|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
32-513 |
0e+00 |
|
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: 581.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 32 YLVDGELLRWQGKTEPVHSammasengllaPLH---LGSCPVLDENAAMRAAkaaVDAYGRGLGEWPAMTQGERIRHLEC 108
Cdd:cd07082 4 YLINGEWKESSGKTIEVYS-----------PIDgevIGSVPALSALEILEAA---ETAYDAGRGWWPTMPLEERIDCLHK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 109 FLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEDSR---RFEGDDILARVRRAPLGPVLCMG 185
Cdd:cd07082 70 FADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPgdwFPGTKGKIAQVRREPLGVVLAIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 186 PYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRD-CFPRGVVNVITG-NTELVHPILKSGCVDVFAFIGS 263
Cdd:cd07082 150 PFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDaGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 264 SGAASALRELHPRpgrLRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGV 343
Cdd:cd07082 230 TEVGNRLKKQHPM---KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 344 GKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINADGGSVlGSLVHPAILYPVDSSMRVYHEEQFGPVVPV 423
Cdd:cd07082 307 AKLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG-GNLIYPTLLDPVTPDMRLAWEEPFGPVLPI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 424 VPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMsaQVCRVNLNSQCQRGPDTLPFGGRKDSAVGTLSVKDGIRA 503
Cdd:cd07082 386 IRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADAL--EVGTVNINSKCQRGPDHFPFLGRKDSGIGTQGIGDALRS 463
|
490
....*....|
gi 648475632 504 FSMRTVVASK 513
Cdd:cd07082 464 MTRRKGIVIN 473
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
84-513 |
3.31e-122 |
|
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: 367.53 E-value: 3.31e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEdSRR 163
Cdd:COG1012 49 VAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGE-TIP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 FEGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC-FPRGVVNVITGN 242
Cdd:COG1012 128 SDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 243 T-ELVHPILKSGCVDVFAFIGSSGAASALRELHPRPGRlRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTA 321
Cdd:COG1012 208 GsEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLK-RVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 322 IKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVL----GSLV 397
Cdd:COG1012 287 ASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLT--GGRRPdgegGYFV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 398 HPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMsaQVCRVNLNSQCQR 477
Cdd:COG1012 365 EPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRL--EAGMVWINDGTTG 442
|
410 420 430
....*....|....*....|....*....|....*.
gi 648475632 478 GPDTLPFGGRKDSAVGTLSVKDGIRAFSMRTVVASK 513
Cdd:COG1012 443 AVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
84-509 |
2.22e-99 |
|
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: 308.31 E-value: 2.22e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEdsRR 163
Cdd:pfam00171 35 IAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLARRLDGE--TL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 FEGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFspilEALRDC-FPRGVVNV 238
Cdd:pfam00171 113 PSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKpselTPLTALLLA----ELFEEAgLPAGVLNV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 239 ITGNT-ELVHPILKSGCVDVFAFIGSSGAAsalRELHPRPGRL--RCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFS 315
Cdd:pfam00171 189 VTGSGaEVGEALVEHPDVRKVSFTGSTAVG---RHIAEAAAQNlkRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 316 GQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVInADGGSVL-- 393
Cdd:pfam00171 266 GQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLL-TGGEAGLdn 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 394 GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVcrVNLNS 473
Cdd:pfam00171 345 GYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGM--VWIND 422
|
410 420 430
....*....|....*....|....*....|....*..
gi 648475632 474 QCQRGPDTLPFGGRKDSAVGTLSVKDGIRAFS-MRTV 509
Cdd:pfam00171 423 YTTGDADGLPFGGFKQSGFGREGGPYGLEEYTeVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
93-511 |
1.76e-97 |
|
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: 302.20 E-value: 1.76e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEdSRRFEGDDILAR 172
Cdd:cd07078 13 AWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGE-VIPSPDPGELAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 173 VRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKL----PKIGRLLFSPILEALrdcFPRGVVNVITGN-----T 243
Cdd:cd07078 92 VRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPseltPLTALLLAELLAEAG---LPPGVLNVVTGDgdevgA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 244 ELV-HPIlksgcVDVFAFIGSSGAASALRE-LHPRPGRLRCvfGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTA 321
Cdd:cd07078 169 ALAsHPR-----VDKISFTGSTAVGKAIMRaAAENLKRVTL--ELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 322 IKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVInaDGGSVL----GSLV 397
Cdd:cd07078 242 ASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLL--CGGKRLeggkGYFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 398 HPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNLNSqcQR 477
Cdd:cd07078 320 PPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS--VG 397
|
410 420 430
....*....|....*....|....*....|....*
gi 648475632 478 GPDTLPFGGRKDSAVGTLSVKDGIRAFS-MRTVVA 511
Cdd:cd07078 398 AEPSAPFGGVKQSGIGREGGPYGLEEYTePKTVTI 432
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
84-510 |
4.50e-73 |
|
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: 239.35 E-value: 4.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDalreMDGEDSRR 163
Cdd:cd07106 25 VAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTAS----LDLPDEVI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 FEGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKlPkigrllfSP--------ILEALRDCFPRGV 235
Cdd:cd07106 101 EDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLK-P-------SPftplctlkLGELAQEVLPPGV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 236 VNVITGNTEL-----VHPIlksgcVDVFAFIGSS--------GAASALR----ELhprpGrlrcvfGLDAknqAVVLQDA 298
Cdd:cd07106 173 LNVVSGGDELgpaltSHPD-----IRKISFTGSTatgkkvmaSAAKTLKrvtlEL----G------GNDA---AIVLPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 299 DMDVAAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAV 378
Cdd:cd07106 235 DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 379 SKGARVINadGGSVL---GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRL 455
Cdd:cd07106 315 AKGAKVLA--GGEPLdgpGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 648475632 456 GRLVDAMSAQvcRVNLNSQCQRGPDTlPFGGRKDSAVGTLSVKDGIRAFSMRTVV 510
Cdd:cd07106 393 EAVARRLEAG--TVWINTHGALDPDA-PFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
94-505 |
9.48e-72 |
|
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: 236.09 E-value: 9.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 94 WPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEdSRRFEGDDILAR- 172
Cdd:cd07145 37 MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAKVLRGE-TIPVDAYEYNERr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 173 ---VRRAPLGPVLCMGPYNFPFNeTFATLI-PALLMGNTAVVKLPK---IGRLLFSPILEalRDCFPRGVVNVITGNTEL 245
Cdd:cd07145 116 iafTVREPIGVVGAITPFNFPAN-LFAHKIaPAIAVGNSVVVKPSSntpLTAIELAKILE--EAGLPPGVINVVTGYGSE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 246 V-HPILKSGCVDVFAFIGSSGAASALRELHPRPGRlRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKT 324
Cdd:cd07145 193 VgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGK-KVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 325 VFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINAdGGSVLGSLVHPAILYP 404
Cdd:cd07145 272 ILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGGKILYG-GKRDEGSFFPPTVLEN 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 405 VDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVcrVNLNSQCQRGPDTLPF 484
Cdd:cd07145 351 DTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGG--VVINDSTRFRWDNLPF 428
|
410 420
....*....|....*....|.
gi 648475632 485 GGRKDSAVGTLSVKDGIRAFS 505
Cdd:cd07145 429 GGFKKSGIGREGVRYTMLEMT 449
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
93-511 |
1.57e-70 |
|
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: 230.19 E-value: 1.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEDSRRfEGDDILAR 172
Cdd:cd06534 9 AWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPS-PDPGGEAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 173 VRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEALrdcFPRGVVNVITGN-TELVH 247
Cdd:cd06534 88 VRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKpselTPLTALALAELLQEAG---LPPGVVNVVPGGgDEVGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 248 PILKSGCVDVFAFIGSSGAASALRE-LHPRPGRLRCVfgLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTVF 326
Cdd:cd06534 165 ALLSHPRVDKISFTGSTAVGKAIMKaAAENLKPVTLE--LGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 327 VHQSRADELLERLKagvgklkigmpfdpdvditpmpepgraeylrdlvddavskgarvinadggsvlgslvhpAILYPVD 406
Cdd:cd06534 243 VHESIYDEFVEKLV-----------------------------------------------------------TVLVDVD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 407 SSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMsaQVCRVNLNSQCQRGPDTLPFGG 486
Cdd:cd06534 264 PDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERL--RAGTVYINDSSIGVGPEAPFGG 341
|
410 420
....*....|....*....|....*.
gi 648475632 487 RKDSAVGTLSVKDGIRAFS-MRTVVA 511
Cdd:cd06534 342 VKNSGIGREGGPYGLEEYTrTKTVVI 367
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
93-505 |
8.36e-68 |
|
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: 225.56 E-value: 8.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQ----YVRDTIDALRemDGEDSRRFEGDD 168
Cdd:cd07099 33 AWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEaidwAARNAPRVLA--PRKVPTGLLMPN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 169 ILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEALrdcFPRGVVNVITGNTE 244
Cdd:cd07099 111 KKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKpsevTPLVGELLAEAWAAAG---PPQGVLQVVTGDGA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 245 LVHPILKSGcVDVFAFIGSSG-----AASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRC 319
Cdd:cd07099 188 TGAALIDAG-VDKVAFTGSVAtgrkvMAAAAERLIP------VVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 320 TAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVinADGGSVL---GSL 396
Cdd:cd07099 261 ISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKA--LTGGARSnggGPF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 397 VHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVcrVNLNSQCQ 476
Cdd:cd07099 339 YEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGA--VSINDVLL 416
|
410 420 430
....*....|....*....|....*....|.
gi 648475632 477 RG--PDtLPFGGRKDSAVGTLSVKDGIRAFS 505
Cdd:cd07099 417 TAgiPA-LPFGGVKDSGGGRRHGAEGLREFC 446
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
93-493 |
1.48e-67 |
|
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: 224.33 E-value: 1.48e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEDSRRfEGDDILAR 172
Cdd:cd07104 15 AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPS-DVPGKESM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 173 VRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEALRdcFPRGVVNVITGNTELV-- 246
Cdd:cd07104 94 VRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKpdsrTPVTGGLLIAEIFEEAG--LPKGVLNVVPGGGSEIgd 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 247 ----HPIlksgcVDVFAFIGSSGAAsalRELHPRPGRL--RCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCT 320
Cdd:cd07104 172 alveHPR-----VRMISFTGSTAVG---RHIGELAGRHlkKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 321 AIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVLGSLVHPA 400
Cdd:cd07104 244 AAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLT--GGTYEGLFYQPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 401 ILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVN---LNSQCQr 477
Cdd:cd07104 322 VLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINdqtVNDEPH- 400
|
410
....*....|....*.
gi 648475632 478 gpdtLPFGGRKDSAVG 493
Cdd:cd07104 401 ----VPFGGVKASGGG 412
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
96-507 |
3.82e-66 |
|
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: 221.32 E-value: 3.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 96 AMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGE----DSRRFeGDDILA 171
Cdd:cd07149 39 SLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEAKRLAGEtipfDASPG-GEGRIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 172 RVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKlP---------KIGRLLFspilEAlrdCFPRGVVNVITGN 242
Cdd:cd07149 118 FTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK-PasqtplsalKLAELLL----EA---GLPKGALNVVTGS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 243 TELVHP-ILKSGCVDVFAFIGSSGAASALRElhpRPGRLRCVFGLdAKNQAV-VLQDADMDVAAPEILSGSLSFSGQRCT 320
Cdd:cd07149 190 GETVGDaLVTDPRVRMISFTGSPAVGEAIAR---KAGLKKVTLEL-GSNAAViVDADADLEKAVERCVSGAFANAGQVCI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 321 AIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVLGSLVHPA 400
Cdd:cd07149 266 SVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLT--GGKRDGAILEPT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 401 ILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNpdrlgrLVDAMSA----QVCRVNLNSQCQ 476
Cdd:cd07149 344 VLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTND------LQKALKAarelEVGGVMINDSST 417
|
410 420 430
....*....|....*....|....*....|.
gi 648475632 477 RGPDTLPFGGRKDSAVGtlsvKDGIRaFSMR 507
Cdd:cd07149 418 FRVDHMPYGGVKESGTG----REGPR-YAIE 443
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
101-498 |
4.68e-66 |
|
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: 220.97 E-value: 4.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 101 ERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVqyvrDTIDAlremDGEDSRRFEGD----DILAR---- 172
Cdd:cd07147 44 RRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAI----DTFRI----AAEEATRIYGEvlplDISARgegr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 173 ---VRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK---LPKIGRLLFSPILeaLRDCFPRGVVNVITGNTELV 246
Cdd:cd07147 116 qglVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKpasRTPLSALILGEVL--AETGLPKGAFSVLPCSRDDA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 247 HPILKSGCVDVFAFIGSSGAASALRElhpRPGRLRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTVF 326
Cdd:cd07147 194 DLLVTDERIKLLSFTGSPAVGWDLKA---RAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 327 VHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVLGSLVHPAILYPVD 406
Cdd:cd07147 271 VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLT--GGKRDGALLEPTILEDVP 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 407 SSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMsaQVCRVNLNSQCQRGPDTLPFGG 486
Cdd:cd07147 349 PDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDEL--EVGGVVINDVPTFRVDHMPYGG 426
|
410
....*....|..
gi 648475632 487 RKDSAVGTLSVK 498
Cdd:cd07147 427 VKDSGIGREGVR 438
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
64-513 |
5.83e-66 |
|
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: 220.77 E-value: 5.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 64 HLGSCPVLDEnaamRAAKAAVDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTV 143
Cdd:cd07094 11 VIGKVPADDR----ADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 144 QYVRDTIDALREMDGE-----DSRRFEGDdiLARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRL 218
Cdd:cd07094 87 DTLRLAAEEAERIRGEeipldATQGSDNR--LAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 219 LFSPILEALRDC-FPRGVVNVITGNTELVHPILKSG-CVDVFAFIGSSGAASALRELHPRPgrlRCVFGLDAKNQAVVLQ 296
Cdd:cd07094 165 SALELAKILVEAgVPEGVLQVVTGEREVLGDAFAADeRVAMLSFTGSAAVGEALRANAGGK---RIALELGGNAPVIVDR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 297 DADMDVAAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDD 376
Cdd:cd07094 242 DADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 377 AVSKGARVINadGGSVLGSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQnpdRLG 456
Cdd:cd07094 322 AVEAGARLLC--GGERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR---DLN 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 648475632 457 RLVDAMSA-QVCRVNLNSQCQRGPDTLPFGGRKDSAVGtlsvKDGIRaFSMRTVVASK 513
Cdd:cd07094 397 VAFKAAEKlEVGGVMVNDSSAFRTDWMPFGGVKESGVG----REGVP-YAMEEMTEEK 449
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
84-493 |
3.00e-65 |
|
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: 219.12 E-value: 3.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEdSRR 163
Cdd:cd07150 27 IAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVRGE-TLP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 FEGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK---LPKIGRLLFSPILEALRdcFPRGVVNVIT 240
Cdd:cd07150 106 SDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKpseETPVIGLKIAEIMEEAG--LPKGVFNVVT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 241 GNTELV------HPIlksgcVDVFAFIGSSGAAsalRELHPRPGRL--RCVFGLDAKNQAVVLQDADMDVAAPEILSGSL 312
Cdd:cd07150 184 GGGAEVgdelvdDPR-----VRMVTFTGSTAVG---REIAEKAGRHlkKITLELGGKNPLIVLADADLDYAVRAAAFGAF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 313 SFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSV 392
Cdd:cd07150 256 MHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKGAKLLT--GGKY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 393 LGSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNLN 472
Cdd:cd07150 334 DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDP 413
|
410 420
....*....|....*....|.
