|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
40-503 |
0e+00 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 912.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 40 VKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQ-------------KEI 106
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQvmfkfrqlleenlDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 107 AKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMA 186
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 187 MVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKR 266
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 267 VQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVG-EAKKWLPELVEHAKNLRVNAGDQPGADLGPL 345
Cdd:cd07085 241 VQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGdEADEWIPKLVERAKKLKVGAGDDPGADMGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 346 ITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIV 425
Cdd:cd07085 321 ISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515870065 426 NNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 503
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVPLAFFSFGGWKGSFFGDLHFYGKDGVRFYTQTKTVTSRW 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
40-503 |
0e+00 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 857.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 40 VKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQ-------------KEI 106
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSvllryqallkehrDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 107 AKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMA 186
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 187 MVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKR 266
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 267 VQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLI 346
Cdd:TIGR01722 241 VQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAADEWVPEIRERAEKIRIGPGDDPGAEMGPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 347 TPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVN 426
Cdd:TIGR01722 321 TPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALIN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515870065 427 NNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQW 503
Cdd:TIGR01722 401 ASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPVPLPYFSFTGWKDSFFGDHHIYGKQGTHFYTRGKTVTTRW 477
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
38-519 |
0e+00 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 645.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 38 PTVKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQ----------KEIA 107
Cdd:PLN02419 112 PRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRvmlkfqelirKNMD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 108 KL---ITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFP 184
Cdd:PLN02419 192 KLamnITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 185 MAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHG 264
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 265 KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGP 344
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 345 LITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQI 424
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 425 VNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWK 504
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKLVTQKQK 591
|
490
....*....|....*
gi 515870065 505 EEDATLSspaVVMPT 519
Cdd:PLN02419 592 DIHSPFS---LAIPI 603
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
38-503 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 530.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 38 PTVKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSV-------------LSRQQK 104
Cdd:COG1012 4 PEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPaeraaillraadlLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 105 EIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFP 184
Cdd:COG1012 84 ELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 185 MAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRH 263
Cdd:COG1012 164 PALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDgSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 264 GKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAGDQPGADL 342
Cdd:COG1012 244 LKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESiYDEFVERLVAAAKALKVGDPLDPGTDM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 343 GPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVkgyENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAI 422
Cdd:COG1012 324 GPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDG---EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 423 QIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDtnFYGKQGIQFYTQLKTITSQ 502
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQAPFGGVKQSGIGR--EGGREGLEEYTETKTVTIR 478
|
.
gi 515870065 503 W 503
Cdd:COG1012 479 L 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
48-499 |
1.29e-168 |
|
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: 484.73 E-value: 1.29e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 48 FVESKSDKwIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSV-------------LSRQQKEIAKLITLEQ 114
Cdd:pfam00171 1 WVDSESET-IEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAaeraailrkaadlLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 115 GKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFL 194
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 195 MKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGA 273
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSgAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 274 KNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAK 351
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSR-LLVHEsiYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 352 ERVCNLIDSGTKEGASILLDGRKikvkGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYG 431
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGEA----GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515870065 432 NGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 499
Cdd:pfam00171 394 LAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGLPFGGFKQSGFGREG--GPYGLEEYTEVKTV 459
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
43-500 |
1.04e-128 |
|
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: 383.62 E-value: 1.04e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 43 FIGGKFVESKSDKWIDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTS-------------VLSRQQKEIAK 108
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPaprraeylfraaeLLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 109 LITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMV 188
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 189 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 267
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 268 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL-VGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLI 346
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVhESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 347 TPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVN 426
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 427 NNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPI---PVPLPmF-----SFTGSRSSfrgdtnfyGKQGIQFYTQLKT 498
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTigaEVHLP-FggvkkSGNGHREA--------GTTALDAFTEWKA 472
|
..
