPGMIPMWM 159
Cdd:cd07116 82 VAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQ-----EGSISEIDentvAYHFHEPLGVVGQIIPWNFPLLMATWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 160 FAPAIACGNAFILKPSERDPSVPIRLAELmIEAGLPAGILNVVNGDKGAVDAIL-THPDIAAVSFVGSTPIARYVYGTAA 238
Cdd:cd07116 157 LAPALAAGNCVVLKPAEQTPASILVLMEL-IGDLLPPGVVNVVNGFGLEAGKPLaSSKRIAKVAFTGETTTGRLIMQYAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 239 MNGKRAQCFGGAKNHMIIMP------DADLDQAANALIGAGYGSaGERCMAISVAVpVGEETANRLIDKLVPMVESLRIG 312
Cdd:cd07116 236 ENIIPVTLELGGKSPNIFFAdvmdadDAFFDKALEGFVMFALNQ-GEVCTCPSRAL-IQESIYDRFMERALERVKAIKQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 313 PYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYENGHFIGGCLFDDvTPDMDIYKTEIFGPVLSVV 392
Cdd:cd07116 314 NPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVT 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550356027 393 RARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPlAYHSFGGWKSSSFGDLNQH 464
Cdd:cd07116 393 TFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYP-AHAAFGGYKQSGIGRENHK 463
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
6-480 |
6.97e-55 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 192.33 E-value: 6.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 6 HFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAA--QPKWAATNPQRRARVFMKFVQLLNDNMNEL 83
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 84 AEMLSREHGKTIDDAKG-----------------DIVRGLEVCefVIGIPHLQkseftegagpgidmySIRQPVGIGAGI 146
Cdd:PLN02466 140 AALETWDNGKPYEQSAKaelpmfarlfryyagwaDKIHGLTVP--ADGPHHVQ---------------TLHEPIGVAGQI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 147 TPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNG---DKGAvdAILTHPDIAAVSF 223
Cdd:PLN02466 203 IPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfgpTAGA--ALASHMDVDKLAF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 224 VGSTPIARYVYGTAAM-NGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKL 302
Cdd:PLN02466 281 TGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTF-VHERVYDEFVEKA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 303 VPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKT 382
Cdd:PLN02466 360 KARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQDDMLIAQD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 383 EIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVpIPVPLAYHSFGGWKSSSFGdlN 462
Cdd:PLN02466 436 EIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNC-FDVFDAAIPFGGYKMSGIG--R 512
|
490
....*....|....*...
gi 1550356027 463 QHGTDSIKFWTRTKTITS 480
Cdd:PLN02466 513 EKGIYSLNNYLQVKAVVT 530
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
54-456 |
5.40e-54 |
|
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: 187.48 E-value: 5.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 54 QPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGdivrglEVCEFV--IGIPHLQKSEFT-EGAGPG 130
Cdd:cd07095 13 FPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQT------EVAAMAgkIDISIKAYHERTgERATPM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 131 IDMYS-IRQ-PVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGA 208
Cdd:cd07095 87 AQGRAvLRHrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRET 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 209 VDAILTHPDIAAVSFVGSTPIARYVYGTAAMN-GKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAIS-V 286
Cdd:cd07095 167 GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRpGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARrL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 287 AVPVGEEtANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKlqgyENGHFIG 366
Cdd:cd07095 247 IVPDGAV-GDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV----AGTAFLS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 367 GCLFdDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLA 446
Cdd:cd07095 322 PGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGASS 400
|
410
....*....|
gi 1550356027 447 YHSFGGWKSS 456
Cdd:cd07095 401 TAPFGGVGLS 410
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
25-478 |
1.62e-52 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 184.17 E-value: 1.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 25 NPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVR 104
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 105 GLEVCEFVIG-IPHLQKSEFTEGAGPGIDMYSIR-QPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVP 182
Cdd:PRK09406 87 CAKGFRYYAEhAEALLADEPADAAAVGASRAYVRyQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 183 IRLAELMIEAGLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADL 262
Cdd:PRK09406 167 LYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 263 DQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIE 342
Cdd:PRK09406 247 DRAAETAVTARVQNNGQSCIAAKRFI-VHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 343 QGAKLVVDGRdfKLQGyeNGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDA 422
Cdd:PRK09406 326 AGATILCGGK--RPDG--PGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550356027 423 ARDFASRINIGMVGVN---VPIP-VPlayhsFGGWKSSSFG-DLNQHGtdsIKFWTRTKTI 478
Cdd:PRK09406 402 QERFIDDLEAGQVFINgmtVSYPeLP-----FGGVKRSGYGrELSAHG---IREFCNIKTV 454
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
25-459 |
7.93e-52 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 182.37 E-value: 7.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 25 NPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVR 104
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 105 GLEVCE-FVIGIPHLQKSEFT--EGAGPGIDMysirQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSV 181
Cdd:PRK13968 93 SANLCDwYAEHGPAMLKAEPTlvENQQAVIEY----RPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 182 PIRLAELMIEAGLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDAD 261
Cdd:PRK13968 169 AQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 262 LDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGI 341
Cdd:PRK13968 249 LELAVKAAVAGRYQNTGQVCAAAKRFI-IEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 342 EQGAKLVVDGRdfKLQGyeNGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGD 421
Cdd:PRK13968 328 AEGARLLLGGE--KIAG--AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
410 420 430
....*....|....*....|....*....|....*...
gi 1550356027 422 AARDFASRINIGMVGVNvPIPVPLAYHSFGGWKSSSFG 459
Cdd:PRK13968 404 QARQMAARLECGGVFIN-GYCASDARVAFGGVKKSGFG 440
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
15-479 |
8.43e-50 |
|
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: 177.40 E-value: 8.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 15 GTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKT 94
Cdd:cd07130 8 GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 95 IDDAKGDIVRGLEVCEFVIG---------IPhlqkSEftegaGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIA 165
Cdd:cd07130 88 LPEGLGEVQEMIDICDFAVGlsrqlygltIP----SE-----RPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 166 CGNAFILKPSERDPSVPIRLAELMIEA----GLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAmng 241
Cdd:cd07130 159 CGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVA--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 242 KRaqcFG------GAKNHMIIMPDADLDQAANALIGAGYGSAGERCMaisvavpvgeeTANRLI----------DKLVPM 305
Cdd:cd07130 236 AR---FGrsllelGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCT-----------TTRRLIvhesiydevlERLKKA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 306 VESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRdfKLQGyeNGHFIGGCLFdDVTPDMDIYKTEIF 385
Cdd:cd07130 302 YKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGK--VIDG--PGNYVEPTIV-EGLSDAPIVKEETF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 386 GPVLSVVRARNYEEALslpmkhEYGNGV------AIYTRDGDAARDFasrinIGMVG-----VNVPIPVPLAY--HSFGG 452
Cdd:cd07130 377 APILYVLKFDTLEEAI------AWNNEVpqglssSIFTTDLRNAFRW-----LGPKGsdcgiVNVNIGTSGAEigGAFGG 445
|
490 500
....*....|....*....|....*..