gi 648475632 473 SqcQRGPDTLPFGGRKDSAVG 493
Cdd:cd07150 414 T--ILDEAHVPFGGVKASGFG 432
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
93-505 |
3.16e-65 |
|
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: 219.04 E-value: 3.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTID----ALREMDGEDSRRFEGdd 168
Cdd:cd07102 33 GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISiaeeALADIRVPEKDGFER-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 169 ilaRVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEALrdcFPRGVVNVITGNTE 244
Cdd:cd07102 111 ---YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKhspqTPLCGERFAAAFAEAG---LPEGVFQVLHLSHE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 245 LVHPILKSGCVDVFAFIGSSGAASALRElhPRPGRLRCVfGLD--AKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAI 322
Cdd:cd07102 185 TSAALIADPRIDHVSFTGSVAGGRAIQR--AAAGRFIKV-GLElgGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 323 KTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVI-------NADGGsvlGS 395
Cdd:cd07102 262 ERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALidgalfpEDKAG---GA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 396 LVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNlnsQC 475
Cdd:cd07102 339 YLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMN---RC 415
|
410 420 430
....*....|....*....|....*....|.
gi 648475632 476 QRGPDTLPFGGRKDSAVG-TLSvKDGIRAFS 505
Cdd:cd07102 416 DYLDPALAWTGVKDSGRGvTLS-RLGYDQLT 445
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
84-504 |
6.57e-62 |
|
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: 209.98 E-value: 6.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVrdtidalrEMDGEDSRR 163
Cdd:cd07103 25 IDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFL--------EWFAEEARR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 FEGDDILAR-------VRRAPLGPVLCMGPYNFPFNetfatLI-----PALLMGNTAVVKLPKIgrllfSP-----ILEA 226
Cdd:cd07103 97 IYGRTIPSPapgkrilVIKQPVGVVAAITPWNFPAA-----MItrkiaPALAAGCTVVLKPAEE-----TPlsalaLAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 227 LRDC-FPRGVVNVITGNT-ELVHPILKSGCVDVFAFIGSSG--------AASALRelhprpgrlRCVFGLDAKNQAVVLQ 296
Cdd:cd07103 167 AEEAgLPAGVLNVVTGSPaEIGEALCASPRVRKISFTGSTAvgkllmaqAADTVK---------RVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 297 DADMDVAAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDD 376
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 377 AVSKGARVINadGGSVL---GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPD 453
Cdd:cd07103 318 AVAKGAKVLT--GGKRLglgGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 648475632 454 RLGRLVDAMSAQVCRVN--LNSQCQrgpdtLPFGGRKDSAVGTLSVKDGIRAF 504
Cdd:cd07103 396 RAWRVAEALEAGMVGINtgLISDAE-----APFGGVKESGLGREGGKEGLEEY 443
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
101-512 |
1.15e-61 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 210.77 E-value: 1.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 101 ERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRT---VQY-VRDTIDALREMDGEDSRRFEGDD--ILARVR 174
Cdd:PLN00412 76 KRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSgdlISYtAEEGVRILGEGKFLVSDSFPGNErnKYCLTS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 175 RAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLlfSPILEAlrDCF-----PRGVVNVITGN-TEL--- 245
Cdd:PLN00412 156 KIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAV--AALHMV--HCFhlagfPKGLISCVTGKgSEIgdf 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 246 --VHPilksgCVDVFAFIGSSGAASALRELHPRPGRLRcvfgLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIK 323
Cdd:PLN00412 232 ltMHP-----GVNCISFTGGDTGIAISKKAGMVPLQME----LGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 324 TVFVHQSRADELLERLKAGVGKLKIGMPFDpDVDITPMPEPGRAEYLRDLVDDAVSKGARVINADGGSvlGSLVHPAILY 403
Cdd:PLN00412 303 VVLVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKRE--GNLIWPLLLD 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 404 PVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVcrVNLNSQCQRGPDTLP 483
Cdd:PLN00412 380 NVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGT--VQINSAPARGPDHFP 457
|
410 420
....*....|....*....|....*....
gi 648475632 484 FGGRKDSAVGTLSVKDGIrafSMRTVVAS 512
Cdd:PLN00412 458 FQGLKDSGIGSQGITNSI---NMMTKVKS 483
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
84-510 |
1.49e-61 |
|
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: 209.90 E-value: 1.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEW---PAMTQGERIRHLECFLERmvaEGDEIVRLMTLEICKPVRQARGEfdrtvqyVRDTIDALREMDGEd 160
Cdd:cd07131 43 VEAAREAFPEWrkvPAPRRAEYLFRAAELLKK---RKEELARLVTREMGKPLAEGRGD-------VQEAIDMAQYAAGE- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 161 SRRFEGD-------DILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC-FP 232
Cdd:cd07131 112 GRRLFGEtvpselpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 233 RGVVNVITGNTELV-HPILKSGCVDVFAFIGSSGAASALRELHPRPGRlRCVFGLDAKNQAVVLQDADMDVAAPEILSGS 311
Cdd:cd07131 192 PGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNK-RVALEMGGKNPIIVMDDADLDLALEGALWSA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 312 LSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVI----NA 387
Cdd:cd07131 271 FGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLlggeRL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 388 DGGSVL-GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQV 466
Cdd:cd07131 351 TGGGYEkGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGI 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 648475632 467 CRVNLNSQcqrGPDT-LPFGGRKDSAVGTLSVKDG-IRAFSMRTVV 510
Cdd:cd07131 431 TYVNAPTI---GAEVhLPFGGVKKSGNGHREAGTTaLDAFTEWKAV 473
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
84-511 |
1.54e-61 |
|
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: 209.41 E-value: 1.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWP-AMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRT-VQYVRDTIDALREMDGEDS 161
Cdd:cd07089 25 IAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGpIGHLRYFADLADSFPWEFD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 162 RRFEGDDILA---RVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEAlrdCFPRG 234
Cdd:cd07089 105 LPVPALRGGPgrrVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKpapdTPLSALLLGEIIAET---DLPAG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 235 VVNVITGNTELV------HPilksgCVDVFAFIGSSG--------AASALRelhprpgrlRCVFGLDAKNQAVVLQDADM 300
Cdd:cd07089 182 VVNVVTGSDNAVgealttDP-----RVDMVSFTGSTAvgrrimaqAAATLK---------RVLLELGGKSANIVLDDADL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 301 DVAAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSK 380
Cdd:cd07089 248 AAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 381 GARVINADG---GSVLGSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDR--- 454
Cdd:cd07089 328 GARLVTGGGrpaGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRayr 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 648475632 455 LGRLVDAMSaqvcrVNLNSQCQRGPDTlPFGGRKDSAVGTLSVKDGIRAFSMRTVVA 511
Cdd:cd07089 408 VARRIRTGS-----VGINGGGGYGPDA-PFGGYKQSGLGRENGIEGLEEFLETKSIA 458
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
95-502 |
3.47e-61 |
|
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: 208.37 E-value: 3.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 95 PAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEdSRRFE----GDDIL 170
Cdd:cd07146 35 STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRDDGE-SFSCDltanGKARK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 171 ARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC-FPRGVVNVITGN-TELVHP 248
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEpGEIGDE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 249 ILKSGCVDVFAFIGSSGAASALRELhprPGRLRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTVFVH 328
Cdd:cd07146 194 LITHPDVDLVTFTGGVAVGKAIAAT---AGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVH 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 329 QSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVLGSLVHPAILYPVDSS 408
Cdd:cd07146 271 ESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLL--GNQRQGALYAPTVLDHVPPD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 409 MRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMsaQVCRVNLNSQCQRGPDTLPFGGRK 488
Cdd:cd07146 349 AELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERL--DVGTVNVNEVPGFRSELSPFGGVK 426
|
410
....*....|....
gi 648475632 489 DSAVGtlsVKDGIR 502
Cdd:cd07146 427 DSGLG---GKEGVR 437
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
92-493 |
7.09e-61 |
|
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: 207.81 E-value: 7.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFD-RTVQYVRDTIDALREMDGEDSRR-FEGDDI 169
Cdd:cd07139 52 GPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRAQGpGPAALLRYYAALARDFPFEERRPgSGGGHV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 170 LarVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC-FPRGVVNVITGNTE---- 244
Cdd:cd07139 132 L--VRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPADREvgey 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 245 LV-HPilksgCVDVFAFIGSSGAASALRELHPRpgRL-RCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAI 322
Cdd:cd07139 210 LVrHP-----GVDKVSFTGSTAAGRRIAAVCGE--RLaRVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVAL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 323 KTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVinADGGSVL-----GSLV 397
Cdd:cd07139 283 TRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARL--VTGGGRPagldrGWFV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 398 HPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNlnsqcQR 477
Cdd:cd07139 361 EPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-----GF 435
|
410
....*....|....*..
gi 648475632 478 GPD-TLPFGGRKDSAVG 493
Cdd:cd07139 436 RLDfGAPFGGFKQSGIG 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
84-505 |
8.12e-60 |
|
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: 203.96 E-value: 8.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQArgEFDrtvqyVRDTIDALREMDGEDSRR 163
Cdd:cd07105 6 VEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWA--GFN-----VDLAAGMLREAASLITQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 FEG------DDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKigrllFSP-----ILEALRDC-F 231
Cdd:cd07105 79 IGGsipsdkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASE-----LSPrthwlIGRVFHEAgL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 232 PRGVVNVIT----GNTELVHPILKSGCVDVFAFIGSS--G---AASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDV 302
Cdd:cd07105 154 PKGVLNVVThspeDAPEVVEALIAHPAVRKVNFTGSTrvGriiAETAAKHLKP------VLLELGGKAPAIVLEDADLDA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 303 AAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLkigmpFDPDVDITPMPEPGRAEYLRDLVDDAVSKGA 382
Cdd:cd07105 228 AANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKL-----FAGPVVLGSLVSAAAADRVKELVDDALSKGA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 383 RVI--NADGGSVLGSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVD 460
Cdd:cd07105 303 KLVvgGLADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAK 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 648475632 461 AMSAQVCRVNlnsqcqrGPD-----TLPFGGRKDSAVGTLSVKDGIRAFS 505
Cdd:cd07105 383 RIESGAVHIN-------GMTvhdepTLPHGGVKSSGYGRFNGKWGIDEFT 425
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
101-504 |
1.35e-59 |
|
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: 203.46 E-value: 1.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 101 ERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVR---DTIDAL---REMDGEDSRrfegddilARVR 174
Cdd:cd07100 22 ERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRyyaENAEAFladEPIETDAGK--------AYVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 175 RAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLlfspILEALRDC-FPRGVVNVITGNTELVHPI 249
Cdd:cd07100 94 YEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKhasnVPGCALA----IEELFREAgFPEGVFQNLLIDSDQVEAI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 250 LKSGCVDVFAFIGSSGAASAL-----RELHPrpgrlrCVF---GLDAknqAVVLQDADMDVAAPEILSGSLSFSGQRCTA 321
Cdd:cd07100 170 IADPRVRGVTLTGSERAGRAVaaeagKNLKK------SVLelgGSDP---FIVLDDADLDKAVKTAVKGRLQNAGQSCIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 322 IKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVL---GSLVH 398
Cdd:cd07100 241 AKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLL--GGKRPdgpGAFYP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 399 PAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVcrVNLNSQCQRG 478
Cdd:cd07100 319 PTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM--VFINGMVKSD 396
|
410 420
....*....|....*....|....*..
gi 648475632 479 PDtLPFGGRKDSAVG-TLSvKDGIRAF 504
Cdd:cd07100 397 PR-LPFGGVKRSGYGrELG-RFGIREF 421
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
93-493 |
4.66e-57 |
|
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: 197.53 E-value: 4.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEDS-RRFEGDDilA 171
Cdd:cd07151 47 EWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILpSDVPGKE--N 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 172 RVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEALRdcFPRGVVNVITGNTE--- 244
Cdd:cd07151 125 RVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKpasdTPITGGLLLAKIFEEAG--LPKGVLNVVVGAGSeig 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 245 ---LVHPILKsgcvdVFAFIGSSGAASALRELHPRPGRlRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTA 321
Cdd:cd07151 203 dafVEHPVPR-----LISFTGSTPVGRHIGELAGRHLK-KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 322 IKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVLGSLVHPAI 401
Cdd:cd07151 277 INRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEGATLLV--GGEAEGNVLEPTV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 402 LYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDR---LGRLVDA-MsaqvcrVNLNSQCQR 477
Cdd:cd07151 355 LSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERgvqFARRIDAgM------THINDQPVN 428
|
410
....*....|....*.
gi 648475632 478 GPDTLPFGGRKDSAVG 493
Cdd:cd07151 429 DEPHVPFGGEKNSGLG 444
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
84-462 |
2.32e-56 |
|
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: 195.56 E-value: 2.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGE--DS 161
Cdd:cd07088 41 VDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEiiPS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 162 RRfEGDDILarVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC-FPRGVVNVIT 240
Cdd:cd07088 121 DR-PNENIF--IFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 241 GNTELV-HPILKSGCVDVFAFIGSSGAASALREL---HPRPGRLRcvfgLDAKNQAVVLQDADMDVAAPEILSGSLSFSG 316
Cdd:cd07088 198 GRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAaaeNITKVSLE----LGGKAPAIVMKDADLDLAVKAIVDSRIINCG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 317 QRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVinADGGSVL--- 393
Cdd:cd07088 274 QVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAVEAGATL--LTGGKRPege 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 394 -GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAM 462
Cdd:cd07088 352 kGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNEL 421
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
84-493 |
1.13e-55 |
|
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: 193.55 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLecfleRMVAEG-----DEIVRLMTLEICKPVRQAR-GEFDRTVQYVRDTIDALREMD 157
Cdd:cd07093 25 VAAAKEAFPGWSRMSPAERARIL-----HKVADLiearaDELALLESLDTGKPITLARtRDIPRAAANFRFFADYILQLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 158 GEdsrRFE-GDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEAlrdCFP 232
Cdd:cd07093 100 GE---SYPqDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKpsewTPLTAWLLAELANEA---GLP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 233 RGVVNVITGNTE-----LV-HPIlksgcVDVFAFIGSSG--------AASALRELHprpgrlrcvFGLDAKNQAVVLQDA 298
Cdd:cd07093 174 PGVVNVVHGFGPeagaaLVaHPD-----VDLISFTGETAtgrtimraAAPNLKPVS---------LELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 299 DMDVAAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAV 378
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 379 SKGARVINadGGSVL-------GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQN 451
Cdd:cd07093 320 AEGATILT--GGGRPelpdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 648475632 452 PDRLGRLVDAMSAQVCRVNlnsqCQRGPD-TLPFGGRKDSAVG 493
Cdd:cd07093 398 LGRAHRVARRLEAGTVWVN----CWLVRDlRTPFGGVKASGIG 436
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
64-505 |
1.82e-55 |
|
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: 193.28 E-value: 1.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 64 HLGSCPVLDEnaamRAAKAAVDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKP-VRQARGEFDRT 142
Cdd:cd07098 8 HLGSVPADTP----EDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGEILVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 143 VQYVRDTID----ALREmdgedSRRFEGDDIL---ARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKI 215
Cdd:cd07098 84 CEKIRWTLKhgekALRP-----ESRPGGLLMFykrARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 216 ----GRLLFSPILEALRDC-FPRGVVNVITGNTELVHPILKSGCVDVFAFIGSSG-----AASALRELHPrpgrlrCVFG 285
Cdd:cd07098 159 vawsSGFFLSIIRECLAACgHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPvgkkvMAAAAESLTP------VVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 286 LDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPG 365
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 366 RAEYLRDLVDDAVSKGARVINadGGS-------VLGSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQ 438
Cdd:cd07098 313 RFDRLEELVADAVEKGARLLA--GGKryphpeyPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANS 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 439 SDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVN---LNSQCQrgpdTLPFGGRKDSAVGTLSVKDGIRAFS 505
Cdd:cd07098 391 TEYGLGASVFGKDIKRARRIASQLETGMVAINdfgVNYYVQ----QLPFGGVKGSGFGRFAGEEGLRGLC 456
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
92-505 |
4.29e-54 |
|
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: 189.47 E-value: 4.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGeDSRRFEGDDILA 171
Cdd:cd07118 35 GPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHG-DSYNNLGDDMLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 172 RVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKlP---------KIGRLLfspiLEAlrdCFPRGVVNVITGN 242
Cdd:cd07118 114 LVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVK-PseftsgttlMLAELL----IEA---GLPAGVVNIVTGY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 243 TELV-HPILKSGCVDVFAFIGSSGAASALreLHPRPGRLRCV-FGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCT 320
Cdd:cd07118 186 GATVgQAMTEHPDVDMVSFTGSTRVGKAI--AAAAARNLKKVsLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 321 AIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVinADGGSVLGSL---- 396
Cdd:cd07118 264 SGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATL--LLGGERLASAaglf 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 397 VHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDrlGRLVDAMSAQVCRVNLNSQCQ 476
Cdd:cd07118 342 YQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDID--TALTVARRIRAGTVWVNTFLD 419
|
410 420
....*....|....*....|....*....