gi 515870065 499 IT 500
Cdd:cd07131 473 VY 474
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
80-500 |
1.92e-126 |
|
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: 376.16 E-value: 1.92e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 80 DAAIASCKRAFPAWADTS-------------VLSRQQKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGET 146
Cdd:cd07078 1 DAAVAAARAAFKAWAALPpaeraailrkladLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 147 MPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIH 226
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 227 G-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCM 305
Cdd:cd07078 161 GdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 306 ALStAVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGrkiKVKGYENG 383
Cdd:cd07078 241 AAS-RLLVHEsiYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGG---KRLEGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 384 NFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIP 463
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 515870065 464 VPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 500
Cdd:cd07078 397 GAEPSAPFGGVKQS--GIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
43-499 |
3.79e-117 |
|
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: 353.86 E-value: 3.79e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 43 FIGGKFVESKSDKwiDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQ-------------KEIAK 108
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADildkagdelearkEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 109 LITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMV 188
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 189 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 267
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 268 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLV-GEAKKWLPELVEHAKNLRVNAGDQPGADLGPLI 346
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTeGIHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 347 TPQAKERVCNLIDSGTKEGASILLDGRKIkvKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVN 426
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAKLVYGGERL--KRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 427 NNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVP-----IPVPlpmfsFTGSRSSFRGdtnfYGKQG---IQFYTQLKT 498
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPtagvdYHVP-----FGGRKGSSYG----PREQGeaaLEFYTTIKT 470
|
.
gi 515870065 499 I 499
Cdd:cd07097 471 V 471
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
43-461 |
1.25e-114 |
|
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: 347.24 E-value: 1.25e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 43 FIGGKFVESKSDKwIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTS-------------VLSRQQKEIAKL 109
Cdd:cd07086 2 VIGGEWVGSGGET-FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPaprrgeivrqigeALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 110 ITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVC 189
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 190 GNTFLMKPSERVP----GATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGK 265
Cdd:cd07086 161 GNTVVWKPSETTPltaiAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 266 RVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL-VGEAKKWLPELVEHAKNLRVNAGDQPGADLGP 344
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVhESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 345 LITPQAKERVCNLIDSGTKEGASILLDGRKIkvKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQI 424
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGGTVLTGGKRI--DGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAI 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 515870065 425 VNNNPYGNGTAIFTTNGATARKY--AHLVDVGQVGVNVP 461
Cdd:cd07086 399 NNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIP 437
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
59-500 |
9.13e-107 |
|
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: 326.44 E-value: 9.13e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQ-------------KEIAKLITLEQGKTLADAE-GD 124
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARilhkvadliearaDELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 125 VFRGLQVVEHACSVTSLMMGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 204
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALN-YVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 205 TMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDA 283
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFgPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 284 NKENTLNQLVGAAFGAAGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSG 361
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLA-GSRILVQRsiYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 362 TKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNG 441
Cdd:cd07093 319 RAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 515870065 442 ATARKYAHLVDVGQVGVNVPIPVPLPMfSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 500
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNCWLVRDLRT-PFGGVKAS--GIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
61-500 |
1.47e-105 |
|
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: 323.23 E-value: 1.47e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 61 NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQ-------------QKEIAKLITLEQGKTLADAEGDVFR 127
Cdd:cd07103 3 NPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAailrrwadlirerAEDLARLLTLEQGKPLAEARGEVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 128 GLQVV----EHACSVTslmmGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMVCGNTFLMKPSERVP 202
Cdd:cd07103 83 AASFLewfaEEARRIY----GRTIPSPAPGKRILVIKQPVGVVAAITPWNFPaAMITRKIAP-ALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 203 GATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAknHG--VV 279
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIgEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGG--NApfIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 280 MPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNL 357
Cdd:cd07103 236 FDDADLDKAVDGAIASKFRNAGQTCVC-ANRIYVHEsiYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 358 IDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIF 437
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGY----FYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515870065 438 TTNGATARKYAHLVDVGQVGVNVPIPvPLPMFSFTGSRSSfrGdtnfYG----KQGIQFYTQLKTIT 500