gi 1550356027 453 WKSSSFGdlNQHGTDSIKFWTRTKTIT 479
Cdd:cd07130 446 EKETGGG--RESGSDAWKQYMRRSTCT 470
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
3-438 |
2.11e-46 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 173.46 E-value: 2.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 3 ELGHFIDGKRVAG----TSGRVSNIFNPATGEVQ-GTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLN 77
Cdd:PRK11904 542 AIAAFLEKQWQAGpiinGEGEARPVVSPADRRRVvGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLE 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 78 DNMNELAEMLSREHGKTIDDAKGDiVRglEVCEF-----VIGIPHLQKSEFTEgaGP-GIDMYSIRQPVGIGAGITPFNF 151
Cdd:PRK11904 622 ANRAELIALCVREAGKTLQDAIAE-VR--EAVDFcryyaAQARRLFGAPEKLP--GPtGESNELRLHGRGVFVCISPWNF 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 152 PGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-HPDIAAVSFVGSTPIA 230
Cdd:PRK11904 697 PLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTaDPRIAGVAFTGSTETA 776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 231 RYVYGT-AAMNGKRAqCF----GGAkNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPM 305
Cdd:PRK11904 777 RIINRTlAARDGPIV-PLiaetGGQ-NAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLF-VQEDIADRVIEMLKGA 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 306 VESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSgIEQGAKLVvdgrdFKLQ---GYENGHFIGGCLFDdvTPDMDIYKT 382
Cdd:PRK11904 854 MAELKVGDPRLLSTDVGPVIDAEAKANLDAHIER-MKREARLL-----AQLPlpaGTENGHFVAPTAFE--IDSISQLER 925
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1550356027 383 EIFGPVLSVVR--ARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVN 438
Cdd:PRK11904 926 EVFGPILHVIRykASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
18-438 |
2.20e-46 |
|
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: 168.55 E-value: 2.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 18 GRVSNIFNPATGEVQ-GTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTID 96
Cdd:TIGR01238 50 GEAQPVTNPADRRDIvGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 97 DAKGDIVRGLEVCEFVIGIPHLQKSEFTEgagpgidmysirQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSE 176
Cdd:TIGR01238 130 NAIAEVREAVDFCRYYAKQVRDVLGEFSV------------ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 177 RDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-HPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCF---GGAKN 252
Cdd:TIGR01238 198 QTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTsDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaeTGGQN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 253 HMIIMPDADLDQAANALIGAGYGSAGERCMAISVaVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQR 332
Cdd:TIGR01238 278 AMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRV-LCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQN 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 333 IRSLIDSgIEQGAKLVVDGRDFKLQGYENGHFIGGCLFDdvTPDMDIYKTEIFGPVLSVVR--ARNYEEALSLPMKHEYG 410
Cdd:TIGR01238 357 LLAHIEH-MSQTQKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRykARELDQIVDQINQTGYG 433
|
410 420
....*....|....*....|....*...
gi 1550356027 411 NGVAIYTRDGDAARDFASRINIGMVGVN 438
Cdd:TIGR01238 434 LTMGVHSRIETTYRWIEKHARVGNCYVN 461
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
5-441 |
2.55e-43 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 159.74 E-value: 2.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 5 GHFIDGKRVAGTSGRVSNiFNPATGEV--QGTvaLASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNE 82
Cdd:PRK09457 2 TLWINGDWIAGQGEAFES-RNPVSGEVlwQGN--DATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 83 LAEMLSREHGKTIDDAKgdivrgLEVCEFV--IGIPHLQKSEFT-EGAGPGID-MYSIR-QPVGIGAGITPFNFPGMIPM 157
Cdd:PRK09457 79 LAEVIARETGKPLWEAA------TEVTAMInkIAISIQAYHERTgEKRSEMADgAAVLRhRPHGVVAVFGPYNFPGHLPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 158 WMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGStpiarYVYGT- 236
Cdd:PRK09457 153 GHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGS-----ANTGYl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 237 -----AAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCM-AISVAVPVGEEtANRLIDKLVPMVESLR 310
Cdd:PRK09457 228 lhrqfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTcARRLLVPQGAQ-GDAFLARLVAVAKRLT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 311 IGPYTDEKAD-MGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRdfklQGYENGHFIGGCLFdDVTPDMDIYKTEIFGPVL 389
Cdd:PRK09457 307 VGRWDAEPQPfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMT----QLQAGTGLLTPGII-DVTGVAELPDEEYFGPLL 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1550356027 390 SVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPI 441
Cdd:PRK09457 382 QVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPL 433
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
62-459 |
2.92e-41 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 153.73 E-value: 2.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 62 PQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVR---GLEVCEFVIGipHLQKSEFTEG---AGPGIDMYS 135
Cdd:cd07148 43 AHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRaidGVELAADELG--QLGGREIPMGltpASAGRIAFT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 136 IRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTH 215
Cdd:cd07148 121 TREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 216 PDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNhMIIMPDADLDQAANALIGAGYGSAGERCmaISVA-VPVGEET 294
Cdd:cd07148 201 PRVAFFSFIGSARVGWMLRSKLAPGTRCALEHGGAAP-VIVDRSADLDAMIPPLVKGGFYHAGQVC--VSVQrVFVPAEI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 295 ANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKLQGYENghfigGCLFDDvT 374
Cdd:cd07148 278 ADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTYAP-----TVLLDP-P 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 375 PDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGGWK 454
Cdd:cd07148 352 RDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRR 431
|
....*
gi 1550356027 455 SSSFG 459
Cdd:cd07148 432 QSGYG 436
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
4-479 |
1.63e-37 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 144.21 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 4 LGHFIDGKrvAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNEL 83
Cdd:PLN02315 21 LGCYVGGE--WRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 84 AEMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPA 163
Cdd:PLN02315 99 GRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 164 IACGNAFILKPSERDPSVPIRL----AELMIEAGLPAGILNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVygTAAM 239
Cdd:PLN02315 179 LVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMV--QQTV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 240 NGKRAQCFG--GAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVpVGEETANRLIDKLVPMVESLRIGPYTDE 317
Cdd:PLN02315 257 NARFGKCLLelSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLL-LHESIYDDVLEQLLTVYKQVKIGDPLEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 318 KADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKlqgyENGHFIGGCLFDdVTPDMDIYKTEIFGPVLSVVRARNY 397
Cdd:PLN02315 336 GTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE----SEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 398 EEALSLPMKHEYGNGVAIYTRDGDAARDFASRI--NIGMVGVNVPIPVPLAYHSFGGWKSSSFGdlNQHGTDSIKFWTRT 475
Cdd:PLN02315 411 EEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGG--REAGSDSWKQYMRR 488
|
....