gi 648475632 477 RGPDtLPFGGRKDSAVGTLSVKDGIRAFS 505
Cdd:cd07118 420 GSPE-LPFGGFKQSGIGRELGRYGVEEYT 447
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
102-505 |
1.01e-53 |
|
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: 188.32 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 102 RIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGedsRRFEGD-DILARVRRAPLGP 180
Cdd:cd07120 44 RARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARTEAG---RMIEPEpGSFSLVLREPMGV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 181 VLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC--FPRGVVNVITGNT-ELVHPILKSGCVDV 257
Cdd:cd07120 121 AGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpsLPAGVVNLFTESGsEGAAHLVASPDVDV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 258 FAFIGSSGAASAL-RELHPRPGRlrcvFGLD--AKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTVFVHQSRADE 334
Cdd:cd07120 201 ISFTGSTATGRAImAAAAPTLKR----LGLElgGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 335 LLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVI----NADGGSVLGSLVHPAILYPVDSSMR 410
Cdd:cd07120 277 VRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVVlrggPVTEGLAKGAFLRPTLLEVDDPDAD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 411 VYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVcrVNLNSQCQRGPDTlPFGGRKDS 490
Cdd:cd07120 357 IVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGT--VWINDWNKLFAEA-EEGGYRQS 433
|
410
....*....|....*
gi 648475632 491 AVGTLSVKDGIRAFS 505
Cdd:cd07120 434 GLGRLHGVAALEDFI 448
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
92-505 |
1.50e-52 |
|
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: 185.06 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGeDSRRFEGDDILA 171
Cdd:cd07114 35 GAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLADKIEG-AVIPVDKGDYLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 172 RVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK--------LPKIGRLlfspILEAlrdCFPRGVVNVITG-- 241
Cdd:cd07114 114 FTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKpsehtpasTLELAKL----AEEA---GFPPGVVNVVTGfg 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 242 ---NTELV-HPIlksgcVDVFAFIGSSGAASALRELHPRpgRL-RCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSG 316
Cdd:cd07114 187 petGEALVeHPL-----VAKIAFTGGTETGRHIARAAAE--NLaPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 317 QRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVL--- 393
Cdd:cd07114 260 QTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLT--GGERPsga 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 394 ----GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRV 469
Cdd:cd07114 338 dlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWV 417
|
410 420 430
....*....|....*....|....*....|....*....
gi 648475632 470 N---LNSQCqrgpdtLPFGGRKDSAVGTLSVKDGIRAFS 505
Cdd:cd07114 418 NtyrALSPS------SPFGGFKDSGIGRENGIEAIREYT 450
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
84-505 |
1.83e-52 |
|
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: 184.95 E-value: 1.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGefdrtvQYVRDTIDALREMDGEdSRR 163
Cdd:cd07115 25 VAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR------LDVPRAADTFRYYAGW-ADK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 FEGD------DILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC-FPRGVV 236
Cdd:cd07115 98 IEGEvipvrgPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 237 NVITGNTELV------HPilksgCVDVFAFIGSSGAASALreLHPRPGRLRCV-FGLDAKNQAVVLQDADMDVAAPEILS 309
Cdd:cd07115 178 NVVTGFGEVAgaalveHP-----DVDKITFTGSTAVGRKI--MQGAAGNLKRVsLELGGKSANIVFADADLDAAVRAAAT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 310 GSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadG 389
Cdd:cd07115 251 GIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLT--G 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 390 G---SVLGSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQV 466
Cdd:cd07115 329 GkrpGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGT 408
|
410 420 430
....*....|....*....|....*....|....*....
gi 648475632 467 CRVNLNSQCQRGpdtLPFGGRKDSAVGTLSVKDGIRAFS 505
Cdd:cd07115 409 VWINTYNRFDPG---SPFGGYKQSGFGREMGREALDEYT 444
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
92-510 |
2.16e-52 |
|
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: 185.46 E-value: 2.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEW---PAMTQGERIRHLEcflERMVAEGDEIVRLMTLEICKPVRQARGEfdrtVQYVRDTIDalreMDGEDSRRFEGDD 168
Cdd:cd07086 49 KEWrkvPAPRRGEIVRQIG---EALRKKKEALGRLVSLEMGKILPEGLGE----VQEMIDICD----YAVGLSRMLYGLT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 169 I-------LARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEALRDC-FPRGVV 236
Cdd:cd07086 118 IpserpghRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKpsetTPLTAIAVTKILAEVLEKNgLPPGVV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 237 NVITGNTELVHPILKSGCVDVFAFIGSSGAASALRELHPRPGRlRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSG 316
Cdd:cd07086 198 NLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG-RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 317 QRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVL--- 393
Cdd:cd07086 277 QRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLT--GGKRIdgg 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 394 --GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNL 471
Cdd:cd07086 355 epGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNV 434
|
410 420 430
....*....|....*....|....*....|....*....
gi 648475632 472 NSQCQRGPDTLPFGGRKDSAVGTLSVKDGIRAFSMRTVV 510
Cdd:cd07086 435 NIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
92-493 |
2.10e-51 |
|
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: 182.64 E-value: 2.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARG-EFDRTVQYVR-----------DTID-ALREMDG 158
Cdd:cd07113 52 SAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfEVGQSANFLRyfagwatkingETLApSIPSMQG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 159 EDSRRFegddilarVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILE-ALRDCFPRGVVN 237
Cdd:cd07113 132 ERYTAF--------TRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAElAKEAGIPDGVLN 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 238 VITGNTELVHPILKSGCVDVFAFIGSSGAASALRELHPRPGRlRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQ 317
Cdd:cd07113 204 VVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLT-RVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQ 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 318 RCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVL---G 394
Cdd:cd07113 283 VCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVR--GGEALageG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 395 SLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNLNSQ 474
Cdd:cd07113 361 YFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTF 440
|
410
....*....|....*....
gi 648475632 475 CQrgpDTLPFGGRKDSAVG 493
Cdd:cd07113 441 LD---PAVPFGGMKQSGIG 456
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
84-493 |
4.31e-51 |
|
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: 181.68 E-value: 4.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTvqyvrdtIDALREMDGEdSRR 163
Cdd:cd07097 43 IAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRA-------GQIFRYYAGE-ALR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 FEGD-------DILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC-FPRGV 235
Cdd:cd07097 115 LSGEtlpstrpGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 236 VNVITGNTELV-HPILKSGCVDVFAFIGSSG-----AASALRELhprpgrLRCVFGLDAKNQAVVLQDADMDVAAPEILS 309
Cdd:cd07097 195 FNLVMGSGSEVgQALVEHPDVDAVSFTGSTAvgrriAAAAAARG------ARVQLEMGGKNPLVVLDDADLDLAVECAVQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 310 GSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPM-PEPGRAEYLRdLVDDAVSKGARVinAD 388
Cdd:cd07097 269 GAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVvSERQLEKDLR-YIEIARSEGAKL--VY 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 389 GGSVL-----GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMS 463
Cdd:cd07097 346 GGERLkrpdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVE 425
|
410 420 430
....*....|....*....|....*....|.
gi 648475632 464 AQVCRVNLNSQcqrGPD-TLPFGGRKDSAVG 493
Cdd:cd07097 426 AGVVMVNLPTA---GVDyHVPFGGRKGSSYG 453
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
92-493 |
2.10e-50 |
|
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: 179.35 E-value: 2.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFD---RTVQYVRDTIDALremDGEdSRRFeGDD 168
Cdd:cd07109 34 SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEaaaRYFEYYGGAADKL---HGE-TIPL-GPG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 169 ILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPK---IGRLLFSPILEALRdcFPRGVVNVITGNTE- 244
Cdd:cd07109 109 YFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEdapLTALRLAELAEEAG--LPAGALNVVTGLGAe 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 245 ----LV-HPilksgCVDVFAFIGSSG-----AASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSF 314
Cdd:cd07109 187 agaaLVaHP-----GVDHISFTGSVEtgiavMRAAAENVVP------VTLELGGKSPQIVFADADLEAALPVVVNAIIQN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 315 SGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDpDVDITPMPEPGRAEYLRDLVDDAVSKGARVinADGGSVL- 393
Cdd:cd07109 256 AGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARARARGARI--VAGGRIAe 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 394 -----GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQvcR 468
Cdd:cd07109 333 gapagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAG--Q 410
|
410 420
....*....|....*....|....*
gi 648475632 469 VNLNSQCQRGPDTLPFGGRKDSAVG 493
Cdd:cd07109 411 VFVNNYGAGGGIELPFGGVKKSGHG 435
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
93-513 |
3.61e-50 |
|
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: 179.25 E-value: 3.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGE---DSRRfegdDI 169
Cdd:cd07085 53 AWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEyleNVAR----GI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 170 LARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEAlrdCFPRGVVNVITGNTEL 245
Cdd:cd07085 129 DTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKpserVPGAAMRLAELLQEA---GLPDGVLNVVHGGKEA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 246 VHPILKSGCVDVFAFIGSSGAAsalRELHPRPGRL--RCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIK 323
Cdd:cd07085 206 VNALLDHPDIKAVSFVGSTPVG---EYIYERAAANgkRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 324 TVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVInADGGSVL------GSLV 397
Cdd:cd07085 283 VAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLV-LDGRGVKvpgyenGNFV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 398 HPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPD---RLGRLVDAmsAQVcRVNLNSQ 474
Cdd:cd07085 362 GPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAaarKFQREVDA--GMV-GINVPIP 438
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 648475632 475 CQRGPdtLPFGGRKDSAVGTLSV--KDGIRAFSMRTVVASK 513
Cdd:cd07085 439 VPLAF--FSFGGWKGSFFGDLHFygKDGVRFYTQTKTVTSR 477
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
84-493 |
4.24e-50 |
|
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: 178.71 E-value: 4.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVR-QARGEfdrtvqyVRDTIDALR-------E 155
Cdd:cd07108 25 VAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPE-------AAVLADLFRyfgglagE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 156 MDGEDSRrfEGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDCFPRGV 235
Cdd:cd07108 98 LKGETLP--FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 236 VNVITG-NTELVHPILKSGCVDVFAFIGSSGAASALRELhpRPGRLRCV-FGLDAKNQAVVLQDADMDVAAPEILSGsLS 313
Cdd:cd07108 176 LNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRA--AADRLIPVsLELGGKSPMIVFPDADLDDAVDGAIAG-MR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 314 FS--GQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVS-KGARVIN---- 386
Cdd:cd07108 253 FTrqGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLStSGATVLRggpl 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 387 -ADGGSVLGSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQ 465
Cdd:cd07108 333 pGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAG 412
|
410 420
....*....|....*....|....*...
gi 648475632 466 VCRVNLNSQCQRGpdtLPFGGRKDSAVG 493
Cdd:cd07108 413 WVQVNQGGGQQPG---QSYGGFKQSGLG 437
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
93-504 |
1.02e-49 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 178.73 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVrdtidalrEMDGEDSRRFEGDDI--- 169
Cdd:PLN02278 77 SWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFL--------EYFAEEAKRVYGDIIpsp 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 170 LARVR----RAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLL-FSPILEALRDCFPRGVVNVITGNTE 244
Cdd:PLN02278 149 FPDRRllvlKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTaLAAAELALQAGIPPGVLNVVMGDAP 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 245 LV-HPILKSGCVDVFAFIGSS--------GAASALRELHPRPGrlrcvfgldAKNQAVVLQDADMDVAAPEILSGSLSFS 315
Cdd:PLN02278 229 EIgDALLASPKVRKITFTGSTavgkklmaGAAATVKRVSLELG---------GNAPFIVFDDADLDVAVKGALASKFRNS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 316 GQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVL-- 393
Cdd:PLN02278 300 GQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLL--GGKRHsl 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 394 -GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVN-- 470
Cdd:PLN02278 378 gGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNeg 457
|
410 420 430
....*....|....*....|....*....|....
gi 648475632 471 LNSQCQRgpdtlPFGGRKDSAVGTLSVKDGIRAF 504
Cdd:PLN02278 458 LISTEVA-----PFGGVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
93-504 |
4.57e-49 |
|
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: 175.58 E-value: 4.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQArgeFDRTVQ-------YVRDTIDALRemdgeDSRRFE 165
Cdd:cd07101 33 AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHA---FEEVLDvaivaryYARRAERLLK-----PRRRRG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 166 GDDILARVR--RAPLGPVLCMGPYNFPFNETFATLIPALLMGNtAVVKLPKiGRLLFSPIL--EALRDC-FPRGVVNVIT 240
Cdd:cd07101 105 AIPVLTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGN-AVVLKPD-SQTALTALWavELLIEAgLPRDLWQVVT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 241 GNTELVHPILKSGCvDVFAFIGSSGAAsalRELHPRPGR--LRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQR 318
Cdd:cd07101 183 GPGSEVGGAIVDNA-DYVMFTGSTATG---RVVAERAGRrlIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 319 CTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSV---LGS 395
Cdd:cd07101 259 CVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLA--GGRArpdLGP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 396 LVH-PAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNLNSQ 474
Cdd:cd07101 337 YFYePTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYA 416
|
410 420 430
....*....|....*....|....*....|
gi 648475632 475 CQRGPDTLPFGGRKDSAVGTLSVKDGIRAF 504
Cdd:cd07101 417 AAWASIDAPMGGMKDSGLGRRHGAEGLLKY 446
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
84-494 |
1.67e-48 |
|
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: 174.05 E-value: 1.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQAR-GEFDRTVQYVRDTIDALREMDGEDSR 162
Cdd:cd07092 25 VAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPGAVDNFRFFAGAARTLEGPAAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 163 RFEGDdILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDCFPRGVVNVITGN 242
Cdd:cd07092 105 EYLPG-HTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 243 TELV------HPIlksgcVDVFAFIGS--------SGAASALRELHprpgrlrcvFGLDAKNQAVVLQDADMDVAAPEIL 308
Cdd:cd07092 184 GASAgdalvaHPR-----VRMVSLTGSvrtgkkvaRAAADTLKRVH---------LELGGKAPVIVFDDADLDAAVAGIA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 309 SGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAvSKGARVinAD 388
Cdd:cd07092 250 TAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERA-PAHARV--LT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 389 GGSVL---GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQ 465
Cdd:cd07092 327 GGRRAegpGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFG 406
|
410 420 430
....*....|....*....|....*....|.