Cdd:cd07103 391 TRDLARAWRVAEALEAGMVGINTGLI-SDAEAPFGGVKES--G----LGreggKEGLEEYLETKYVS 450
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
43-499 |
2.17e-103 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 318.06 E-value: 2.17e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 43 FIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTS-------------VLSRQQKEIAKL 109
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPaieraaylrkladLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 110 ITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMV 188
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPfFLIARKLAP-ALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 189 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 267
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 268 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLG 343
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTC-AERVYVHEdiYDEFMEKLVEKMKAVKV--GDpfDAATDMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 344 PLITPQAKERVCNLIDSGTKEGASILLDGRKIKVkgyENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQ 423
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEG---EKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515870065 424 IVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSfTGSRSSFRGDTNfyGKQGIQFYTQLKTI 499
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH-AGWKKSGLGGAD--GKHGLEEYLQTKVV 466
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
59-499 |
3.22e-98 |
|
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: 304.07 E-value: 3.22e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQK-------------EIAKLITLEQGKTLADAEGDV 125
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAAllaiadaieanaeELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 126 FRGLQVVEHACSVTslmmgetMPSI----TKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERV 201
Cdd:cd07106 81 GGAVAWLRYTASLD-------LPDEviedDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 202 PGATMLLAKLLQDSgAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMP 281
Cdd:cd07106 154 PLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 282 DANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLID 359
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKR-LYVHESiyDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 360 SGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTT 439
Cdd:cd07106 312 DAKAKGAKVLAGGEPLDGPGY----FIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 440 NGATARKYAHLVDVGQVGVNvPIPVPLPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 499
Cdd:cd07106 388 DLERAEAVARRLEAGTVWIN-THGALDPDAPFGGHKQSGIGVE--FGIEGLKEYTQTQVI 444
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
42-500 |
7.21e-95 |
|
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: 295.95 E-value: 7.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 42 LFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSV-------------LSRQQKEIAK 108
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVeeraalleriaeaYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 109 LITLEQG--KTLAdAEGDVFRGLQVVEHACSVTSLMMGETMPSITKdmdlySYRLPLGVCAGIAPFNFPA-MIPLWMFPm 185
Cdd:cd07138 81 AITLEMGapITLA-RAAQVGLGIGHLRAAADALKDFEFEERRGNSL-----VVREPIGVCGLITPWNWPLnQIVLKVAP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 186 AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHG 264
Cdd:cd07138 154 ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEAAADTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 265 KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAVLVGEAKkwLPELVEHAK----NLRVNAGDQPGA 340
Cdd:cd07138 234 KRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAP-TRMLVPRSR--YAEAEEIAAaaaeAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 341 DLGPLITPQAKERVCNLIDSGTKEGASILLDGRKiKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDE 420
Cdd:cd07138 311 TLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPG-RPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 421 AIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPL-PmfsFTGSRSSfrGDTNFYGKQGIQFYTQLKTI 499
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNPGaP---FGGYKQS--GNGREWGRYGLEEFLEVKSI 464
|
.
gi 515870065 500 T 500
Cdd:cd07138 465 Q 465
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
43-459 |
7.26e-95 |
|
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: 296.53 E-value: 7.26e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 43 FIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAF--PAWADTSVLSR-------------QQKEIA 107
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERaallfriadkireDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 108 KLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSiTKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAM 187
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDV-PPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 188 VCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKR 266
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 267 VQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGP 344
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSR-LLVEEsiHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 345 LITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQI 424
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430
....*....|....*....|....*....|....*
gi 515870065 425 VNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN 433
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
39-500 |
6.72e-94 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 294.90 E-value: 6.72e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 39 TVKLFIGGKFVESkSDKwIDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTS-------------VLSRQQK 104
Cdd:cd07124 32 EYPLVIGGKEVRT-EEK-IESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPpeerarlllraaaLLRRRRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 105 EIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFP 184
Cdd:cd07124 110 ELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYR-PLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 185 MAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFER---- 259
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVgDYLVEHPDVRFIAFTGSREVGLRIYERaakv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 260 --GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEA-KKWLPELVEHAKNLRVNAGD 336
Cdd:cd07124 269 qpGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVyDEFLERLVERTKALKVGDPE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 337 QPGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRKIKVKgyENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETE 416