gi 1550356027 476 KTIT 479
Cdd:PLN02315 489 STCT 492
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
23-393 |
1.65e-37 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 147.32 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 23 IFNPA-TGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGD 101
Cdd:PRK11905 571 VLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 102 iVRglEVCEFvigiphL-----QKSEFTEGAGpgidmysiRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSE 176
Cdd:PRK11905 651 -VR--EAVDF------LryyaaQARRLLNGPG--------HKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAE 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 177 RDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-HPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCF----GGaK 251
Cdd:PRK11905 714 QTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVaDPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaetGG-Q 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 252 NHMIIMPDADLDQAANALIGAGYGSAGERCMAISVaVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQ 331
Cdd:PRK11905 793 NAMIVDSSALPEQVVADVIASAFDSAGQRCSALRV-LCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQA 871
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550356027 332 RIRSLIDSGIEQGAKLvvdgrdFKL---QGYENGHFIGGCLFDdvTPDMDIYKTEIFGPVLSVVR 393
Cdd:PRK11905 872 NIEAHIEAMRAAGRLV------HQLplpAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVR 928
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
55-474 |
4.25e-36 |
|
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: 138.91 E-value: 4.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 55 PKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTID---DAKGDIV--RGLEVCEFVIGIPHlqKSEFTEGAGP 129
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMfaeNICGDQVqlRARAFVIYSYRIPH--EPGNHLGQGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 130 GIDMYSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAG-LPAGILNVVNGDKGA 208
Cdd:cd07084 91 KQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 209 VDAILTHPDIAAVSFVGSTPIARyvygTAAMNGKRAQCFG--GAKNHMIIMPDAD-LDQAANALIGAGYGSAGERCMAIS 285
Cdd:cd07084 171 MQALLLHPNPKMVLFTGSSRVAE----KLALDAKQARIYLelAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 286 VA-VPVGEETaNRLIDKLVPMVESLrigpyTDEKADMGPVVTKEAEQRIRSLidsGIEQGAKLVVDGRDFKLQGYENghF 364
Cdd:cd07084 247 MLfVPENWSK-TPLVEKLKALLARR-----KLEDLLLGPVQTFTTLAMIAHM---ENLLGSVLLFSGKELKNHSIPS--I 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 365 IGGC----LFDDVTPDMDIYKT---EIFGPVLSVVRARNYEEALSLPMKhEYGNG---VAIYTRDGDAARDFASRINI-G 433
Cdd:cd07084 316 YGACvasaLFVPIDEILKTYELvteEIFGPFAIVVEYKKDQLALVLELL-ERMHGsltAAIYSNDPIFLQELIGNLWVaG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1550356027 434 MVGVNVPIP---VPLAYHSFGGWKSSSFGDLNqhGTDSIKFWTR 474
Cdd:cd07084 395 RTYAILRGRtgvAPNQNHGGGPAADPRGAGIG--GPEAIKLVWR 436
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
8-438 |
2.38e-35 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 140.84 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 8 IDGKRVAGTSGRVsniFNPA-TGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEM 86
Cdd:COG4230 562 IAGEAASGEARPV---RNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMAL 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 87 LSREHGKTIDDAKGdivrglEVCEFVigiphlqksEF---------TEGAGPgidmySIRQPVGIGAGITPFNFP----- 152
Cdd:COG4230 639 LVREAGKTLPDAIA------EVREAV---------DFcryyaaqarRLFAAP-----TVLRGRGVFVCISPWNFPlaift 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 153 GMIpmwmfAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT-HPDIAAVSFVGSTPIAR 231
Cdd:COG4230 699 GQV-----AAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVaDPRIAGVAFTGSTETAR 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 232 yvygtaAMNGKRAQCFG---------GAKNHMIImpD--ADLDQAANALIGAGYGSAGERCMAISVaVPVGEETANRLID 300
Cdd:COG4230 774 ------LINRTLAARDGpivpliaetGGQNAMIV--DssALPEQVVDDVLASAFDSAGQRCSALRV-LCVQEDIADRVLE 844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 301 KLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSgIEQGAKLVvdgrdFKL---QGYENGHFIGGCLFDdvTPDM 377
Cdd:COG4230 845 MLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIER-MRAEGRLV-----HQLplpEECANGTFVAPTLIE--IDSI 916
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550356027 378 DIYKTEIFGPVLSVVR--------------ARNYeeALSLpmkheygngvAIYTRDGDAARDFASRINIGMVGVN 438
Cdd:COG4230 917 SDLEREVFGPVLHVVRykadeldkvidainATGY--GLTL----------GVHSRIDETIDRVAARARVGNVYVN 979
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
54-424 |
1.82e-34 |
|
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: 135.79 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 54 QPKWAATNPQRRARVFMKFVQLLNDNMNEL---AEMLSRehGKTIDDAKGDIvrGLEVCEFvigiphlqkseFTEGAGPG 130
Cdd:cd07123 82 RKEWARMPFEDRAAIFLKAADLLSGKYRYElnaATMLGQ--GKNVWQAEIDA--ACELIDF-----------LRFNVKYA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 131 IDMYSIrQPVGIGAG----------------ITPFNFP---GMIPMwmfAPAIAcGNAFILKPSERDPSVPIRLAELMIE 191
Cdd:cd07123 147 EELYAQ-QPLSSPAGvwnrleyrplegfvyaVSPFNFTaigGNLAG---APALM-GNVVLWKPSDTAVLSNYLVYKILEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 192 AGLPAGILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCF----G--GAKNHMIIMPDADLDQ 264
Cdd:cd07123 222 AGLPPGVINFVPGDGPVVgDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYprivGetGGKNFHLVHPSADVDS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 265 AANALIGAGYGSAGERCMAISVA-VPvgEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQ 343
Cdd:cd07123 302 LVTATVRGAFEYQGQKCSAASRAyVP--ESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSD 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 344 -GAKLVVDGRDFKLQGYenghFIGGCLFDDVTPDMDIYKTEIFGPVLS--VVRARNYEEALSLPMK-HEYGNGVAIYTRD 419
Cdd:cd07123 380 pEAEIIAGGKCDDSVGY----FVEPTVIETTDPKHKLMTEEIFGPVLTvyVYPDSDFEETLELVDTtSPYALTGAIFAQD 455
|
....*
gi 1550356027 420 GDAAR 424
Cdd:cd07123 456 RKAIR 460
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
134-478 |
1.22e-32 |
|
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: 128.80 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 134 YSIRQPVGIGAGITPFNFP---GMIPMwmfAPAIACGNAFILKPSERDPSVPIRLAELmIEAGLPAGILNVVNGDKGAVD 210