gi 648475632 466 VCRVNlnsqcQRGPDT--LPFGGRKDSAVGT 494
Cdd:cd07092 407 TVWVN-----THIPLAaeMPHGGFKQSGYGK 432
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
84-493 |
1.88e-48 |
|
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: 174.23 E-value: 1.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARG-EFDRTVQYVRDTIDALREMDGEdsR 162
Cdd:cd07138 42 VAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAaQVGLGIGHLRAAADALKDFEFE--E 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 163 RFEGddilARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK---LPKIGRLLFSPILEALRdcFPRGVVNVI 239
Cdd:cd07138 120 RRGN----SLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKpseVAPLSAIILAEILDEAG--LPAGVFNLV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 240 TGNTELV------HPIlksgcVDVFAFIGSSGAASALRELHPRPGRlRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLS 313
Cdd:cd07138 194 NGDGPVVgealsaHPD-----VDMVSFTGSTRAGKRVAEAAADTVK-RVALELGGKSANIILDDADLEKAVPRGVAACFA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 314 FSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVInADG---- 389
Cdd:cd07138 268 NSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLV-AGGpgrp 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 390 -GSVLGSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCR 468
Cdd:cd07138 347 eGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVH 426
|
410 420
....*....|....*....|....*...
gi 648475632 469 VN---LNSQcqrgpdtLPFGGRKDSAVG 493
Cdd:cd07138 427 INgaaFNPG-------APFGGYKQSGNG 447
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
92-493 |
2.05e-48 |
|
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: 174.33 E-value: 2.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEfDrtvqyVRDTIDALR-------EMDGEDSRrf 164
Cdd:cd07112 40 GVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAV-D-----VPSAANTFRwyaeaidKVYGEVAP-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 165 EGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKlP---------KIGRLlfspileALRDCFPRGV 235
Cdd:cd07112 112 TGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLK-PaeqspltalRLAEL-------ALEAGLPAGV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 236 VNVITGNTELV-HPILKSGCVDVFAFIGSSGAASALRELHPRPGRLRCVFGLDAKNQAVVLQDA-DMDVAAPEILSGSLS 313
Cdd:cd07112 184 LNVVPGFGHTAgEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFW 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 314 FSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVinADGGSVL 393
Cdd:cd07112 264 NQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARL--VAGGKRV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 394 -----GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCR 468
Cdd:cd07112 342 ltetgGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVW 421
|
410 420
....*....|....*....|....*
gi 648475632 469 VNlnsQCQRGPDTLPFGGRKDSAVG 493
Cdd:cd07112 422 VN---CFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
91-490 |
3.55e-48 |
|
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: 172.84 E-value: 3.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 91 LGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEdsRRFEGDDIL 170
Cdd:cd07095 13 FPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTGE--RATPMAQGR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 171 ARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEAlrdCFPRGVVNVITGNTELV 246
Cdd:cd07095 91 AVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKpselTPAVAELMVELWEEA---GLPPGVLNLVQGGRETG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 247 HPILKSGCVDVFAFIGSSGAASAL-RELHPRPGRLrCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTV 325
Cdd:cd07095 168 EALAAHEGIDGLLFTGSAATGLLLhRQFAGRPGKI-LALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 326 FVHQS-RADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINA----DGGsvlGSLVHPA 400
Cdd:cd07095 247 IVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAmerlVAG---TAFLSPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 401 ILYPVDSSMRVyHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVcrVNLNSQCQRGPD 480
Cdd:cd07095 324 IIDVTDAADVP-DEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGI--VNWNRPTTGASS 400
|
410
....*....|
gi 648475632 481 TLPFGGRKDS 490
Cdd:cd07095 401 TAPFGGVGLS 410
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
93-494 |
2.16e-47 |
|
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: 172.41 E-value: 2.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEDSRRFEGDDILAR 172
Cdd:cd07124 84 TWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 173 VRraPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEAlrdCFPRGVVNVITGNTELV-- 246
Cdd:cd07124 164 YR--PLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKpaedTPVIAAKLVEILEEA---GLPPGVVNFLPGPGEEVgd 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 247 ----HPIlksgcVDVFAFIGSSGAASALRE----LHPRPGRL-RCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQ 317
Cdd:cd07124 239 ylveHPD-----VRFIAFTGSREVGLRIYEraakVQPGQKWLkRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQ 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 318 RCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGaRVINadGGSVL---- 393
Cdd:cd07124 314 KCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLL--GGEVLelaa 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 394 -GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNln 472
Cdd:cd07124 391 eGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYAN-- 468
|
410 420
....*....|....*....|....*..
gi 648475632 473 sqcqRG-----PDTLPFGGRKDSAVGT 494
Cdd:cd07124 469 ----RKitgalVGRQPFGGFKMSGTGS 491
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
92-493 |
3.30e-46 |
|
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: 168.64 E-value: 3.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEDSRRfeGDDILA 171
Cdd:cd07119 51 GEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDV--PPHVIS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 172 RVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRL----LFSPILEAlrdCFPRGVVNVITGNTELV- 246
Cdd:cd07119 129 RTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLttiaLFELIEEA---GLPAGVVNLVTGSGATVg 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 247 HPILKSGCVDVFAFIGSSGA-ASALRELhprPGRL-RCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKT 324
Cdd:cd07119 206 AELAESPDVDLVSFTGGTATgRSIMRAA---AGNVkKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 325 VFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVIN-----ADGGSVLGSLVHP 399
Cdd:cd07119 283 LLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCggkrpTGDELAKGYFVEP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 400 AILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNlnsqcQRGP 479
Cdd:cd07119 363 TIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN-----DYHP 437
|
410
....*....|....*.
gi 648475632 480 DT--LPFGGRKDSAVG 493
Cdd:cd07119 438 YFaeAPWGGYKQSGIG 453
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
93-494 |
5.85e-45 |
|
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: 164.39 E-value: 5.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEiCKPVR-QARGEFDRTVQYVRDTIDALREMDGEDSRRFEGDDILA 171
Cdd:cd07152 28 AWAATPPRERAAVLRRAADLLEEHADEIADWIVRE-SGSIRpKAGFEVGAAIGELHEAAGLPTQPQGEILPSAPGRLSLA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 172 RvrRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEALRdcFPRGVVNVITGNTELVH 247
Cdd:cd07152 107 R--RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKpdprTPVSGGVVIARLFEEAG--LPAGVLHVLPGGADAGE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 248 PILKSGCVDVFAFIGSSGAASALRELhprPGRL--RCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTV 325
Cdd:cd07152 183 ALVEDPNVAMISFTGSTAVGRKVGEA---AGRHlkKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 326 FVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVLGSLVHPAILYPV 405
Cdd:cd07152 260 LVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEA--GGTYDGLFYRPTVLSGV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 406 DSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMsaQVCRVNLNSQCQRGPDTLPFG 485
Cdd:cd07152 338 KPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRL--RTGMLHINDQTVNDEPHNPFG 415
|
....*....
gi 648475632 486 GRKDSAVGT 494
Cdd:cd07152 416 GMGASGNGS 424
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
84-493 |
1.32e-44 |
|
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: 164.16 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGeFD-----RTVQYVRDTIDAlremdG 158
Cdd:cd07117 44 VKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRA-VDiplaaDHFRYFAGVIRA-----E 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 159 EDSRRFEGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDCFPRGVVNV 238
Cdd:cd07117 118 EGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 239 ITG------NTELVHPILksgcvDVFAFIGSSG-----AASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDVAAPEI 307
Cdd:cd07117 198 VTGkgsksgEYLLNHPGL-----DKLAFTGSTEvgrdvAIAAAKKLIP------ATLELGGKSANIIFDDANWDKALEGA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 308 LSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVIN- 386
Cdd:cd07117 267 QLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTg 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 387 ----ADGGSVLGSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAM 462
Cdd:cd07117 347 ghrlTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAV 426
|
410 420 430
....*....|....*....|....*....|.
gi 648475632 463 saQVCRVNLNSQCQRgPDTLPFGGRKDSAVG 493
Cdd:cd07117 427 --ETGRVWVNTYNQI-PAGAPFGGYKKSGIG 454
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
84-504 |
1.34e-44 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 164.31 E-value: 1.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVrdtidalrEMDGEDSRR 163
Cdd:PRK11241 54 IDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFI--------EWFAEEGKR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 FEGDDILAR-------VRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKlpKIGRLLFSPILE---ALRDCFPR 233
Cdd:PRK11241 126 IYGDTIPGHqadkrliVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLK--PASQTPFSALALaelAIRAGIPA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 234 GVVNVITGNTELVHPILKSG-CVDVFAFIGSSGAASALRELHPRPGRlRCVFGLDAKNQAVVLQDADMDVAAPEILSGSL 312
Cdd:PRK11241 204 GVFNVVTGSAGAVGGELTSNpLVRKLSFTGSTEIGRQLMEQCAKDIK-KVSLELGGNAPFIVFDDADLDKAVEGALASKF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 313 SFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINADGGSV 392
Cdd:PRK11241 283 RNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 393 L-GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVN- 470
Cdd:PRK11241 363 LgGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINt 442
|
410 420 430
....*....|....*....|....*....|....*
gi 648475632 471 -LNSQcqrgpDTLPFGGRKDSAVGTLSVKDGIRAF 504
Cdd:PRK11241 443 gIISN-----EVAPFGGIKASGLGREGSKYGIEDY 472
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
84-493 |
1.92e-44 |
|
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: 163.29 E-value: 1.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDR---TVQYVRDTIDALREMDGEd 160
Cdd:cd07110 25 VRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDvagCFEYYADLAEQLDAKAER- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 161 SRRFEGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRL----LFSPILEAlrdCFPRGVV 236
Cdd:cd07110 104 AVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLteleLAEIAAEA---GLPPGVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 237 NVITGNTELV------HPIlksgcVDVFAFIGSSG-------AASALRelhpRPGRLRcvfgLDAKNQAVVLQDADMDVA 303
Cdd:cd07110 181 NVVTGTGDEAgaplaaHPG-----IDKISFTGSTAtgsqvmqAAAQDI----KPVSLE----LGGKSPIIVFDDADLEKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 304 APEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGAR 383
Cdd:cd07110 248 VEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGAR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 384 VINadGGSVLGSL-----VHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRL 458
Cdd:cd07110 328 LLC--GGRRPAHLekgyfIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRV 405
|
410 420 430
....*....|....*....|....*....|....*...
gi 648475632 459 VDAMSAQVCRVNlNSQ---CQrgpdtLPFGGRKDSAVG 493
Cdd:cd07110 406 AEALEAGIVWIN-CSQpcfPQ-----APWGGYKRSGIG 437
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
84-494 |
5.46e-44 |
|
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: 161.77 E-value: 5.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEDSRr 163
Cdd:cd07107 25 VAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVTELKGETIP- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 fEGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPK---IGRLLFSpilEALRDCFPRGVVNVIT 240
Cdd:cd07107 104 -VGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEqapLSALRLA---ELAREVLPPGVFNILP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 241 GNTELV------HPIlksgcVDVFAFIGS--------SGAASALRELhprpgrlrcVFGLDAKNQAVVLQDADMDVAAPE 306
Cdd:cd07107 180 GDGATAgaalvrHPD-----VKRIALIGSvptgraimRAAAEGIKHV---------TLELGGKNALIVFPDADPEAAADA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 307 ILSG-SLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVI 385
Cdd:cd07107 246 AVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREGARLV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 386 NADG---GSVL--GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVD 460
Cdd:cd07107 326 TGGGrpeGPALegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTAR 405
|
410 420 430
....*....|....*....|....*....|....
gi 648475632 461 AMSAQVCRVNLNSQCQRGpdtLPFGGRKDSAVGT 494
Cdd:cd07107 406 RVEAGYVWINGSSRHFLG---APFGGVKNSGIGR 436
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
118-453 |
2.22e-42 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 156.43 E-value: 2.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 118 DEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGE--DSRRfEGDDILarVRRAPLGPVLCMGPYNFPFNETF 195
Cdd:PRK10090 13 SEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEiiQSDR-PGENIL--LFKRALGVTTGILPWNFPFFLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 196 ATLIPALLMGNTAVVK---LPKIGRLLFSPILEALRdcFPRGVVNVITGNTELV-HPILKSGCVDVFAFIGSSGAASALR 271
Cdd:PRK10090 90 RKMAPALLTGNTIVIKpseFTPNNAIAFAKIVDEIG--LPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGSVSAGEKIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 272 ElHPRPGRLRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMP 351
Cdd:PRK10090 168 A-AAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 352 FD-PDVDITPMPEPGRAEYLRDLVDDAVSKGARVI---NADGGSvlGSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFD 427
Cdd:PRK10090 247 AErNDIAMGPLINAAALERVEQKVARAVEEGARVAlggKAVEGK--GYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFD 324
|
330 340
....*....|....*....|....*.
gi 648475632 428 DDRTPVEYQAQSDFGQQVSLFGQNPD 453
Cdd:PRK10090 325 TLEEAIAMANDSDYGLTSSIYTQNLN 350
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
93-505 |
1.20e-41 |
|
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: 155.54 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEfdrtVQYVRDTID----ALREMDGEdsrRFE-GD 167
Cdd:cd07090 34 EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD----IDSSADCLEyyagLAPTLSGE---HVPlPG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 168 DILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK---LPKIGRLLFSPIL-EAlrdCFPRGVVNVITGNT 243
Cdd:cd07090 107 GSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKpspFTPLTALLLAEILtEA---GLPDGVFNVVQGGG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 244 ELVHPILKSGCVDVFAFIGSSGAASALRELhpRPGRLRCV-FGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAI 322
Cdd:cd07090 184 ETGQLLCEHPDVAKVSFTGSVPTGKKVMSA--AAKGIKHVtLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 323 KTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVL--------G 394
Cdd:cd07090 262 TRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEGAKVLC--GGERVvpedglenG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 395 SLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNLNSQ 474
Cdd:cd07090 340 FYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNI 419
|
410 420 430
....*....|....*....|....*....|.
gi 648475632 475 cqrGPDTLPFGGRKDSAVGTLSVKDGIRAFS 505
Cdd:cd07090 420 ---SPVEVPFGGYKQSGFGRENGTAALEHYT 447
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
86-513 |
3.60e-41 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 154.11 E-value: 3.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 86 AYGRGL--GEWPAMTqgERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGED--- 160
Cdd:cd07148 30 AHALFLdrNNWLPAH--ERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREipm 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 161 SRRFEGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEAlrdCFPRGVV 236
Cdd:cd07148 108 GLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKpalaTPLSCLAFVDLLHEA---GLPEGWC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 237 NVITGNTELVHPILKSGCVDVFAFIGSSGAASALRElHPRPGRlRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSG 316
Cdd:cd07148 185 QAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRS-KLAPGT-RCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 317 QRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVLG-S 395
Cdd:cd07148 263 QVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLC--GGKRLSdT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 396 LVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEyQAQS-DFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNLNSQ 474
Cdd:cd07148 341 TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIA-QANSlPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTA 419
|
410 420 430
....*....|....*....|....*....|....*....