Cdd:cd07124 349 DPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELA--AEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 417 TLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMF-SFTGSRSSfrGDTnfyGKQG-----I 490
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRqPFGGFKMS--GTG---SKAGgpdylL 500
|
490
....*....|
gi 515870065 491 QFyTQLKTIT 500
Cdd:cd07124 501 QF-MQPKTVT 509
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
37-500 |
1.09e-92 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 290.65 E-value: 1.09e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 37 VPTvKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAW-----------------ADtsVL 99
Cdd:cd07091 2 QPT-GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGwwrkmdprergrllnklAD--LI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 100 SRQQKEIAKLITLEQGKTL-ADAEGDVfrglqvvehACSVTSL---------MMGETMPSITKDMDlYSYRLPLGVCAGI 169
Cdd:cd07091 79 ERDRDELAALESLDNGKPLeESAKGDV---------ALSIKCLryyagwadkIQGKTIPIDGNFLA-YTRREPIGVCGQI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 170 APFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVG 248
Cdd:cd07091 149 IPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFgPTAGAAISSHMDVDKIAFTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 249 SNKAGEYIFERGSRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVE 325
Cdd:cd07091 229 STAVGRTIMEAAAKSNlKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSR-IFVQESiyDEFVEKFKA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 326 HAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEI 405
Cdd:cd07091 308 RAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGY----FIQPTVFTDVKDDMKIAKEEI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 406 FGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVpIPVPLPMFSFTGSRSSFRGDTNfy 485
Cdd:cd07091 384 FGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNT-YNVFDAAVPFGGFKQSGFGREL-- 460
|
490
....*....|....*
gi 515870065 486 GKQGIQFYTQLKTIT 500
Cdd:cd07091 461 GEEGLEEYTQVKAVT 475
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
87-500 |
2.23e-92 |
|
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: 286.43 E-value: 2.23e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 87 KRAFPAWADTSV-------------LSRQQKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKD 153
Cdd:cd06534 4 RAAFKAWAALPPaeraailrkiadlLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 154 MDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAV 232
Cdd:cd06534 84 GEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGgGDEVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 233 NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVL 312
Cdd:cd06534 164 AALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR-LL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 313 VGEAkkwlpelvehaknlrvnagdqpgadlgplITPQAKERVCnlidsgtkegasilldgrkikvkgyengnfvgpTIIS 392
Cdd:cd06534 243 VHES-----------------------------IYDEFVEKLV---------------------------------TVLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 393 NVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFT 472
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEAPFG 340
|
410 420
....*....|....*....|....*...
gi 515870065 473 GSRSSFRGDTNfyGKQGIQFYTQLKTIT 500
Cdd:cd06534 341 GVKNSGIGREG--GPYGLEEYTRTKTVV 366
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
43-497 |
1.49e-90 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 285.16 E-value: 1.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 43 FIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQK-------------EIAKL 109
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRIlrraadlirerneELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 110 ITLEQGKTLADAE-GDVFRGLQVVEHACSVTSLMMGETMPSITKDmDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMV 188
Cdd:TIGR01804 81 ETLDTGKTLQETIvADMDSGADVFEFFAGLAPALNGEIIPLGGPS-FAYTIREPLGVCVGIGAWNYPLQIASWKIAPALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 189 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 267
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVgPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 268 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPL 345
Cdd:TIGR01804 240 TMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSN-GTRVFVHKKikERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 346 ITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIV 425
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515870065 426 NNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLK 497
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTynLYPAEAP---FGGYKQSGIGREN--GKAALAHYTEVK 467
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
41-459 |
1.80e-90 |
|
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: 284.85 E-value: 1.80e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 41 KLFIGGKFVESkSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADT--------------SVLSRQQKEI 106
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmpleeridclhkfaDLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 107 AKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSY----RLPLGVCAGIAPFNFP------A 176
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIaqvrREPLGVVLAIGPFNYPlnltvsK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 177 MIPlwmfpmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEY 255
Cdd:cd07082 162 LIP------ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRgREIGDPLVTHGRIDVISFTGSTEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 256 IFERGSRhgKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVN 333
Cdd:cd07082 236 LKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-VLVHEsvADELVELLKEEVAKLKVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 334 AGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGrkikvkGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVL 413
Cdd:cd07082 313 MPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGG------GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPII 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 515870065 414 ETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:cd07082 387 RVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNIN 432
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
59-499 |
1.81e-90 |
|
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: 284.58 E-value: 1.81e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSR-------------QQKEIAKLITLEQGKTLADAEGDV 125