Cdd:cd07087 95 YVIPEPLGVVLIIGPWNYPlqlALAPL---IGAIAAGNTVVLKPSELAPATSALLAKL-IPKYFDPEAVAVVEGGVEVAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 211 AILTHP-DIaaVSFVGSTPIARYVYGTAAMNgkRAQC---FGGaKNHMIIMPDADLDQAANALIGAGYGSAGERCMAisv 286
Cdd:cd07087 171 ALLAEPfDH--IFFTGSPAVGKIVMEAAAKH--LTPVtleLGG-KSPCIVDKDANLEVAARRIAWGKFLNAGQTCIA--- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 287 avP----VGEETANRLIDKLVPMVESLrIGPYTDEKADMGPVVTKEAEQRIRSLIDSGieqgaKLVVDGrdfklQGYENG 362
Cdd:cd07087 243 --PdyvlVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDG-----KVVIGG-----QVDKEE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 363 HFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEygNGVAIY--TRDGDAARDFASRINIGMVGVNVP 440
Cdd:cd07087 310 RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRP--KPLALYlfSEDKAVQERVLAETSSGGVCVNDV 387
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1550356027 441 IpVPLAYHS--FGGWKSSSFGdlNQHGTDSIKFWTRTKTI 478
Cdd:cd07087 388 L-LHAAIPNlpFGGVGNSGMG--AYHGKAGFDTFSHLKSV 424
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
55-393 |
1.40e-30 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 126.24 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 55 PKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDiVRglEVCEFVIGIPHLQKSEFTEgagpgiDMY 134
Cdd:PRK11809 696 PIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAE-VR--EAVDFLRYYAGQVRDDFDN------DTH 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 135 sirQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILT 214
Cdd:PRK11809 767 ---RPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALV 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 215 -HPDIAAVSFVGSTPIARYVYGTAAmngKRAQCFG---------GAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAI 284
Cdd:PRK11809 844 aDARVRGVMFTGSTEVARLLQRNLA---GRLDPQGrpipliaetGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSAL 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 285 SVaVPVGEETANRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGRDFKlQGYENGHF 364
Cdd:PRK11809 921 RV-LCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENS-EDWQSGTF 998
|
330 340 350
....*....|....*....|....*....|.
gi 1550356027 365 IGGCL--FDDVtpdmDIYKTEIFGPVLSVVR 393
Cdd:PRK11809 999 VPPTLieLDSF----DELKREVFGPVLHVVR 1025
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
75-478 |
2.08e-28 |
|
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: 116.94 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 75 LLNDNMNELAEMLSREHGKT--------IDDAKGDIvrgLEVCEfviGIPHLQKSEFTEGAGPGIDMYSIR---QPVGIG 143
Cdd:cd07135 39 AVKDNEEAIVEALKKDLGRPpfetllteVSGVKNDI---LHMLK---NLKKWAKDEKVKDGPLAFMFGKPRirkEPLGVV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 144 AGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELmIEAGLPAGILNVVNGDKGAVDAILTHP-DiaAVS 222
Cdd:cd07135 113 LIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVVQGGVPETTALLEQKfD--KIF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 223 FVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVaVPVGEETANRLIDKL 302
Cdd:cd07135 190 YTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDY-VLVDPSVYDEFVEEL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 303 VPMVESLrIGPYTDEKADMGPVVTKEAEQRIRSLIDsgiEQGAKLVVDG-RDfklqgyENGHFIGGCLFDDVTPDMDIYK 381
Cdd:cd07135 269 KKVLDEF-YPGGANASPDYTRIVNPRHFNRLKSLLD---TTKGKVVIGGeMD------EATRFIPPTIVSDVSWDDSLMS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 382 TEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVN-VPIPVPLAYHSFGGWKSSSFGd 460
Cdd:cd07135 339 EELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdTLIHVGVDNAPFGGVGDSGYG- 417
|
410
....*....|....*...
gi 1550356027 461 lNQHGTDSIKFWTRTKTI 478
Cdd:cd07135 418 -AYHGKYGFDTFTHERTV 434
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
146-438 |
9.90e-28 |
|
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: 115.02 E-value: 9.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 146 ITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAElMIEAGLPAGILNVVNGDKGAVDAILTHP-DiaAVSFV 224
Cdd:cd07134 107 ISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAK-IIREAFDEDEVAVFEGDAEVAQALLELPfD--HIFFT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 225 GSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMA---ISVAVPVGEETANRLIDK 301
Cdd:cd07134 184 GSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIApdyVFVHESVKDAFVEHLKAE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 302 LVPMVESlriGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVDGrdfklQGYENGHFIGGCLFDDVTPDMDIYK 381
Cdd:cd07134 264 IEKFYGK---DAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG-----QFDAAQRYIAPTVLTNVTPDMKIMQ 335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550356027 382 TEIFGPVLSVVRARNYEEALslpmkhEYGN------GVAIYTRDGDAARDFASRINIGMVGVN 438
Cdd:cd07134 336 EEIFGPVLPIITYEDLDEVI------EYINakpkplALYVFSKDKANVNKVLARTSSGGVVVN 392
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
136-478 |
8.20e-27 |
|
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: 112.50 E-value: 8.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 136 IRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELmIEAGLPAGILNVVNGDKGAVDAILTH 215
Cdd:cd07137 98 VSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYLDTKAIKVIEGGVPETTALLEQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 216 P-DiaAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGS-AGERCMAISVaVPVGEE 293
Cdd:cd07137 177 KwD--KIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDY-VLVEES 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 294 TANRLIDKLVPMVESLrIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQgAKLVVDG-RDfklqgyENGHFIGGCLFDD 372
Cdd:cd07137 254 FAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVA-DKIVHGGeRD------EKNLYIEPTILLD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 373 VTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIpVPLAYHS--F 450
Cdd:cd07137 326 PPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTV-VQYAIDTlpF 404
|
330 340
....*....|....*....|....*...