gi 648475632 475 CQrgPDTLPFGGRKDSAVGTlsvkDGIrAFSMRTVVASK 513
Cdd:cd07148 420 FR--VDWMPFAGRRQSGYGT----GGI-PYTMHDMTQEK 451
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
85-498 |
4.25e-41 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 154.89 E-value: 4.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 85 DAYGRGLG-EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTV---QYVRDTIDALREMDGED 160
Cdd:PLN02467 56 KAFKRNKGkDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAgcfEYYADLAEALDAKQKAP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 161 ----SRRFEGddilaRVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC-FPRGV 235
Cdd:PLN02467 136 vslpMETFKG-----YVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVgLPPGV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 236 VNVITG-NTELVHPILKSGCVDVFAFIGSSG-----AASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDVAAPEILS 309
Cdd:PLN02467 211 LNVVTGlGTEAGAPLASHPGVDKIAFTGSTAtgrkiMTAAAQMVKP------VSLELGGKSPIIVFDDVDLDKAVEWAMF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 310 GSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadG 389
Cdd:PLN02467 285 GCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILC--G 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 390 GS-----VLGSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSA 464
Cdd:PLN02467 363 GKrpehlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQA 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 648475632 465 QVCRVNLnSQ---CQrgpdtLPFGGRKDSAVGT----------LSVK 498
Cdd:PLN02467 443 GIVWINC-SQpcfCQ-----APWGGIKRSGFGRelgewglenyLSVK 483
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
92-493 |
6.19e-41 |
|
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: 153.90 E-value: 6.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGeFDrtvqyVRDTIDALR-------EMDGedsRRF 164
Cdd:cd07091 57 GWWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESAK-GD-----VALSIKCLRyyagwadKIQG---KTI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 165 E-GDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKigrllFSPiLEALRDC-------FPRGVV 236
Cdd:cd07091 128 PiDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAE-----QTP-LSALYLAelikeagFPPGVV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 237 NVITGNTELV------HPIlksgcVDVFAFIGS---------SGAASALRelhprpgrlRCVFGLDAKNQAVVLQDADMD 301
Cdd:cd07091 202 NIVPGFGPTAgaaissHMD-----VDKIAFTGStavgrtimeAAAKSNLK---------KVTLELGGKSPNIVFDDADLD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 302 VAAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKG 381
Cdd:cd07091 268 KAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 382 ARVINadGGSVLGS---LVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRL 458
Cdd:cd07091 348 ATLLT--GGERHGSkgyFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRV 425
|
410 420 430
....*....|....*....|....*....|....*....
gi 648475632 459 VDAMSAQVCRVN----LNSQCqrgpdtlPFGGRKDSAVG 493
Cdd:cd07091 426 SRALKAGTVWVNtynvFDAAV-------PFGGFKQSGFG 457
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
115-509 |
7.08e-41 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 153.35 E-value: 7.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 115 AEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEDSRrfEGDDILAR---VRRAPLGPVLCMGPYNFPF 191
Cdd:PRK09406 60 AEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEALLADEPA--DAAAVGASrayVRYQPLGVVLAVMPWNFPL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 192 NETFATLIPALLMGNTAVVK----LPKIGrlLFspiLEAL--RDCFPRGVVNVITGNTELVHPILKSGCVDVFAFIGS-- 263
Cdd:PRK09406 138 WQVVRFAAPALMAGNVGLLKhasnVPQTA--LY---LADLfrRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSep 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 264 ---SGAASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLK 340
Cdd:PRK09406 213 agrAVAAIAGDEIKK------TVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 341 AGVGKLKIGMPFDPDVDITPMP-EPGRAEyLRDLVDDAVSKGARVINadGGSVL---GSLVHPAILYPVDSSMRVYHEEQ 416
Cdd:PRK09406 287 ARMAALRVGDPTDPDTDVGPLAtEQGRDE-VEKQVDDAVAAGATILC--GGKRPdgpGWFYPPTVITDITPDMRLYTEEV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 417 FGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQvcRVNLNSQCQRGPDtLPFGGRKDSAVGTLS 496
Cdd:PRK09406 364 FGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAG--QVFINGMTVSYPE-LPFGGVKRSGYGREL 440
|
410
....*....|....
gi 648475632 497 VKDGIRAF-SMRTV 509
Cdd:PRK09406 441 SAHGIREFcNIKTV 454
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
84-458 |
8.01e-41 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 153.53 E-value: 8.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARgEFDrtvqyVRDTIDALREMDGEdSRR 163
Cdd:PRK13473 45 VAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLAL-NDE-----IPAIVDVFRFFAGA-ARC 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 FEG-------DDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDCFPRGVV 236
Cdd:PRK13473 118 LEGkaageylEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 237 NVITGNTELV------HPIlksgcVDVFAFIGS--------SGAASALRELHprpgrlrcvFGLDAKNQAVVLQDADMDV 302
Cdd:PRK13473 198 NVVTGRGATVgdalvgHPK-----VRMVSLTGSiatgkhvlSAAADSVKRTH---------LELGGKAPVIVFDDADLDA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 303 AAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKG- 381
Cdd:PRK13473 264 VVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGh 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 382 ARVINadGGSVL---GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRL 458
Cdd:PRK13473 344 IRVVT--GGEAPdgkGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRV 421
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
93-493 |
1.68e-40 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 153.50 E-value: 1.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQArgeFDRTVQ-------YVRDTIDALRemdgeDSRRFE 165
Cdd:PRK09407 69 AWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHA---FEEVLDvaltaryYARRAPKLLA-----PRRRAG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 166 GDDIL--ARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKlPKiGRLLFSPIL--EALRDC-FPRGVVNVIT 240
Cdd:PRK09407 141 ALPVLtkTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK-PD-SQTPLTALAavELLYEAgLPRDLWQVVT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 241 GNTELVHPILKSGCvDVFAFIGSSGAAsalRELHPRPGR--LRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQR 318
Cdd:PRK09407 219 GPGPVVGTALVDNA-DYLMFTGSTATG---RVLAEQAGRrlIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 319 CTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSV---LGS 395
Cdd:PRK09407 295 CISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLA--GGKArpdLGP 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 396 LVH-PAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDR---LGRLVDAMSaqvcrVNL 471
Cdd:PRK09407 373 LFYePTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARgraIAARIRAGT-----VNV 447
|
410 420 430
....*....|....*....|....*....|.
gi 648475632 472 NsqcqrgpDTL---------PFGGRKDSAVG 493
Cdd:PRK09407 448 N-------EGYaaawgsvdaPMGGMKDSGLG 471
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
92-493 |
2.79e-40 |
|
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: 152.26 E-value: 2.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQAR-GEFDRTVQYVR------DTIDALR-EMDGedsrr 163
Cdd:cd07142 57 GPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARyAEVPLAARLFRyyagwaDKIHGMTlPADG----- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 fegdDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPK--------IGRLLfspiLEAlrdCFPRGV 235
Cdd:cd07142 132 ----PHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEqtplsallAAKLA----AEA---GLPDGV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 236 VNVITGNTELV-HPILKSGCVDVFAFIGSSGAASALRELHPRPGRLRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSF 314
Cdd:cd07142 201 LNIVTGFGPTAgAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 315 SGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVLG 394
Cdd:cd07142 281 QGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLIT--GGDRIG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 395 S---LVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNl 471
Cdd:cd07142 359 SkgyYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVN- 437
|
410 420
....*....|....*....|...
gi 648475632 472 nsqCQRGPD-TLPFGGRKDSAVG 493
Cdd:cd07142 438 ---CYDVFDaSIPFGGYKMSGIG 457
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
84-508 |
4.83e-40 |
|
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: 151.39 E-value: 4.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARgefDRTVQYVR----------DTIDal 153
Cdd:cd07111 65 VAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESR---DCDIPLVArhfyhhagwaQLLD-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 154 REMDGedsrrfegddilarvrRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGR---LLFSPILEALRdc 230
Cdd:cd07111 140 TELAG----------------WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPltaLLFAEICAEAG-- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 231 FPRGVVNVITGNTELVHPILKSGCVDVFAFIGSSGAASALRELHPRPGRlRCVFGLDAKNQAVVLQDADMDVAAPEILSG 310
Cdd:cd07111 202 LPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGK-KLSLELGGKSPFIVFDDADLDSAVEGIVDA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 311 SLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINADGG 390
Cdd:cd07111 281 IWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGAD 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 391 SVLGSLVHPAILYP-VDSSMRVYHEEQFGPVVPVVPFdddRTPVEYQA---QSDFGQQVSLFGQNPDRLgrLVDAMSAQV 466
Cdd:cd07111 361 LPSKGPFYPPTLFTnVPPASRIAQEEIFGPVLVVLTF---RTAKEAVAlanNTPYGLAASVWSENLSLA--LEVALSLKA 435
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 648475632 467 CRVNLNSQCQRGPdTLPFGGRKDSAVGTLSVKDGIRAFSMRT 508
Cdd:cd07111 436 GVVWINGHNLFDA-AAGFGGYRESGFGREGGKEGLYEYLRPS 476
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
93-505 |
5.11e-39 |
|
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: 147.76 E-value: 5.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQAR-GEFDRTVQYVRDTIDALRE----------MDGEDS 161
Cdd:cd07134 13 ALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlTEILPVLSEINHAIKHLKKwmkpkrvrtpLLLFGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 162 RrfegddilARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDCFPRGVVNVITG 241
Cdd:cd07134 93 K--------SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 242 NTELVHPILKSGCVDVFaFIGSsgaasalrelhPRPGRLrcVFGLDAKNQA-VVLQ-----------DADMDVAAPEILS 309
Cdd:cd07134 165 DAEVAQALLELPFDHIF-FTGS-----------PAVGKI--VMAAAAKHLAsVTLElggksptivdeTADLKKAAKKIAW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 310 GSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKL--KIGMPFDPDvDITPMPEPGRAEYLRDLVDDAVSKGARVIna 387
Cdd:cd07134 231 GKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFygKDAARKASP-DLARIVNDRHFDRLKGLLDDAVAKGAKVE-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 388 DGGSVLGS--LVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQ 465
Cdd:cd07134 308 FGGQFDAAqrYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 648475632 466 VCRVN------LNSQcqrgpdtLPFGGRKDSAVGTLSVKDGIRAFS 505
Cdd:cd07134 388 GVVVNdvvlhfLNPN-------LPFGGVNNSGIGSYHGVYGFKAFS 426
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
84-493 |
1.10e-38 |
|
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: 147.88 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARG-EFDRTVQYVRDTIDALREMDGEDSR 162
Cdd:cd07559 44 VDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSLSE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 163 RFEgdDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDCFPRGVVNVITG- 241
Cdd:cd07559 124 IDE--DTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGf 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 242 NTELVHPILKSGCVDVFAFIGSSG-----AASALRELHPrpgrlrCVFGLDAKNQAVVLQDA-----DMDVAAPEILSGS 311
Cdd:cd07559 202 GSEAGKPLASHPRIAKLAFTGSTTvgrliMQYAAENLIP------VTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 312 LSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVI-----N 386
Cdd:cd07559 276 AFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLtggerL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 387 ADGGSVLGSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMsaQV 466
Cdd:cd07559 356 TLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGI--QT 433
|
410 420
....*....|....*....|....*..
gi 648475632 467 CRVNLNSQCQRgPDTLPFGGRKDSAVG 493
Cdd:cd07559 434 GRVWVNCYHQY-PAHAPFGGYKKSGIG 459
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
170-493 |
1.13e-38 |
|
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: 147.68 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 170 LARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKigrllFSPiLEALRDC-------FPRGVVNVITGN 242
Cdd:cd07143 137 LTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSE-----LTP-LSALYMTklipeagFPPGVINVVSGY 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 243 TELVHPILKSGC-VDVFAFIGSSGAASALRELHPRPGRLRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTA 321
Cdd:cd07143 211 GRTCGNAISSHMdIDKVAFTGSTLVGRKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 322 IKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSV---LGSLVH 398
Cdd:cd07143 291 GSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVET--GGKRhgnEGYFIE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 399 PAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNLNSQCQRG 478
Cdd:cd07143 369 PTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQ 448
|
330
....*....|....*
gi 648475632 479 pdtLPFGGRKDSAVG 493
Cdd:cd07143 449 ---VPFGGYKQSGIG 460
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
94-513 |
1.15e-37 |
|
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: 144.64 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 94 WPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEDSRRFEGDDILARV 173
Cdd:TIGR01722 54 WGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 174 RRaPLGPVLCMGPYNFPfnetfaTLIP------ALLMGNTAVVK----LPKIGRLLFSPILEAlrdCFPRGVVNVITGNT 243
Cdd:TIGR01722 134 RQ-PLGVCAGITPFNFP------AMIPlwmfpiAIACGNTFVLKpsekVPSAAVKLAELFSEA---GAPDGVLNVVHGDK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 244 ELVHPILKSGCVDVFAFIGSSGAASALRELHPRPGRLRCVFGlDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIK 323
Cdd:TIGR01722 204 EAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALG-GAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 324 TVfVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVInADGGSVL------GSLV 397
Cdd:TIGR01722 283 AA-VLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVL-LDGRGYKvdgyeeGNWV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 398 HPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLF---GQNPDRLGRLVDamsaqVCRVNLNSQ 474
Cdd:TIGR01722 361 GPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFtrdGAAARRFQHEIE-----VGQVGVNVP 435
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 648475632 475 CqrgPDTLP---FGGRKDSAVGTLSV--KDGIRAFSMRTVVASK 513
Cdd:TIGR01722 436 I---PVPLPyfsFTGWKDSFFGDHHIygKQGTHFYTRGKTVTTR 476
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
84-486 |
4.31e-37 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 143.17 E-value: 4.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEdsRR 163
Cdd:PRK09457 43 VRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAMINKIAISIQAYHERTGE--KR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 FEGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEAlrdCFPRGVVNVI 239
Cdd:PRK09457 121 SEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKpselTPWVAELTVKLWQQA---GLPAGVLNLV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 240 TGNTELVHPILKSGCVDVFAFIGSSGAASAL-RELHPRPGRlrcVFGLD--AKNQAVVLQDADMDVAAPEILSGSLSFSG 316
Cdd:PRK09457 198 QGGRETGKALAAHPDIDGLLFTGSANTGYLLhRQFAGQPEK---ILALEmgGNNPLVIDEVADIDAAVHLIIQSAFISAG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 317 QRCTAIKTVFVHQS-RADELLERLKAGVGKLKIGMPF-DPDVDITPMPEPGRAEYLRDLVDDAVSKGARVI----NADGG 390
Cdd:PRK09457 275 QRCTCARRLLVPQGaQGDAFLARLVAVAKRLTVGRWDaEPQPFMGAVISEQAAQGLVAAQAQLLALGGKSLlemtQLQAG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 391 SvlgSLVHPAILyPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVcrVN 470
Cdd:PRK09457 355 T---GLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGI--VN 428
|
410
....*....|....*.
gi 648475632 471 LNSQCQRGPDTLPFGG 486
Cdd:PRK09457 429 WNKPLTGASSAAPFGG 444
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
89-493 |
2.18e-35 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 138.07 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 89 RGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEDSRRFEGDD 168
Cdd:PRK13968 40 AGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAMLKAEPTLVENQQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 169 ILARVRraPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK-LPKI---GRLlfspILEALRDC-FPRGVVNVITGNT 243
Cdd:PRK13968 120 AVIEYR--PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKhAPNVmgcAQL----IAQVFKDAgIPQGVYGWLNADN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 244 ELVHPILK---------SGCVDVFAFIGSSgAASALRelhprpgrlRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSF 314
Cdd:PRK13968 194 DGVSQMINdsriaavtvTGSVRAGAAIGAQ-AGAALK---------KCVLELGGSDPFIVLNDADLELAVKAAVAGRYQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 315 SGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVL- 393
Cdd:PRK13968 264 TGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLL--GGEKIa 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 394 --GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLvdAMSAQVCRVNL 471
Cdd:PRK13968 342 gaGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQM--AARLECGGVFI 419
|
410 420
....*....|....*....|..