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERgrilrkaadllreRNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 126 FRGLQVVEHACSVTSLMMGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT 205
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVP-LPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 206 MLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANK 285
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 286 ENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSG 361
Cdd:cd07090 240 ENAVNGAMMANFLSQGQVCSN-GTRVFVQRSikDEFTERLVERTKKIRI--GDplDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 362 TKEGASILLDGRKIKVK-GYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTN 440
Cdd:cd07090 317 KQEGAKVLCGGERVVPEdGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515870065 441 GATARKYAHLVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 499
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINtyniSPVEVP-----FGGYKQSGFGREN--GTAALEHYTQLKTV 452
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
59-499 |
1.23e-89 |
|
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: 282.13 E-value: 1.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAF--PAWADTS-------------VLSRQQKEIAKLITLEQGKTLADAEG 123
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTptergkllrrladLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 124 DVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPG 203
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 204 ATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPD 282
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFgPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 283 ANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDS 360
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSR-LLVQRsiYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 361 GTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTN 440
Cdd:cd07114 320 AREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 515870065 441 GATARKYAHLVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 499
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNTYRALS-PSSPFGGFKDSGIGREN--GIEAIREYTQTKSV 455
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
58-500 |
1.37e-88 |
|
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: 279.21 E-value: 1.37e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 58 DIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTS-------------VLSRQQKEIAKLITLEQGKTLADAEGD 124
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTpsererillkaaeIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 125 VFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 204
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 205 TMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDA 283
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 284 NkentLNQLVG-AAFGA---AGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVC 355
Cdd:cd07150 242 D----LDYAVRaAAFGAfmhQGQICMS-ASRIIVEEPvyDEFVKKFVARASKLKV--GDprDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 356 NLIDSGTKEGASILldgrkikVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTA 435
Cdd:cd07150 315 RQVEDAVAKGAKLL-------TGGKYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515870065 436 IFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 500
Cdd:cd07150 388 ILTNDLQRAFKLAERLESGMVHINDPTILDEAHVPFGGVKAS--GFGREGGEWSMEEFTELKWIT 450
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
42-500 |
1.98e-88 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 279.71 E-value: 1.98e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 42 LFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAF-PAWADTSVLSRQQK-------------EIA 107
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRIllrladlieqhgeELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 108 KLITLEQGKTLAdaegdVFRGLQVvehACSVTSL---------MMGETM-PSIT----KDMDLYSYRLPLGVCAGIAPFN 173
Cdd:cd07113 82 QLETLCSGKSIH-----LSRAFEV---GQSANFLryfagwatkINGETLaPSIPsmqgERYTAFTRREPVGVVAGIVPWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 174 FPAMIPLWMFPMAMVCGNTFLMKPSERVPgATML-LAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKA 252
Cdd:cd07113 154 FSVMIAVWKIGAALATGCTIVIKPSEFTP-LTLLrVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVAT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 253 GEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCmALSTAVLVGEAKkwLPELVEHAK---- 328
Cdd:cd07113 233 GKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVC-AAPERFYVHRSK--FDELVTKLKqals 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 329 NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGP 408
Cdd:cd07113 310 SFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGY----FVQPTLVLARSADSRLMREETFGP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 409 VLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTnfYGKQ 488
Cdd:cd07113 386 VVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLD-PAVPFGGMKQSGIGRE--FGSA 462
|
490
....*....|..
gi 515870065 489 GIQFYTQLKTIT 500
Cdd:cd07113 463 FIDDYTELKSVM 474
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
42-500 |
2.29e-88 |
|
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: 279.46 E-value: 2.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 42 LFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAF--PAWADTS-------------VLSRQQKEI 106
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSpaeraavlrrladALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 107 AKLITLEQGKTLA--------------DAEGDVFRGLQVVEHacsVTSLMMGETMPSitkdmdlysyRLPLGVCAGIAPF 172
Cdd:cd07139 81 ARLWTAENGMPISwsrraqgpgpaallRYYAALARDFPFEER---RPGSGGGHVLVR----------REPVGVVAAIVPW 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 173 NFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKA 252
Cdd:cd07139 148 NAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 253 GEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALsTAVLVGEAKK--WLPELVEHAKNL 330
Cdd:cd07139 228 GRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVAL-TRILVPRSRYdeVVEALAAAVAAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 331 RVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVL 410
Cdd:cd07139 307 KVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGR--PAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 411 VVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVP-LPmfsFTGSRSSfrGDTNFYGKQG 489
Cdd:cd07139 385 SVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFgAP---FGGFKQS--GIGREGGPEG 459
|
490
....*....|.