gi 1550356027 451 GGWKSSSFGdlNQHGTDSIKFWTRTKTI 478
Cdd:cd07137 405 GGVGESGFG--AYHGKFSFDAFSHKKAV 430
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
65-438 |
2.13e-26 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 112.04 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 65 RARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAK-GDIVRGLEVCEFVIGipHLQK-----SEFTEGA-GPGiDMYSIR 137
Cdd:PTZ00381 31 RKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmTEVLLTVAEIEHLLK--HLDEylkpeKVDTVGVfGPG-KSYIIP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 138 QPVGIGAGITPFNFP---GMIPMwmfAPAIACGNAFILKPSERDPSVPIRLAELmIEAGLPAGILNVVNGDKGAVDAILT 214
Cdd:PTZ00381 108 EPLGVVLVIGAWNYPlnlTLIPL---AGAIAAGNTVVLKPSELSPHTSKLMAKL-LTKYLDPSYVRVIEGGVEVTTELLK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 215 HP-DIaaVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAIS-VAVPvge 292
Cdd:PTZ00381 184 EPfDH--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDyVLVH--- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 293 etaNRLIDKLVPMVESLRI---GPYTDEKADMGPVVTKEAEQRIRSLIDsgiEQGAKLVVDGrdfklQGYENGHFIGGCL 369
Cdd:PTZ00381 259 ---RSIKDKFIEALKEAIKeffGEDPKKSEDYSRIVNEFHTKRLAELIK---DHGGKVVYGG-----EVDIENKYVAPTI 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550356027 370 FDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVN 438
Cdd:PTZ00381 328 IVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN 396
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
134-481 |
1.29e-23 |
|
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: 103.35 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 134 YSIRQPVGIGAGITPFNFPGMIpmwMFAP---AIACGNAFILKPSERDPSVPIRLAElMIEAGLPAGILNVVNGDKGAVD 210
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQL---ALAPligAIAAGNTAVLKPSELTPNTSKVIAK-IIEETFDEEYVAVVEGGVEENQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 211 AILTHP-DiaAVSFVGSTPIARYVYGTAAMN---------GKraqcfggakNHMIIMPDADLDQAANALIGAGYGSAGER 280
Cdd:cd07136 171 ELLDQKfD--YIFFTGSVRVGKIVMEAAAKHltpvtlelgGK---------SPCIVDEDANLKLAAKRIVWGKFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 281 CMAisvavP----VGEETANRLIDKLVPMVESLrIGPYTDEKADMGPVVTKEAEQRIRSLIDSGieqgaKLVVDGrdfkl 356
Cdd:cd07136 240 CVA-----PdyvlVHESVKEKFIKELKEEIKKF-YGEDPLESPDYGRIINEKHFDRLAGLLDNG-----KIVFGG----- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 357 QGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEygNGVAIY--TRDGDAARDFASRINIGM 434
Cdd:cd07136 304 NTDRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRP--KPLALYlfSEDKKVEKKVLENLSFGG 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1550356027 435 VGVNVPIpVPLA--YHSFGGWKSSSFGdlNQHGTDSIKFWTRTKTITSR 481
Cdd:cd07136 382 GCINDTI-MHLAnpYLPFGGVGNSGMG--SYHGKYSFDTFSHKKSILKK 427
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
136-402 |
8.30e-23 |
|
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: 100.64 E-value: 8.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 136 IRQP---VGIgagITPFNFPGMIpmwMFAP---AIACGNAFILKPSERDPsvpiRLAELMIE---AGLPAGILNVVNGDk 206
Cdd:cd07133 98 EYQPlgvVGI---IVPWNYPLYL---ALGPliaALAAGNRVMIKPSEFTP----RTSALLAEllaEYFDEDEVAVVTGG- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 207 gavdailthPDIA-AVS--------FVGSTPIARYVYGTAAMN---------GKraqcfggakNHMIIMPDADLDQAANA 268
Cdd:cd07133 167 ---------ADVAaAFSslpfdhllFTGSTAVGRHVMRAAAENltpvtlelgGK---------SPAIIAPDADLAKAAER 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 269 LIGAGYGSAGERCMAIS-VAVPvgEETANRLIDKLVPMVESLrigpYTDEKA--DMGPVVTKEAEQRIRSLIDSGIEQGA 345
Cdd:cd07133 229 IAFGKLLNAGQTCVAPDyVLVP--EDKLEEFVAAAKAAVAKM----YPTLADnpDYTSIINERHYARLQGLLEDARAKGA 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 346 KLV---VDGRDFklqgyENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALS 402
Cdd:cd07133 303 RVIelnPAGEDF-----AATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAID 357
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
1-427 |
1.97e-21 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 97.08 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 1 MYELGHFIDGKRVAGtSGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNM 80
Cdd:PRK11903 2 TELLANYVAGRWQAG-SGAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 81 NELAEMLSREHGKTIDDAKGDIVRGLevceFVIG-----------IPHLQKSEFTE-GAGPGIDMYSIRQPV-GIGAGIT 147
Cdd:PRK11903 81 DAYYDIATANSGTTRNDSAVDIDGGI----FTLGyyaklgaalgdARLLRDGEAVQlGKDPAFQGQHVLVPTrGVALFIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 148 PFNFPGMiPMW-MFAPAIACGNAFILKPSERDPSVPIRLAELMIEAG-LPAGILNVVNGDKGAVDAILTHPDIaaVSFVG 225
Cdd:PRK11903 157 AFNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSAGLLDHLQPFDV--VSFTG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 226 STPIARYVYGTAAM--NGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYG-----SAGERCMAIS-VAVPvgEETANR 297
Cdd:PRK11903 234 SAETAAVLRSHPAVvqRSVRVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVremtvKSGQKCTAIRrIFVP--EALYDA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 298 LIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDsGIEQGAKLVVDGRDFKLQGYEN--GHFIGGCLFddVTP 375
Cdd:PRK11903 312 VAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVDADPavAACVGPTLL--GAS 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1550356027 376 DMD----IYKTEIFGPVLSVVRARNYEEALSLPMKHEyGNGVA-IYTRDGDAARDFA 427
Cdd:PRK11903 389 DPDaataVHDVEVFGPVATLLPYRDAAHALALARRGQ-GSLVAsVYSDDAAFLAAAA 444
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
136-481 |
1.17e-18 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 88.56 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 136 IRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMiEAGLPAGILNVVNGDKGAVDAILTH 215
Cdd:PLN02174 109 VSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 216 pDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYG-SAGERCMAISVAVPVgEET 294
Cdd:PLN02174 188 -KWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT-KEY 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 295 ANRLIDKLVPMVESLrIGPYTDEKADMGPVVTKEAEQRIRSLIDSGiEQGAKLVVDGRdfklQGYENGHfIGGCLFDDVT 374
Cdd:PLN02174 266 APKVIDAMKKELETF-YGKNPMESKDMSRIVNSTHFDRLSKLLDEK-EVSDKIVYGGE----KDRENLK-IAPTILLDVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 375 PDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNvPIPVPLAYHS--FGG 452
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVN-DIAVHLALHTlpFGG 417
|
330 340
....*....|....*....|....*....