gi 648475632 472 NSQCQRGPdTLPFGGRKDSAVG 493
Cdd:PRK13968 420 NGYCASDA-RVAFGGVKKSGFG 440
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
171-509 |
2.56e-35 |
|
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: 137.23 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 171 ARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKL----PKIGRLLfspiLEALRDCFPRGVVNVITGNtelv 246
Cdd:cd07133 95 AEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPseftPRTSALL----AELLAEYFDEDEVAVVTGG---- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 247 hpilksgcVDV---FA--------FIGSSG-----AASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDVAAPEILSG 310
Cdd:cd07133 167 --------ADVaaaFSslpfdhllFTGSTAvgrhvMRAAAENLTP------VTLELGGKSPAIIAPDADLAKAAERIAFG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 311 SLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLkigmpFdPDV----DITPMPEPGRAEYLRDLVDDAVSKGARVIN 386
Cdd:cd07133 233 KLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-----Y-PTLadnpDYTSIINERHYARLQGLLEDARAKGARVIE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 387 ADGGSVLGSLVH---PAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVD-AM 462
Cdd:cd07133 307 LNPAGEDFAATRklpPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRrTH 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 648475632 463 SAQVCrVNlNSQCQRGPDTLPFGGRKDSAVGTLSVKDGIRAFS-MRTV 509
Cdd:cd07133 387 SGGVT-IN-DTLLHVAQDDLPFGGVGASGMGAYHGKEGFLTFShAKPV 432
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
84-493 |
3.80e-35 |
|
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: 137.92 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQG-ERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQ-ARGEFDrtvqyvrDTIDALREMDGEdS 161
Cdd:cd07144 51 VKAARKAFESWWSKVTGeERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnALGDLD-------EIIAVIRYYAGW-A 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 162 RRFEGDDI------LARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRL----LFSPILEAlrdCF 231
Cdd:cd07144 123 DKIQGKTIptspnkLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLsllyFANLVKEA---GF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 232 PRGVVNVITGNTELV-HPILKSGCVDVFAFIGSSG--------AASALRELhprpgRLRCvfglDAKNQAVVLQDADMDV 302
Cdd:cd07144 200 PPGVVNIIPGYGAVAgSALAEHPDVDKIAFTGSTAtgrlvmkaAAQNLKAV-----TLEC----GGKSPALVFEDADLDQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 303 AAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGK-LKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKG 381
Cdd:cd07144 271 AVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 382 ARVINADGGSVL----GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGR 457
Cdd:cd07144 351 AKLVYGGEKAPEglgkGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHR 430
|
410 420 430
....*....|....*....|....*....|....*..
gi 648475632 458 LVDAMSAQVCRVNL-NSQCQRgpdtLPFGGRKDSAVG 493
Cdd:cd07144 431 VARELEAGMVWINSsNDSDVG----VPFGGFKMSGIG 463
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
171-510 |
1.33e-34 |
|
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: 134.96 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 171 ARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIgrllfSP-----ILEALRDCFPRGVVNVITG---- 241
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSEL-----APatsalLAKLIPKYFDPEAVAVVEGgvev 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 242 NTELV-HP---ILKSGCVDVfafiGSSGAASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQ 317
Cdd:cd07087 169 ATALLaEPfdhIFFTGSPAV----GKIVMEAAAKHLTP------VTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 318 RCTAIKTVFVHQSRADELLERLKAGVGKLkigmpFDPDVDITPmpepgraEYLRDLVDDAVSKGARVINAD----GGSVL 393
Cdd:cd07087 239 TCIAPDYVLVHESIKDELIEELKKAIKEF-----YGEDPKESP-------DYGRIINERHFDRLASLLDDGkvviGGQVD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 394 GS--LVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSA-QVCrVN 470
Cdd:cd07087 307 KEerYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSgGVC-VN 385
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 648475632 471 -LNSQCqrGPDTLPFGGRKDSAVGTLSVKDGIRAFS-MRTVV 510
Cdd:cd07087 386 dVLLHA--AIPNLPFGGVGNSGMGAYHGKAGFDTFShLKSVL 425
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
92-493 |
1.47e-33 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 133.48 E-value: 1.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQA-RGEFDRTVQYVRDTIDALREMDGEDSRrfEGDDIL 170
Cdd:PRK09847 73 GDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVAT--TSSHEL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 171 ARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIgrllfSPiLEALR-------DCFPRGVVNVITG-N 242
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEK-----SP-LSAIRlaglakeAGLPDGVLNVVTGfG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 243 TELVHPILKSGCVDVFAFIGSSGAASALRELHPRPGRLRCVFGLDAKNQAVVLQDA-DMDVAAPEILSGSLSFSGQRCTA 321
Cdd:PRK09847 225 HEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 322 IKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVInaDG-GSVLGSLVHPA 400
Cdd:PRK09847 305 GTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLL--DGrNAGLAAAIGPT 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 401 ILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNlnsQCQRGPD 480
Cdd:PRK09847 383 IFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVN---NYNDGDM 459
|
410
....*....|...
gi 648475632 481 TLPFGGRKDSAVG 493
Cdd:PRK09847 460 TVPFGGYKQSGNG 472
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
84-493 |
3.94e-32 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 129.23 E-value: 3.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARgefdrtvqyvrdTIDAlreMDGEDSRR 163
Cdd:PRK13252 50 VASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETS------------VVDI---VTGADVLE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 F--------EGDDI------LARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKlPK----IGRLLFSPIL- 224
Cdd:PRK13252 115 YyaglapalEGEQIplrggsFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFK-PSevtpLTALKLAEIYt 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 225 EAlrdCFPRGVVNVITGNTE----LV-HPIlksgcVDVFAFIGSSG--------AASALRELhprpgrlrcVFGLDAKNQ 291
Cdd:PRK13252 194 EA---GLPDGVFNVVQGDGRvgawLTeHPD-----IAKVSFTGGVPtgkkvmaaAAASLKEV---------TMELGGKSP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 292 AVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLR 371
Cdd:PRK13252 257 LIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 372 DLVDDAVSKGARVINadGGSVL-------GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQ 444
Cdd:PRK13252 337 GYIEKGKAEGARLLC--GGERLteggfanGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLA 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 648475632 445 VSLFGQNPDRLGRLVDAMSAQVCRVNLNSQCqrgPDTLPFGGRKDSAVG 493
Cdd:PRK13252 415 AGVFTADLSRAHRVIHQLEAGICWINTWGES---PAEMPVGGYKQSGIG 460
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
119-457 |
7.04e-32 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 128.90 E-value: 7.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 119 EIVRLMTLEICKPVRQARGEfdrtvqyVRDTIDAL----REM----DGEDSRRFEGDDilARVRRAPLGPVLCMGPYNFP 190
Cdd:PRK03137 114 EFSAWLVKEAGKPWAEADAD-------TAEAIDFLeyyaRQMlklaDGKPVESRPGEH--NRYFYIPLGVGVVISPWNFP 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 191 FNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEAlrdCFPRGVVNVITGNTE-----LV-HPilKSGCVdvfAF 260
Cdd:PRK03137 185 FAIMAGMTLAAIVAGNTVLLKpasdTPVIAAKFVEVLEEA---GLPAGVVNFVPGSGSevgdyLVdHP--KTRFI---TF 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 261 IGSSgaASALReLHPRPGRL--------RCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTVFVHQSRA 332
Cdd:PRK03137 257 TGSR--EVGLR-IYERAAKVqpgqiwlkRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVY 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 333 DELLERLKAGVGKLKIGMPFDPDvDITPMPEPGRAEYLRDLVDDAVSKGARVINADGGSVLGSLVHPAILYPVDSSMRVY 412
Cdd:PRK03137 334 DEVLEKVVELTKELTVGNPEDNA-YMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQPTIFADVDPKARIM 412
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 648475632 413 HEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGR 457
Cdd:PRK03137 413 QEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEK 457
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
156-510 |
1.67e-31 |
|
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: 127.08 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 156 MDGedsrrfegdDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEAlrdCF 231
Cdd:cd07141 133 MDG---------DFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKpaeqTPLTALYLASLIKEA---GF 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 232 PRGVVNVITGNTELVHPILKSGC-VDVFAFIGSSGAASALRELHPRPGRLRCVFGLDAKNQAVVLQDADMDVAApEILSG 310
Cdd:cd07141 201 PPGVVNVVPGYGPTAGAAISSHPdIDKVAFTGSTEVGKLIQQAAGKSNLKRVTLELGGKSPNIVFADADLDYAV-EQAHE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 311 SLSFS-GQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVinADG 389
Cdd:cd07141 280 ALFFNmGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKL--ECG 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 390 GSVLGS---LVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQV 466
Cdd:cd07141 358 GKRHGDkgyFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGT 437
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 648475632 467 CRVN----LNSQCqrgpdtlPFGGRKDSAVGTLSVKDGIRAFS-MRTVV 510
Cdd:cd07141 438 VWVNcynvVSPQA-------PFGGYKMSGNGRELGEYGLQEYTeVKTVT 479
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
92-493 |
1.37e-30 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 125.31 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARG-EFDRTVQYVR------DTIDALR-EMDGEDSrr 163
Cdd:PLN02466 111 GPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKaELPMFARLFRyyagwaDKIHGLTvPADGPHH-- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 fegddilARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRL--LFSPILeALRDCFPRGVVNVITG 241
Cdd:PLN02466 189 -------VQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLsaLYAAKL-LHEAGLPPGVLNVVSG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 242 NTELVHPILKSGC-VDVFAFIGSSGAASALRELHPRPGRLRCVFGLDAKNQAVVLQDADMDVAApEILSGSLSFS-GQRC 319
Cdd:PLN02466 261 FGPTAGAALASHMdVDKLAFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAV-ELAHFALFFNqGQCC 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 320 TAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVLGS---L 396
Cdd:PLN02466 340 CAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLEC--GGDRFGSkgyY 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 397 VHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNlnsqCQ 476
Cdd:PLN02466 418 IQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN----CF 493
|
410
....*....|....*...
gi 648475632 477 RGPD-TLPFGGRKDSAVG 493
Cdd:PLN02466 494 DVFDaAIPFGGYKMSGIG 511
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
92-432 |
1.56e-30 |
|
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: 123.89 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQArGEFDRTV---QYVRDTIDALREMDGEDSRRFEGDD 168
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFA-ENICGDQvqlRARAFVIYSYRIPHEPGNHLGQGLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 169 ILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC--FPRGVVNVITGNTELV 246
Cdd:cd07084 92 QQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAglLPPEDVTLINGDGKTM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 247 HPILKSGCVDVFAFIGSSGAASALReLHPRPGRLRcvFGLDAKNQAVVLQDAD-MDVAAPEILSGSLSFSGQRCTAIKTV 325
Cdd:cd07084 172 QALLLHPNPKMVLFTGSSRVAEKLA-LDAKQARIY--LELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSML 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 326 FVHQSRADE-LLERLKAGVGKLKIGMPFDPDVdITPMPEPGRAEYLRDLVDDAVSKGARVINADGGSVLGSLVHPAILYP 404
Cdd:cd07084 249 FVPENWSKTpLVEKLKALLARRKLEDLLLGPV-QTFTTLAMIAHMENLLGSVLLFSGKELKNHSIPSIYGACVASALFVP 327
|
330 340 350
....*....|....*....|....*....|.
gi 648475632 405 VDSSMR---VYHEEQFGPVVPVVPFDDDRTP 432
Cdd:cd07084 328 IDEILKtyeLVTEEIFGPFAIVVEYKKDQLA 358
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
171-510 |
8.11e-30 |
|
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: 121.56 E-value: 8.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 171 ARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEALrdcfPRGVVNVITGNTELV 246
Cdd:cd07135 102 PRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKpselTPHTAALLAELVPKYL----DPDAFQVVQGGVPET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 247 HPILKSGCVDVF----AFIGSSGAASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAI 322
Cdd:cd07135 178 TALLEQKFDKIFytgsGRVGRIIAEAAAKHLTP------VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 323 KTVFVHQSRADELLERLKAGVGKLKIGMPFDPDvDITPMPEPGRAEYLRDLVDDavSKGARVIN--ADGGSVLGSlvhPA 400
Cdd:cd07135 252 DYVLVDPSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSLLDT--TKGKVVIGgeMDEATRFIP---PT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 401 ILYPV---DSSMRvyhEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNlNSQCQR 477
Cdd:cd07135 326 IVSDVswdDSLMS---EELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVIN-DTLIHV 401
|
330 340 350
....*....|....*....|....*....|....
gi 648475632 478 GPDTLPFGGRKDSAVGTLSVKDGIRAFS-MRTVV 510
Cdd:cd07135 402 GVDNAPFGGVGDSGYGAYHGKYGFDTFThERTVV 435
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
173-517 |
1.34e-29 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 122.06 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 173 VRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDCFPRGVVNVITGNTELVHPILKS 252
Cdd:PTZ00381 105 IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIEGGVEVTTELLKE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 253 GcVDVFAFIGSSG-----AASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTVFV 327
Cdd:PTZ00381 185 P-FDHIFFTGSPRvgklvMQAAAENLTP------CTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 328 HQSRADELLERLKAGVgKLKIGmpfdpdvditpmPEPGRAE-YLRDLVDDAVSKGARVINADGGSVL--GSL------VH 398
Cdd:PTZ00381 258 HRSIKDKFIEALKEAI-KEFFG------------EDPKKSEdYSRIVNEFHTKRLAELIKDHGGKVVygGEVdienkyVA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 399 PAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNlNSQCQRG 478
Cdd:PTZ00381 325 PTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN-DCVFHLL 403
|
330 340 350
....*....|....*....|....*....|....*....
gi 648475632 479 PDTLPFGGRKDSAVGTLSVKDGIRAFSMRTVVASKNTDN 517
Cdd:PTZ00381 404 NPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGN 442
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
92-493 |
1.47e-29 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 121.85 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARG-EFDRTVQYVRDTIDALREMDGED---SRRFEGD 167
Cdd:PLN02766 74 GPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETlkmSRQLQGY 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 168 DIlarvrRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRL--LFSPILeALRDCFPRGVVNVITGNTEL 245
Cdd:PLN02766 154 TL-----KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLsaLFYAHL-AKLAGVPDGVINVVTGFGPT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 246 VHPILKSGC-VDVFAFIGSSGAASALRELHPRPGRLRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKT 324
Cdd:PLN02766 228 AGAAIASHMdVDKVSFTGSTEVGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 325 VFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVLGS---LVHPAI 401
Cdd:PLN02766 308 VYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLT--GGKPCGDkgyYIEPTI 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 402 LYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNlnsqCQRGPDT 481
Cdd:PLN02766 386 FTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN----CYFAFDP 461
|
410
....*....|...