gi 515870065 490 IQFYTQLKTIT 500
Cdd:cd07139 460 LDAYLETKSIY 470
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
61-499 |
2.89e-87 |
|
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: 276.24 E-value: 2.89e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 61 NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTS-------------VLSRQQKEIAKLITLEQGKTLADAEG-DVF 126
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDpaergrilwrlaeLILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 127 RGLQVVEHACSVTSLMMGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATM 206
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIP-VRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 207 LLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANK 285
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFgEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 286 ENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTK 363
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSR-LLVHEsiYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 364 EGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGAT 443
Cdd:cd07115 321 EGARLLTGGKRPGARGF----FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515870065 444 ARKYAHLVDVGQVGVNVpipvplpmFSFTGSRSSFRG--DTNF---YGKQGIQFYTQLKTI 499
Cdd:cd07115 397 AHRVAAALKAGTVWINT--------YNRFDPGSPFGGykQSGFgreMGREALDEYTEVKSV 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
78-500 |
2.00e-86 |
|
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: 273.25 E-value: 2.00e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 78 EMDAAIASCKRAFPAWADTS-------------VLSRQQKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMG 144
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPpqeraailrkaaeILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 145 ETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKLLQDSGAPDGTLN 223
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 224 IIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 302
Cdd:cd07104 161 VVPGGGSEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 303 RCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGDQ--PGADLGPLITPQAKERVCNLIDSGTKEGAsilldgrKIKVK 378
Cdd:cd07104 241 ICMAAGR-ILVHEsvYDEFVEKLVAKAKALPV--GDPrdPDTVIGPLINERQVDRVHAIVEDAVAAGA-------RLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 379 GYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGV 458
Cdd:cd07104 311 GTYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHI 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 515870065 459 NVPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 500
Cdd:cd07104 391 NDQTVNDEPHVPFGGVKAS--GGGRFGGPASLEEFTEWQWIT 430
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
57-500 |
2.58e-86 |
|
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: 273.70 E-value: 2.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 57 IDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSV-------------LSRQQKEIAKLITLEQGKTLADAEG 123
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAyeraeileraaqlLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 124 DVFRGLQVVEHACSVTSLMMGETMPsitkdMDL---------YSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFL 194
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIP-----FDAspggegrigFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 195 MKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGsrhG-KRVQANMG 272
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARKA---GlKKVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 273 AKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEAKK--WLPELVEHAKNLRVnaGD--QPGADLGPLITP 348
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQR-IFVHEDIYdeFLERFVAATKKLVV--GDplDEDTDVGPMISE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 349 QAKERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNN 428
Cdd:cd07149 310 AEAERIEEWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 429 PYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPipvplpmfsftgsrSSFRGDTNFYG--------KQGIQF----YTQL 496
Cdd:cd07149 383 PYGLQAGVFTNDLQKALKAARELEVGGVMINDS--------------STFRVDHMPYGgvkesgtgREGPRYaieeMTEI 448
|
....
gi 515870065 497 KTIT 500
Cdd:cd07149 449 KLVC 452
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
43-497 |
1.07e-85 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 273.49 E-value: 1.07e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 43 FIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSR-------------QQKEIAKL 109
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERskilrrwydliiaNKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 110 ITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMV 188
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPlAMITRKVGP-ALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 189 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 267
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIgDALLASPKVRKITFTGSTAVGKKLMAGAAATVKRV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 268 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPL 345
Cdd:PLN02278 267 SLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVC-ANRILVQEGiyDKFAEAFSKAVQKLVVGDGFEEGVTQGPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 346 ITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGyengNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIV 425
Cdd:PLN02278 346 INEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGG----TFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIA 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515870065 426 NNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 497
Cdd:PLN02278 422 NDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL-ISTEVAPFGGVKQSGLGREG--SKYGIDEYLEIK 490
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
38-499 |
6.39e-84 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 268.51 E-value: 6.39e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 38 PTvKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPA-WADTS-------------VLSRQQ 103
Cdd:cd07144 7 PT-GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTgeergelldkladLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 104 KEIAKLITLEQGKTL-ADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWM 182
Cdd:cd07144 86 DLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKL-AYTLHEPYGVCGQIIPWNYPLAMAAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 183 FPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGS 261
Cdd:cd07144 165 LAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAgSALAEHPDVDKIAFTGSTATGRLVMKAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 262 RHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAK-NLRVNAGDQP 338