gi 1550356027 453 WKSSSFGDLnqHGTDSIKFWTRTKTITSR 481
Cdd:PLN02174 418 VGESGMGAY--HGKFSFDAFSHKKAVLYR 444
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
7-427 |
1.80e-16 |
|
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: 81.93 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 7 FIDGKRVAGTsGRVSNIFNPATGEVQGTVALASDADLAAAVESAKAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEm 86
Cdd:cd07128 4 YVAGQWHAGT-GDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLYA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 87 LSREHGKTIDDAKGDI--------------VRGLEVCEFVIGIPHLQKSEftEGAGPGIDMYSIRQpvGIGAGITPFNFP 152
Cdd:cd07128 82 LSAATGATRRDSWIDIdggigtlfayaslgRRELPNAHFLVEGDVEPLSK--DGTFVGQHILTPRR--GVAVHINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 153 --GMipMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAG-LPAGILNVVNGDKGAVDAILTHPDIaaVSFVGSTPI 229
Cdd:cd07128 158 vwGM--LEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQDV--VAFTGSAAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 230 ARYVYGTAAMNGKRAQCFGGAK--NHMIIMPDADLDQAANALIGAGY-----GSAGERCMAI-SVAVPVGEETAnrLIDK 301
Cdd:cd07128 234 AAKLRAHPNIVARSIRFNAEADslNAAILGPDATPGTPEFDLFVKEVaremtVKAGQKCTAIrRAFVPEARVDA--VIEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 302 LVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSgIEQGAKLVVDGRD-FKLQG--YENGHFIGGCLF--DDVTPD 376
Cdd:cd07128 312 LKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDrFEVVGadAEKGAFFPPTLLlcDDPDAA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1550356027 377 MDIYKTEIFGPVLSVVRARNYEEALSLPMKheyGNG--VA-IYTRDGDAARDFA 427
Cdd:cd07128 391 TAVHDVEAFGPVATLMPYDSLAEAIELAAR---GRGslVAsVVTNDPAFARELV 441
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
71-468 |
4.33e-16 |
|
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: 80.34 E-value: 4.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 71 KFVQLLNDNMNELAEMLSREHGKT--------IDDAKGDIVRGLEvcefvigipHLQ---KSEFTEGAGPGI--DMYSIR 137
Cdd:cd07132 28 ALLRMLEENEDEIVEALAKDLRKPkfeavlseILLVKNEIKYAIS---------NLPewmKPEPVKKNLATLldDVYIYK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 138 QPVGIGAGITPFNFPGMIpmwMFAP---AIACGNAFILKPSERDPSVPIRLAELmieagLPAGILN----VVNGD----- 205
Cdd:cd07132 99 EPLGVVLIIGAWNYPLQL---TLVPlvgAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLDKecypVVLGGveett 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 206 ---KGAVDAILthpdiaavsFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCM 282
Cdd:cd07132 171 ellKQRFDYIF---------YTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 283 AISVaVPVGEETANRLIDKLVPMVESLrigpYTD---EKADMGPVVTKEAEQRIRSLIDSGieqgaKLVVDGrdfklQGY 359
Cdd:cd07132 242 APDY-VLCTPEVQEKFVEALKKTLKEF----YGEdpkESPDYGRIINDRHFQRLKKLLSGG-----KVAIGG-----QTD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 360 ENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNV 439
Cdd:cd07132 307 EKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVND 386
|
410 420 430
....*....|....*....|....*....|.
gi 1550356027 440 PIpVPLAYHS--FGGWKSSSFGdlNQHGTDS 468
Cdd:cd07132 387 TI-MHYTLDSlpFGGVGNSGMG--AYHGKYS 414
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
138-481 |
4.66e-16 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 80.54 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 138 QPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAElMIEAGLPAGILNVVNGDKGAVDAILTHP- 216
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAA-NIPKYLDSKAVKVIEGGPAVGEQLLQHKw 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 217 DiaAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMI---IMPDADLDQAANALIGAGYGS-AGERCMAISVaVPVGE 292
Cdd:PLN02203 186 D--KIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDY-VLVEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 293 ETANRLIDKLVPMVESLrIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAklVVDGRDFKlqgyENGHFIGGCLFDD 372
Cdd:PLN02203 263 RFAPILIELLKSTIKKF-FGENPRESKSMARILNKKHFQRLSNLLKDPRVAAS--IVHGGSID----EKKLFIEPTILLN 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 373 VTPDMDIYKTEIFGPVLSVVRARNYEEALslpmkhEYGNG----VAIY--TRDGDAARDFASRINIGMVGVNVPIpVPLA 446
Cdd:PLN02203 336 PPLDSDIMTEEIFGPLLPIITVKKIEDSI------AFINSkpkpLAIYafTNNEKLKRRILSETSSGSVTFNDAI-IQYA 408
|
330 340 350
....*....|....*....|....*....|....*..