gi 648475632 482 -LPFGGRKDSAVG 493
Cdd:PLN02766 462 dCPFGGYKMSGFG 474
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
95-517 |
2.42e-29 |
|
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: 120.77 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 95 PAMTQGERIRHLEcflERMVAEGDEIVRLMTLEICKPVRQARGEfdrtVQYVRDTID---ALremdgedSRRFEGDdILA 171
Cdd:cd07130 54 PAPKRGEIVRQIG---DALRKKKEALGKLVSLEMGKILPEGLGE----VQEMIDICDfavGL-------SRQLYGL-TIP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 172 RVRRA--------PLGPVLCMGPYNFP-----FNetfATLipALLMGNTAVVK-LPKIGRL------LFSPILEalRDCF 231
Cdd:cd07130 119 SERPGhrmmeqwnPLGVVGVITAFNFPvavwgWN---AAI--ALVCGNVVVWKpSPTTPLTaiavtkIVARVLE--KNGL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 232 PRGVVNVITGNTELVHPILKSGCVDVFAFIGSS--GAASALReLHPRPGRlrCVFGLDAKNQAVVLQDADMDVAAPEILS 309
Cdd:cd07130 192 PGAIASLVCGGADVGEALVKDPRVPLVSFTGSTavGRQVGQA-VAARFGR--SLLELGGNNAIIVMEDADLDLAVRAVLF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 310 GSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadG 389
Cdd:cd07130 269 AAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLF--G 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 390 GSVL---GSLVHPAILYPvDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQV 466
Cdd:cd07130 347 GKVIdgpGNYVEPTIVEG-LSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSDC 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 648475632 467 CRVNLN---SQCQRGPdtlPFGGRKDSAVGTLSVKDGIRAFsMRTvvaSKNTDN 517
Cdd:cd07130 426 GIVNVNigtSGAEIGG---AFGGEKETGGGRESGSDAWKQY-MRR---STCTIN 472
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
94-486 |
3.44e-29 |
|
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71), the fourth enzyme in the arginine succinyltransferase (AST) pathway for arginine catabolism. [Energy metabolism, Amino acids and amines]
Pssm-ID: 274486 Cd Length: 484 Bit Score: 120.59 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 94 WPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALREMDGEdsRRFEGDDILARV 173
Cdd:TIGR03240 51 WARLSLEERIAVVQRFAALLEERKEALARVIARETGKPLWETRTEVASMIGKVAISIKAYHERTGE--SENPMPDGRAVL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 174 RRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLlfspILEALRDC-FPRGVVNVITGNTELVHP 248
Cdd:TIGR03240 129 RHRPHGVVAVFGPYNFPGHLPNGHIVPALIAGNTVVFKpselTPWVAEE----TVKLWEKAgLPAGVLNLVQGARETGVA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 249 ILKSGCVDVFAFIGSSGAASAL-RELHPRPGRlrcVFGLD--AKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTV 325
Cdd:TIGR03240 205 LAAHPQIDGLLFTGSSNTGTLLhRQFGGRPEK---ILALEmgGNNPLIVDEVADIDAAVHHIIQSAFISAGQRCTCARRL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 326 FVHQS-RADELLERLKAGVGKLKIGMpFDPDvditpmPEP-------GRA-EYLRDLVDDAVSKGAR-VINADGGSVLGS 395
Cdd:TIGR03240 282 LVPDGaQGDAFLARLVEVAERLTVGA-WDAE------PQPfmgavisLRAaQRLLAAQAKLLALGGKsLLEMRQLDPGAA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 396 LVHPAILyPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVcrVNLNSQC 475
Cdd:TIGR03240 355 FLTPGII-DVTGVAELPDEEHFGPLLQVIRYTDFDEAIAIANNTRFGLSAGLLSDDRELYDRFLLEIRAGI--VNWNKPL 431
|
410
....*....|.
gi 648475632 476 QRGPDTLPFGG 486
Cdd:TIGR03240 432 TGASSAAPFGG 442
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
170-493 |
1.32e-27 |
|
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: 116.06 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 170 LARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILE-ALRDCFPRGVVNVITGNTELV-- 246
Cdd:cd07140 140 LTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAElTVKAGFPKGVINILPGSGSLVgq 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 247 ----HPILK----SGCVDVFAFIGSSGAASALRelhprpgrlRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQR 318
Cdd:cd07140 220 rlsdHPDVRklgfTGSTPIGKHIMKSCAVSNLK---------KVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGEN 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 319 CTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVL---GS 395
Cdd:cd07140 291 CIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVY--GGKQVdrpGF 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 396 LVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDD-DRTPVEYQAQ-SDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNLNS 473
Cdd:cd07140 369 FFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgDVDGVLQRANdTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYN 448
|
330 340
....*....|....*....|
gi 648475632 474 QCQRGPdtlPFGGRKDSAVG 493
Cdd:cd07140 449 KTDVAA---PFGGFKQSGFG 465
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
84-516 |
9.60e-26 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 111.38 E-value: 9.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTID-ALREMDGEDSR 162
Cdd:PLN02419 157 VSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGmATLQMGEYLPN 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 163 RFEGDDILARvrRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKL----PKIGRLLFSPILEAlrdCFPRGVVNV 238
Cdd:PLN02419 237 VSNGVDTYSI--REPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPsekdPGASVILAELAMEA---GLPDGVLNI 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 239 ITGNTELVHPILKSGCVDVFAFIGSSGAASALRELHPRPGRlRCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQR 318
Cdd:PLN02419 312 VHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGK-RIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQR 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 319 CTAIKT-VFVHQSRA--DELLERLKAgvgkLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVInADGGSVL-- 393
Cdd:PLN02419 391 CMALSTvVFVGDAKSweDKLVERAKA----LKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLL-LDGRDIVvp 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 394 ----GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLvdAMSAQVCRV 469
Cdd:PLN02419 466 gyekGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKF--QMDIEAGQI 543
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 648475632 470 NLNSQCqrgPDTLP---FGGRKDSAVGTLSV--KDGIRAFSMRTVVASKNTD 516
Cdd:PLN02419 544 GINVPI---PVPLPffsFTGNKASFAGDLNFygKAGVDFFTQIKLVTQKQKD 592
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
171-514 |
2.41e-25 |
|
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: 108.75 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 171 ARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKigrllFSP-----ILEALRDCFPRGVVNVITGNTEL 245
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSE-----LTPntskvIAKIIEETFDEEYVAVVEGGVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 246 VHPILKSgCVDVFAFIGSSG-----AASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCT 320
Cdd:cd07136 169 NQELLDQ-KFDYIFFTGSVRvgkivMEAAAKHLTP------VTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 321 AIKTVFVHQSRADELLERLKAGVGKLKIGMPFDpdvditpMPEPGRA------EYLRDLVDDavskgARVINADGGSVLG 394
Cdd:cd07136 242 APDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-------SPDYGRIinekhfDRLAGLLDN-----GKIVFGGNTDRET 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 395 SLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMS-AQVCrVNlns 473
Cdd:cd07136 310 LYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSfGGGC-IN--- 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 648475632 474 qcqrgpDT--------LPFGGRKDSAVGTLSVKDGIRAFS-MRTVVASKN 514
Cdd:cd07136 386 ------DTimhlanpyLPFGGVGNSGMGSYHGKYSFDTFShKKSILKKST 429
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
92-493 |
2.62e-23 |
|
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: 103.43 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 92 GEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEfdrtvqyVRDTIDALR----EMDGEDSRRFEGD 167
Cdd:cd07125 83 AGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAE-------VREAIDFCRyyaaQARELFSDPELPG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 168 DI--LARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC-FPRGVVNVITGNTE 244
Cdd:cd07125 156 PTgeLNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAgVPRDVLQLVPGDGE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 245 LV-HPILKSGCVDVFAFIGSSGAASA-LRELHPRPGRLRCVF----GldaKNQAVVLQDADMDVAAPEILSGSLSFSGQR 318
Cdd:cd07125 236 EIgEALVAHPRIDGVIFTGSTETAKLiNRALAERDGPILPLIaetgG---KNAMIVDSTALPEQAVKDVVQSAFGSAGQR 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 319 CTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVdDAVSKGARVI-NADGGSVLGSLV 397
Cdd:cd07125 313 CSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHT-ELMRGEAWLIaPAPLDDGNGYFV 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 398 HPAILYPVDSSmrVYHEEQFGPVVPVVPFDDDRTP--VEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNLN--- 472
Cdd:cd07125 392 APGIIEIVGIF--DLTTEVFGPILHVIRFKAEDLDeaIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNitg 469
|
410 420
....*....|....*....|....*
gi 648475632 473 ----SQcqrgpdtlPFGGRKDSAVG 493
Cdd:cd07125 470 aivgRQ--------PFGGWGLSGTG 486
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
95-493 |
7.64e-23 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 101.83 E-value: 7.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 95 PAMTQGERIRHLEcflERMVAEGDEIVRLMTLEICKPVRQARGEfdrtVQYVRDTIDAL----REMDGEDSRRFEGDDIL 170
Cdd:PLN02315 76 PAPKRGEIVRQIG---DALRAKLDYLGRLVSLEMGKILAEGIGE----VQEIIDMCDFAvglsRQLNGSIIPSERPNHMM 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 171 ARVRRaPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEAL-RDCFPRGVVNVITGNTEL 245
Cdd:PLN02315 149 MEVWN-PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKgaptTPLITIAMTKLVAEVLeKNNLPGAIFTSFCGGAEI 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 246 VHPILKSGCVDVFAFIGSSGAASALRE-LHPRPGRlrCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKT 324
Cdd:PLN02315 228 GEAIAKDTRIPLVSFTGSSKVGLMVQQtVNARFGK--CLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 325 VFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVINadGGSVL---GSLVHPAI 401
Cdd:PLN02315 306 LLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILT--GGSAIeseGNFVQPTI 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 402 LyPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNLNSQCQRGPDT 481
Cdd:PLN02315 384 V-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIG 462
|
410
....*....|..
gi 648475632 482 LPFGGRKDSAVG 493
Cdd:PLN02315 463 GAFGGEKATGGG 474
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
84-430 |
1.27e-22 |
|
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: 101.12 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVR-DTIDALREMD----- 157
Cdd:cd07083 61 LEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRyYARAALRLRYpavev 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 158 ----GEDSRRFegddilarvrRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC-FP 232
Cdd:cd07083 141 vpypGEDNESF----------YVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFP 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 233 RGVVNVITGNTELV------HPILKSGCvdvfaFIGSSGAA----SALRELHPRPGRLRCVFG-LDAKNQAVVLQDADMD 301
Cdd:cd07083 211 PGVVQFLPGVGEEVgaylteHERIRGIN-----FTGSLETGkkiyEAAARLAPGQTWFKRLYVeTGGKNAIIVDETADFE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 302 VAAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKG 381
Cdd:cd07083 286 LVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 648475632 382 ARVInadGGSVL---GSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDR 430
Cdd:cd07083 366 QLVL---GGKRLegeGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDD 414
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
84-493 |
2.98e-21 |
|
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: 96.90 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMtleickpVRQARGEFDRTVQYVRDTIDALREMDGEdsrr 163
Cdd:TIGR01238 80 IDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALC-------VREAGKTIHNAIAEVREAVDFCRYYAKQ---- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 feGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC-FPRGVVNVITGN 242
Cdd:TIGR01238 149 --VRDVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 243 TELVHPILKS-GCVDVFAFIGSSGAASAL-RELHPR---PGRLRCVFGldAKNQAVVLQDADMDVAAPEILSGSLSFSGQ 317
Cdd:TIGR01238 227 GADVGAALTSdPRIAGVAFTGSTEVAQLInQTLAQRedaPVPLIAETG--GQNAMIVDSTALPEQVVRDVLRSAFDSAGQ 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 318 RCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARV----INADGGSVL 393
Cdd:TIGR01238 305 RCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIaqltLDDSRACQH 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 394 GSLVHPaILYPVDsSMRVYHEEQFGPVVPVVPFDDDRTP--VEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNL 471
Cdd:TIGR01238 385 GTFVAP-TLFELD-DIAELSEEVFGPVLHVVRYKARELDqiVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNR 462
|
410 420
....*....|....*....|..
gi 648475632 472 NsQCQRGPDTLPFGGRKDSAVG 493
Cdd:TIGR01238 463 N-QVGAVVGVQPFGGQGLSGTG 483
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
93-429 |
3.36e-20 |
|
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: 93.37 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEFDRTVQYVRDTIDALRE-------MDGEDSRRFE 165
Cdd:cd07129 14 SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgswldarIDPADPDRQP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 166 GD--DIlaRVRRAPLGPVLCMGPYNFPFneTFATL----IPALLMGNTAVVKL----PKIGRLLFSPILEALRDC-FPRG 234
Cdd:cd07129 94 LPrpDL--RRMLVPLGPVAVFGASNFPL--AFSVAggdtASALAAGCPVVVKAhpahPGTSELVARAIRAALRATgLPAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 235 VVNVITGN-----TELV-HPILKSGcvdvfAFIGSSGAASALREL-----HPRPgrlrcVFG-LDAKNQAVVLQDAdMDV 302
Cdd:cd07129 170 VFSLLQGGgrevgVALVkHPAIKAV-----GFTGSRRGGRALFDAaaarpEPIP-----FYAeLGSVNPVFILPGA-LAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 303 AAPEI---LSGSLSF-SGQRCTAIKTVFVHQSRA-DELLERLKAGVGKLKIGmpfdpdvditPMPEPGRAEYLRDLVDDA 377
Cdd:cd07129 239 RGEAIaqgFVGSLTLgAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQ----------TMLTPGIAEAYRQGVEAL 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 648475632 378 VSKGARVINADGGSVLGSLVHPAILYPVDSSM----RVYHEEQFGPVVPVVPFDDD 429
Cdd:cd07129 309 AAAPGVRVLAGGAAAEGGNQAAPTLFKVDAAAfladPALQEEVFGPASLVVRYDDA 364
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
157-473 |
4.07e-19 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 90.53 E-value: 4.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 157 DGEDSR-----RFEGDDILARVRraplGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC- 230
Cdd:PRK11903 127 DGEAVQlgkdpAFQGQHVLVPTR----GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAg 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 231 -FPRGVVNVITGNTELVHPILKSGcvDVFAFIGSSGAASALReLHPRPGR--LRCVFGLDAKNQAVVLQDADMDVAAPEI 307
Cdd:PRK11903 203 iLPAGALSVVCGSSAGLLDHLQPF--DVVSFTGSAETAAVLR-SHPAVVQrsVRVNVEADSLNSALLGPDAAPGSEAFDL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 308 LSGSLSF-----SGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMpePGRAEY------LRDLVDD 376
Cdd:PRK11903 280 FVKEVVRemtvkSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPL--VSRAQLaavragLAALRAQ 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 377 A--VSKGARVINADGGSVLGSLVHPAILY--PVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNP 452
Cdd:PRK11903 358 AevLFDGGGFALVDADPAVAACVGPTLLGasDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDA 437
|
330 340
....*....|....*....|.
gi 648475632 453 DRLGRLVDAMSAQVCRVNLNS 473
Cdd:PRK11903 438 AFLAAAALELADSHGRVHVIS 458
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
84-493 |
4.71e-19 |
|
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: 89.82 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARG-EFDRTVQYVRDTIDALREMDGEDSR 162
Cdd:cd07116 44 LDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSISE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 163 RfeGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDCFPRGVVNVITG- 241
Cdd:cd07116 124 I--DENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGf 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 242 NTELVHPILKSGCVDVFAFIGSSGAAS-----ALRELHPRP----GRLRCVFGLDAKNQavvlQDADMDVAapeiLSGSL 312
Cdd:cd07116 202 GLEAGKPLASSKRIAKVAFTGETTTGRlimqyASENIIPVTlelgGKSPNIFFADVMDA----DDAFFDKA----LEGFV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 313 SF---SGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARVI---- 385
Cdd:cd07116 274 MFalnQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLtgge 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 386 -NADGGSVLGSLVHPAILYPvDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMsa 464
Cdd:cd07116 354 rNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGI-- 430
|
410 420 430
....*....|....*....|....*....|
gi 648475632 465 QVCRVNLNsqCQRG-PDTLPFGGRKDSAVG 493
Cdd:cd07116 431 QAGRVWTN--CYHLyPAHAAFGGYKQSGIG 458
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
102-505 |
1.18e-17 |
|
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: 85.35 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 102 RIRHLECfLERMVAEG-DEIVRLMTLEICKPVRQA-RGEFDRTVQYVRDTIDALRE-MDGED-SRRF--EGDDilARVRR 175
Cdd:cd07132 22 RIQQLEA-LLRMLEENeDEIVEALAKDLRKPKFEAvLSEILLVKNEIKYAISNLPEwMKPEPvKKNLatLLDD--VYIYK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 176 APLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEAL-RDCFPrgvvnVITGNTELVHPIL 250
Cdd:cd07132 99 EPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKpsevSPATAKLLAELIPKYLdKECYP-----VVLGGVEETTELL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 251 KSGCVDVFaFIGSSG-----AASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSFSGQRCTAIKTV 325
Cdd:cd07132 174 KQRFDYIF-YTGSTSvgkivMQAAAKHLTP------VTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 326 FVHQSRADELLERLKAGV----GKlkigmpfdpdvDITPMPEPGR---AEYLRDLVddAVSKGARVinADGGSVLGS--L 396
Cdd:cd07132 247 LCTPEVQEKFVEALKKTLkefyGE-----------DPKESPDYGRiinDRHFQRLK--KLLSGGKV--AIGGQTDEKerY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 397 VHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNlNSQCQ 476
Cdd:cd07132 312 IAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVN-DTIMH 390
|
410 420
....*....|....*....|....*....
gi 648475632 477 RGPDTLPFGGRKDSAVGTLSVKDGIRAFS 505
Cdd:cd07132 391 YTLDSLPFGGVGNSGMGAYHGKYSFDTFS 419
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
172-430 |
1.94e-14 |
|
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: 75.70 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 172 RVRRAPL-GPVLCMGPYNFpfnetfaTLI-------PALlMGNTAVVKlPKIGRLLFSPIL-EALRDC-FPRGVVNVITG 241
Cdd:cd07123 164 RLEYRPLeGFVYAVSPFNF-------TAIggnlagaPAL-MGNVVLWK-PSDTAVLSNYLVyKILEEAgLPPGVINFVPG 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 242 NTELV-HPILKSGCVDVFAFIGSSG--------AASALRELHPRPgrlRCVFGLDAKNQAVVLQDADMDVAAPEILSGSL 312
Cdd:cd07123 235 DGPVVgDTVLASPHLAGLHFTGSTPtfkslwkqIGENLDRYRTYP---RIVGETGGKNFHLVHPSADVDSLVTATVRGAF 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 313 SFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGmpfDPDVDITPM-PEPGRAEYLR--DLVDDA-VSKGARVInAD 388
Cdd:cd07123 312 EYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMG---DPDDFSNFMgAVIDEKAFDRikGYIDHAkSDPEAEII-AG 387
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 648475632 389 G---GSVlGSLVHPAILYPVDSSMRVYHEEQFGPVVPVVPFDDDR 430
Cdd:cd07123 388 GkcdDSV-GYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSD 431
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
171-510 |
3.46e-14 |
|
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: 74.75 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 171 ARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK----LPKIGRLLFSPILEALRDcfprGVVNVITGNTELV 246
Cdd:cd07137 95 AEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKpselAPATSALLAKLIPEYLDT----KAIKVIEGGVPET 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 247 HPILKSGCVDVFaFIGSSGA-----ASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDVAAPEILSGSL-SFSGQRCT 320
Cdd:cd07137 171 TALLEQKWDKIF-FTGSPRVgriimAAAAKHLTP------VTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 321 AIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDvDITPMPEPGRAEYLRDLVDDAvSKGARVINadGGSVLGS--LVH 398
Cdd:cd07137 244 APDYVLVEESFAPTLIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLDDP-SVADKIVH--GGERDEKnlYIE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 399 PAILY--PVDSSMRVyhEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNlNSQCQ 476
Cdd:cd07137 320 PTILLdpPLDSSIMT--EEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFN-DTVVQ 396
|
330 340 350
....*....|....*....|....*....|....
gi 648475632 477 RGPDTLPFGGRKDSAVGTLSVKDGIRAFSMRTVV 510
Cdd:cd07137 397 YAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
171-510 |
3.83e-13 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 71.68 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 171 ARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKigrllFSPILEA-LRDCFPR----GVVNVITGNTEL 245
Cdd:PLN02203 102 AEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSE-----LAPATSAfLAANIPKyldsKAVKVIEGGPAV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 246 VHPILKSGCVDVFaFIGSSGA-----ASALRELHPRP----GRLRCVF-GLDAKNqavvlqdaDMDVAAPEILSGSLSF- 314
Cdd:PLN02203 177 GEQLLQHKWDKIF-FTGSPRVgriimTAAAKHLTPVAlelgGKCPCIVdSLSSSR--------DTKVAVNRIVGGKWGSc 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 315 SGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDvDITPMPEPGRAEYLRDLVDDAVSKGARVinaDGGSVLG 394
Cdd:PLN02203 248 AGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVAASIV---HGGSIDE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 395 S--LVHPAILY--PVDSSmrVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVN 470
Cdd:PLN02203 324 KklFIEPTILLnpPLDSD--IMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFN 401
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 648475632 471 lNSQCQRGPDTLPFGGRKDSAVGTLSVKDGIRAFSMRTVV 510
Cdd:PLN02203 402 -DAIIQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
187-473 |
3.91e-13 |
|
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: 71.53 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 187 YNFP---FNETFAtliPALLMGNTAVVKlPK-----IGRLLFSPILEAlrDCFPRGVVNVITGNTE--LVHpilkSGCVD 256
Cdd:cd07128 154 FNFPvwgMLEKFA---PALLAGVPVIVK-PAtatayLTEAVVKDIVES--GLLPEGALQLICGSVGdlLDH----LGEQD 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 257 VFAFIGSSGAASALReLHPRPGRLRCVFGLDAK--NQAVVLQDA-----DMDVAAPEILSGSLSFSGQRCTAIKTVFVHQ 329
Cdd:cd07128 224 VVAFTGSAATAAKLR-AHPNIVARSIRFNAEADslNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFVPE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 330 SRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVdDAVSKGARVINADGGSVL--------GSLVHPAI 401
Cdd:cd07128 303 ARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPDRFEvvgadaekGAFFPPTL 381
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648475632 402 LY--PVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYqAQSDFGQQV-SLFGQNPDRLGRLVDAMSAQVCRVNLNS 473
Cdd:cd07128 382 LLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIEL-AARGRGSLVaSVVTNDPAFARELVLGAAPYHGRLLVLN 455
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
93-429 |
4.42e-13 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 72.20 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 93 EWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEfdrtvqyVRDTIDALREMDGEDSRRFEGDdilar 172
Cdd:PRK11905 605 EWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE-------VREAVDFLRYYAAQARRLLNGP----- 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 173 vRRAPLGPVLCMGPYNFP---FNETFATlipALLMGNTAVVK----LPKIG----RLLFSPILealrdcfPRGVVNVITG 241
Cdd:PRK11905 673 -GHKPLGPVVCISPWNFPlaiFTGQIAA---ALVAGNTVLAKpaeqTPLIAaravRLLHEAGV-------PKDALQLLPG 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 242 NTELV-HPILKSGCVDVFAFIGSSGAASAL-RELHPRPGRLrcvfgldaknqaVVL------QDAdMDV---AAPE---- 306
Cdd:PRK11905 742 DGRTVgAALVADPRIAGVMFTGSTEVARLIqRTLAKRSGPP------------VPLiaetggQNA-MIVdssALPEqvva 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 307 -ILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAEYLRDLVDDAVSKGARV- 384
Cdd:PRK11905 809 dVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVh 888
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 648475632 385 -INADGGSVLGSLVHPAIlYPVDsSMRVYHEEQFGPVVPVVPFDDD 429
Cdd:PRK11905 889 qLPLPAETEKGTFVAPTL-IEID-SISDLEREVFGPVLHVVRFKAD 932
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
84-427 |
1.04e-12 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 71.00 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 84 VDAYGRGLGEWPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEfdrtvqyVRDTIDALREMDGEDSRR 163
Cdd:PRK11904 591 LAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAE-------VREAVDFCRYYAAQARRL 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 164 FEGDDILA-------RVRRAPLGPVLCMGPYNFPFnETFATLIPALLM-GNTAVVK----LPKIG----RLLFspilEAl 227
Cdd:PRK11904 664 FGAPEKLPgptgesnELRLHGRGVFVCISPWNFPL-AIFLGQVAAALAaGNTVIAKpaeqTPLIAaeavKLLH----EA- 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 228 rdCFPRGVVNVITGNTELV-HPILKSGCVDVFAFIGSSGAASAL-RELHPRPGRLrcvfgldaknqaVVL------QDAd 299
Cdd:PRK11904 738 --GIPKDVLQLLPGDGATVgAALTADPRIAGVAFTGSTETARIInRTLAARDGPI------------VPLiaetggQNA- 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 300 MDV---AAPE------ILSgslSF--SGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEPGRAE 368
Cdd:PRK11904 803 MIVdstALPEqvvddvVTS---AFrsAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKA 879
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648475632 369 YLRDLVdDAVSKGARVINA---DGGSVLGSLVHPAIlYPVDsSMRVYHEEQFGPVVPVVPFD 427
Cdd:PRK11904 880 NLDAHI-ERMKREARLLAQlplPAGTENGHFVAPTA-FEID-SISQLEREVFGPILHVIRYK 938
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
175-437 |
1.16e-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: 70.22 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 175 RAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVKLPKIGRLLFSPILEALRDC-FPRGVVNVITGNTELVHPILKSG 253
Cdd:cd07126 140 RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCgMPATDVDLIHSDGPTMNKILLEA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 254 CVDVFAFIGSSGAASAL-RELHprpGRLRC--------VFGLDAKNQAVVLQDADMDVAApeilsgslsFSGQRCTAIKT 324
Cdd:cd07126 220 NPRMTLFTGSSKVAERLaLELH---GKVKLedagfdwkILGPDVSDVDYVAWQCDQDAYA---------CSGQKCSAQSI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 325 VFVHQSRADE-LLERLKAGVGKLKIgmpfdPDVDITPMPEpGRAEYLRDLVDDAVS-KGARVI-------NADGGSVLGS 395
Cdd:cd07126 288 LFAHENWVQAgILDKLKALAEQRKL-----EDLTIGPVLT-WTTERILDHVDKLLAiPGAKVLfggkpltNHSIPSIYGA 361
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 648475632 396 LVHPAILYPVDSSMRVYH-----EEQFGPVVPVVPFDDDRTPVEYQA 437
Cdd:cd07126 362 YEPTAVFVPLEEIAIEENfelvtTEVFGPFQVVTEYKDEQLPLVLEA 408
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
171-510 |
4.84e-11 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 65.07 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 171 ARVRRAPLGPVLCMGPYNFPFNETFATLIPALLMGNTAVVK---LPKIGRLLFSPILEALRDcfpRGVVNVITGNTELVH 247
Cdd:PLN02174 106 AEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKpseLAPASSALLAKLLEQYLD---SSAVRVVEGAVTETT 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 248 PILKSGCVDVFaFIGSSG-----AASALRELHPrpgrlrCVFGLDAKNQAVVLQDADMDVAAPEILSGSLSF-SGQRCTA 321
Cdd:PLN02174 183 ALLEQKWDKIF-YTGSSKigrviMAAAAKHLTP------VVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACIS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 322 IKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDvDITPMPEPGRAEYLRDLVDDAvSKGARVINADGGSVLGSLVHPAI 401
Cdd:PLN02174 256 PDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLDEK-EVSDKIVYGGEKDRENLKIAPTI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 402 LYPVDSSMRVYHEEQFGPVVPVVPFDDDRTPVEYQAQSDFGQQVSLFGQNPDRLGRLVDAMSAQVCRVNlNSQCQRGPDT 481
Cdd:PLN02174 334 LLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVN-DIAVHLALHT 412
|
330 340
....*....|....*....|....*....
gi 648475632 482 LPFGGRKDSAVGTLSVKDGIRAFSMRTVV 510
Cdd:PLN02174 413 LPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
132-426 |
1.86e-10 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 63.84 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 132 VRQARGEFDRTVQYVRDTIDALREMDGEDSRRFEGDdilarVRRaPLGPVLCMGPYNFP---FNETFATlipALLMGNTA 208
Cdd:PRK11809 729 VREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDND-----THR-PLGPVVCISPWNFPlaiFTGQVAA---ALAAGNSV 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 209 VVKLPKIGRLLFSPILEALRDC-FPRGVVNVITGNTELVHPIL-KSGCVDVFAFIGSSGAASAL-RELHPRpgrlrcvfg 285
Cdd:PRK11809 800 LAKPAEQTPLIAAQAVRILLEAgVPAGVVQLLPGRGETVGAALvADARVRGVMFTGSTEVARLLqRNLAGR--------- 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 286 LDAKNQAVVL------QDAdMDV---AAPE-----ILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMP 351
Cdd:PRK11809 871 LDPQGRPIPLiaetggQNA-MIVdssALTEqvvadVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNP 949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 352 FDPDVDITP-MPEPGRAEYLRDlVDDAVSKGARV----INADGGSVLGSLVHPAiLYPVDSSMRVyHEEQFGPVVPVVPF 426
Cdd:PRK11809 950 DRLSTDIGPvIDAEAKANIERH-IQAMRAKGRPVfqaaRENSEDWQSGTFVPPT-LIELDSFDEL-KREVFGPVLHVVRY 1026
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
94-427 |
3.90e-10 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 62.65 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 94 WPAMTQGERIRHLECFLERMVAEGDEIVRLMTLEICKPVRQARGEfdrtvqyVRDTIDALREMDGEDSRRFEGDDILArv 173
Cdd:COG4230 609 WSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAE-------VREAVDFCRYYAAQARRLFAAPTVLR-- 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 174 rraPLGPVLCMGPYNFPfnetfatL-------IPALLMGNTAVVK----LPKIGRLLFSPILEAlrdCFPRGVVNVITGN 242
Cdd:COG4230 680 ---GRGVFVCISPWNFP-------LaiftgqvAAALAAGNTVLAKpaeqTPLIAARAVRLLHEA---GVPADVLQLLPGD 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 243 TELV-HPILKSGCVDVFAFIGSSGAASAL-RELHPRPGRLrcvfgldaknqaVVL------QDAdMDV---AAPE----- 306
Cdd:COG4230 747 GETVgAALVADPRIAGVAFTGSTETARLInRTLAARDGPI------------VPLiaetggQNA-MIVdssALPEqvvdd 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 307 -ILSGSLSfSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDPDVDITPMPEpgrAEYLRDLVD--DAVSKGAR 383
Cdd:COG4230 814 vLASAFDS-AGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVID---AEARANLEAhiERMRAEGR 889
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 648475632 384 VI---NADGGSVLGSLVHPAiLYPVDsSMRVYHEEQFGPVVPVVPFD 427
Cdd:COG4230 890 LVhqlPLPEECANGTFVAPT-LIEID-SISDLEREVFGPVLHVVRYK 934
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
148-403 |
7.68e-06 |
|
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: 48.37 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 148 DTIDALREMDGEDSR---RFEGDDILARVRRAPLGPVLCMGPYNFPFNETFATLIpALLMGNTAVVKL-------PKIGR 217
Cdd:cd07077 68 KNIDTERGITASVGHiqdVLLPDNGETYVRAFPIGVTMHILPSTNPLSGITSALR-GIATRNQCIFRPhpsapftNRALA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 218 LLFSPILEAlrdcFPR--GVVNVITGNTELVHPILKSGCVDVFAFIGSSGAASALRelhpRPGRLRCVFGLDAKNQAVVL 295
Cdd:cd07077 147 LLFQAADAA----HGPkiLVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAV----KHSPHIPVIGFGAGNSPVVV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648475632 296 QDADMDVAAPEILSGSLSFSGQRCTAIKTVFVHQSRADELLERLKAGVGKLKIGMPFDP---DVDITPMPEPGRAEYLRD 372
Cdd:cd07077 219 DETADEERASGSVHDSKFFDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETkplSKETTPSFDDEALESMTP 298
|
250 260 270
....*....|....*....|....*....|....*....
gi 648475632 373 L--------VDDAVSKGARVINADGGSvlgslvHPAILY 403
Cdd:cd07077 299 LecqfrvldVISAVENAWMIIESGGGP------HTRCVY 331
|
|
| |