gi 1550356027 447 YHS--FGGWKSSSFGdlNQHGTDSIKFWTRTKTITSR 481
Cdd:PLN02203 409 CDSlpFGGVGESGFG--RYHGKYSFDTFSHEKAVLRR 443
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
61-403 |
1.74e-12 |
|
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: 69.45 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 61 NPQRR---ARVFMKFVQLLNDNMNE--LAEMLSREHGKTIDDAKGDIVRGLEVCEFVIG--IPHLQKSEFTEGAGPGIDM 133
Cdd:cd07126 57 NPERYllyGDVSHRVAHELRKPEVEdfFARLIQRVAPKSDAQALGEVVVTRKFLENFAGdqVRFLARSFNVPGDHQGQQS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 134 YSIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAIL 213
Cdd:cd07126 137 SGYRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKIL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 214 THPDIAAVSFVGSTPIARYVygTAAMNGKrAQCFGGAKNHMIIMPD-ADLDQAANALIGAGYGSAGERCMAISVAVPVGE 292
Cdd:cd07126 217 LEANPRMTLFTGSSKVAERL--ALELHGK-VKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHEN 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 293 ETANRLIDKLVPMVESLRIGPYTdekadMGPVVTKEAeQRIRSLIDSGIE-QGAKLVVDGRDFKlqgyenGHFIGGClFD 371
Cdd:cd07126 294 WVQAGILDKLKALAEQRKLEDLT-----IGPVLTWTT-ERILDHVDKLLAiPGAKVLFGGKPLT------NHSIPSI-YG 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1550356027 372 DVTP--------------DMDIYKTEIFGPVLSVVRARNYEEALSL 403
Cdd:cd07126 361 AYEPtavfvpleeiaieeNFELVTTEVFGPFQVVTEYKDEQLPLVL 406
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
54-459 |
1.15e-11 |
|
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: 66.52 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 54 QPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKgdIVRGLEVCEfviGIPHLQKSEFTEGAGPGIDM 133
Cdd:cd07081 12 QQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDK--VIKNHFAAE---YIYNVYKDEKTCGVLTGDEN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 134 Y---SIRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAG-----ILNVVNGD 205
Cdd:cd07081 87 GgtlIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGapenlIGWIDNPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 206 KGAVDAILTHPDIAAVSFVGSTPIARYVYGtaamNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCmAIS 285
Cdd:cd07081 167 IELAQRLMKFPGIGLLLATGGPAVVKAAYS----SGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVIC-ASE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 286 VAVPVGEETANRLIDKLvpmveslrigpytdeKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVvdGRDfklqGYENGHFI 365
Cdd:cd07081 242 QSVIVVDSVYDEVMRLF---------------EGQGAYKLTAEELQQVQPVILKNGDVNRDIV--GQD----AYKIAAAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 366 G-------GCLFDDVTP--DMDIYKTEIFGPVLSVVRARNYEEAL--SLPMKHEYGNG--VAIYTRDgDAARD----FAS 428
Cdd:cd07081 301 GlkvpqetRILIGEVTSlaEHEPFAHEKLSPVLAMYRAANFADADakALALKLEGGCGhtSAMYSDN-IKAIEnmnqFAN 379
|
410 420 430
....*....|....*....|....*....|....
gi 1550356027 429 RINIGMVGVNVPIPVP---LAYhSFGGWKSSSFG 459
Cdd:cd07081 380 AMKTSRFVKNGPCSQGglgDLY-NFRGWPSMTLG 412
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
58-465 |
1.47e-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: 66.09 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 58 AATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTI--------------DDAKGDIVRGLEvcefviGIPHLQKSEF 123
Cdd:cd07077 11 AVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIrslianwiammgcsESKLYKNIDTER------GITASVGHIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 124 TEGAGPGIDMYSIRQPVGIGAGITPFNFPGMIPMwMFAPAIACGNAFILKPSERDPsVPIRLAELMIEAGLPAG-----I 198
Cdd:cd07077 85 DVLLPDNGETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHgpkilV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 199 LNVVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAamNGKRAQCFGGAKNHMIIMPDADLDQAAN-ALIGAGYGSA 277
Cdd:cd07077 163 LYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHS--PHIPVIGFGAGNSPVVVDETADEERASGsVHDSKFFDQN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 278 GerCMAISVAVpvgeetanrlidklvpmveslrigpytdekadmgpVVTKEAEQRIRSLIDSGIEQGAKLvvdgrdfklq 357
Cdd:cd07077 241 A--CASEQNLY-----------------------------------VVDDVLDPLYEEFKLKLVVEGLKV---------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 358 gYENGHFiggcLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEAL--SLPMKHEYGNGV--AIYTRDGDAARDFASRINIG 433
Cdd:cd07077 274 -PQETKP----LSKETTPSFDDEALESMTPLECQFRVLDVISAVenAWMIIESGGGPHtrCVYTHKINKVDDFVQYIDTA 348
|
410 420 430
....*....|....*....|....*....|...
gi 1550356027 434 MVGVNVP-IPVPLAYHSFGGWKSSSFGDLNQHG 465
Cdd:cd07077 349 SFYPNESsKKGRGAFAGKGVERIVTSGMNNIFG 381
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
136-452 |
3.43e-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: 58.66 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 136 IRQPVGIGAGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELM----IEAGLPAGILNVV-NGDKGAVD 210
Cdd:cd07122 92 IAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMreaaVAAGAPEGLIQWIeEPSIELTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 211 AILTHPDIAAVSFVGSTPIARYVYGTaamnGKRAQCfGGAKN-HMIIMPDADLDQAANALIGA-----GYGSAGERcmai 284
Cdd:cd07122 172 ELMKHPDVDLILATGGPGMVKAAYSS----GKPAIG-VGPGNvPAYIDETADIKRAVKDIILSktfdnGTICASEQ---- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 285 svAVPVGEETANRLIDKLVpmveslRIGPYtdekadmgpVVTKEAEQRIRSLIdsgIEQGAKLVVD--GRD--------- 353
Cdd:cd07122 243 --SVIVDDEIYDEVRAELK------RRGAY---------FLNEEEKEKLEKAL---FDDGGTLNPDivGKSaqkiaelag 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 354 FKLQgyENGHFIGGcLFDDVTPDmDIYKTEIFGPVLSVVRARNYEEALSLPMK--HEYGNG--VAIYTRDGDAARDFASR 429
Cdd:cd07122 303 IEVP--EDTKVLVA-EETGVGPE-EPLSREKLSPVLAFYRAEDFEEALEKAREllEYGGAGhtAVIHSNDEEVIEEFALR 378
|
330 340
....*....|....*....|...
gi 1550356027 430 INIGMVGVNVPipvplayHSFGG 452
Cdd:cd07122 379 MPVSRILVNTP-------SSLGG 394
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
128-403 |
5.18e-09 |
|
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: 58.32 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 128 GPGIDMYSIRQPVGIGAGITPFNFP-------GMipmwmFAPAIACGNAFILKPSERDPSVPIRLAELMIEA----GLPA 196
Cdd:cd07129 94 LPRPDLRRMLVPLGPVAVFGASNFPlafsvagGD-----TASALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLPA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 197 GILNVVNGDKGAV-DAILTHPDIAAVSFVGSTPIARYVYGTAAmngKRAQ---CFG--GAKNHMIIMPDA---DLDQAAN 267
Cdd:cd07129 169 GVFSLLQGGGREVgVALVKHPAIKAVGFTGSRRGGRALFDAAA---ARPEpipFYAelGSVNPVFILPGAlaeRGEAIAQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 268 ALIGAGYGSAGERCMAISVAVPVGEETANRLIDKLVPMVeslrigpytdEKADMGPVVTkeaeQRIRSLIDSGIEQ---- 343
Cdd:cd07129 246 GFVGSLTLGAGQFCTNPGLVLVPAGPAGDAFIAALAEAL----------AAAPAQTMLT----PGIAEAYRQGVEAlaaa 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1550356027 344 -GAKLVVDGRDfKLQGYENGHFIGGCLFDDVTPDmDIYKTEIFGPVLSVVRARNYEEALSL 403
Cdd:cd07129 312 pGVRVLAGGAA-AEGGNQAAPTLFKVDAAAFLAD-PALQEEVFGPASLVVRYDDAAELLAV 370
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
52-411 |
6.88e-07 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 51.44 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 52 AAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKgdIVRGLEVCEFVIGIPHLQKSEFTEGAGPGI 131
Cdd:PRK15398 47 VAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDK--IAKNVAAAEKTPGVEDLTTEALTGDNGLTL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 132 DMYSirqPVGIGAGITPFNFPG------MIPMwmfapaIACGNAFILKPSERDPSVPIRLAELM----IEAGLPAGILNV 201
Cdd:PRK15398 125 IEYA---PFGVIGAVTPSTNPTetiinnAISM------LAAGNSVVFSPHPGAKKVSLRAIELLneaiVAAGGPENLVVT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 202 V-NGDKGAVDAILTHPDIAAVSFVGSTPIARyvygtAAMN-GKRAQCfGGAKNHMIIMPD-ADLDQAANALI-GAGYGS- 276
Cdd:PRK15398 196 VaEPTIETAQRLMKHPGIALLVVTGGPAVVK-----AAMKsGKKAIG-AGAGNPPVVVDEtADIEKAARDIVkGASFDNn 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 277 ---AGERCMaisVAVpvgEETANRLIDKLVpmveslRIGPYtdekadmgpVVTKEAEQRIRSL-IDSGIEQGAKLVvdGR 352
Cdd:PRK15398 270 lpcIAEKEV---IVV---DSVADELMRLME------KNGAV---------LLTAEQAEKLQKVvLKNGGTVNKKWV--GK 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550356027 353 D--FKLQGyenghfIGG-------CLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGN 411
Cdd:PRK15398 327 DaaKILEA------AGInvpkdtrLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGN 388
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
52-431 |
1.13e-06 |
|
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: 50.70 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 52 AAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKgdIVRGLEVCEFVIGIPHLQKSEFTEGAGPGI 131
Cdd:cd07121 15 AAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDK--IAKNHLAAEKTPGTEDLTTTAWSGDNGLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 132 DMYSirqPVGIGAGITPFNFPG------MIPMwmfapaIACGNAFILKPSERDPSVPIRLAELM----IEAGLPAGILNV 201
Cdd:cd07121 93 VEYA---PFGVIGAITPSTNPTetiinnSISM------LAAGNAVVFNPHPGAKKVSAYAVELInkaiAEAGGPDNLVVT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 202 V-NGDKGAVDAILTHPDIAAVSFVGSTPIARyvygtAAMN-GKRAQCfGGAKNHMIIMPD-ADLDQAANALI-GAGYGS- 276
Cdd:cd07121 164 VeEPTIETTNELMAHPDINLLVVTGGPAVVK-----AALSsGKKAIG-AGAGNPPVVVDEtADIEKAARDIVqGASFDNn 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 277 ---AGERcmaisvAVPVGEETANRLIDKLVpmveslRIGPYtdekadmgpVVT-KEAEQRIRSLI--DSGIEQGAKLVvd 350
Cdd:cd07121 238 lpcIAEK------EVIAVDSVADYLIAAMQ------RNGAY---------VLNdEQAEQLLEVVLltNKGATPNKKWV-- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 351 GRDFKLQGYENGHFIGG---CLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGN--GVAIYTRDGDAARD 425
Cdd:cd07121 295 GKDASKILKAAGIEVPAdirLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTK 374
|
....*.
gi 1550356027 426 FASRIN 431
Cdd:cd07121 375 MARAMQ 380
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
134-269 |
1.57e-06 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 50.52 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 134 YSIRQPVGIGAGITPFNFPGmIPMWMFAPAIACGNAFILKPSERDPSVPIRLAE--LMIEAGLP-AGILNVVNGDKGAV- 209
Cdd:pfam05893 83 YEKAFPPGLVFHVLSGNVPL-LPVMSILMGLLVKNVNLLKVSSSDPFTAAALLAsfADLDPTHPlADSLSVVYWDGGSTq 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1550356027 210 --DAILTHPDiaAVSFVGSTPIARYVYGTAAmNGKRAQCFGGAKNHMIIMPDADLDQAANAL 269
Cdd:pfam05893 162 leDLIVANAD--VVIAWGGEDAINAIRECLK-PGKQWIDFGAKISFAVVDREAALDKAAERA 220
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
129-191 |
1.45e-03 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 41.11 E-value: 1.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550356027 129 PGIDMYSIRQPVGIGAGITPFNFPGmIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIE 191
Cdd:cd07080 102 PGRGGYIRAQPRGLVVHIIAGNVPL-LPVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLAD 163
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
57-452 |
1.51e-03 |
|
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: 41.19 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 57 WAATNPQRRARvfMKFVQLLNDNMNELAEMLSREHGKTIDDAKGDIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSI 136
Cdd:COG0506 544 AAAAAAAAAAA--AAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGLVALLP 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 137 RQPVGIG-AGITPFNFPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILNVVNGDKGAVDAILTH 215
Cdd:COG0506 622 LGPLAAAaAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTL 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 216 PDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGAKNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVPVGEETA 295
Cdd:COG0506 702 AAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLLSLLALLLLDA 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550356027 296 NRLIDKLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVdgrdFKLQGYENGHFIGGCLFDDVTP 375
Cdd:COG0506 782 DLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELL----LPGGGPLVPGLLTAPLLVALIL 857
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1550356027 376 DMDIYKTEIFGPVLSVVRARNYEEALSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSFGG 452
Cdd:COG0506 858 GLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGG 934
|
|
| |