Cdd:cd07144 245 QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSR-IYVQESiyDKFVEKFVEHVKqNYKVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 339 GADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKiKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETL 418
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEK-APEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 419 DEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVP----IPVPlpmfsFTGSRSSfrGDTNFYGKQGIQFYT 494
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSndsdVGVP-----FGGFKMS--GIGRELGEYGLETYT 475
|
....*
gi 515870065 495 QLKTI 499
Cdd:cd07144 476 QTKAV 480
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
59-500 |
6.50e-84 |
|
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: 267.18 E-value: 6.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWA-DTSVLSRQQ-------------KEIAKLITLEQGKTLADAEGD 124
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRlllriarlirehaDELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 125 VFRGLQVVEHACSVTSLMMGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 204
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIP-LGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 205 TMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDA 283
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLgAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 284 NKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAG-DQPgaDLGPLITPQAKERVCNLIDS 360
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSR-LLVHRSiyDEVLERLVERFRALRVGPGlEDP--DLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 361 GTKEGASILLDGRKIKVKgYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTN 440
Cdd:cd07109 317 ARARGARIVAGGRIAEGA-PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515870065 441 GATARKYAHLVDVGQVGVNVPIP---VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 500
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNNYGAgggIELP---FGGVKKSGHGREK--GLEALYNYTQTKTVA 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
57-459 |
7.30e-84 |
|
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: 267.29 E-value: 7.30e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 57 IDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSV-------------LSRQQKEIAKLITLEQGKTLADAEG 123
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAykrykilmkvaelIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 124 DVFRGLQVVEHACSVTSLMMGETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSE 199
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVdayeYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 200 RVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGV 278
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 279 VMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERV 354
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKR-ILVEEevYDKFLKLLVEKVKKLKV--GDplDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 355 CNLIDSGTKEGASILLDGRKIKvkgyenGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGT 434
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKRDE------GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQA 391
|
410 420
....*....|....*....|....*
gi 515870065 435 AIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:cd07145 392 SVFTNDINRALKVARELEAGGVVIN 416
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
41-500 |
3.26e-83 |
|
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: 266.52 E-value: 3.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAF---PAW--ADTS-----------VLSRQQK 104
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWrtMDASergrllnkladLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 105 EIAKLITLEQGKTLADA-EGDVFRGLQVVEHACSVTSLMMGETMPSitkDMDLYSY-RL-PLGVCAGIAPFNFPAMIPLW 181
Cdd:cd07141 88 YLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPM---DGDFFTYtRHePVGVCGQIIPWNFPLLMAAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 182 MFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERG 260
Cdd:cd07141 165 KLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGyGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 261 SRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQ 337
Cdd:cd07141 245 GKSNlKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCA-GSRTFVQESiyDEFVKRSVERAKKRVVGNPFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 338 PGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETET 417
Cdd:cd07141 324 PKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGY----FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 418 LDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 497
Cdd:cd07141 400 IDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVS-PQAPFGGYKMSGNGREL--GEYGLQEYTEVK 476
|
...
gi 515870065 498 TIT 500
Cdd:cd07141 477 TVT 479
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
60-500 |
2.13e-82 |
|
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: 263.43 E-value: 2.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 60 HNPATNEVIGRVPQATKAEMDAAIASCKRAFPA--WADTS-------------VLSRQQKEIAKLITLEQGKTLADAEGD 124
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSgaeraavllkvadLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 125 VFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 204
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 205 TMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDA 283
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 284 NKENTLNqlvGAAFGA---AGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCN 356
Cdd:cd07118 242 DLDAAAD---AVVFGVyfnAGECCNSGSR-LLVHEsiADAFVAAVVARSRKVRV--GDplDPETKVGAIINEAQLAKITD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 357 LIDSGTKEGASILLDGRKIkvkGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAI 436
Cdd:cd07118 316 YVDAGRAEGATLLLGGERL---ASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGV 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515870065 437 FTTNGATARKYAHLVDVGQVGVNVPIP--VPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 500
Cdd:cd07118 393 WSKDIDTALTVARRIRAGTVWVNTFLDgsPELP---FGGFKQSGIGREL--GRYGVEEYTELKTVH 453
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
38-499 |
1.78e-81 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 262.12 E-value: 1.78e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 38 PTVKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTS------VLSR-------QQK 104
Cdd:PRK13252 5 PLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTamersrILRRavdilreRND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 105 EIAKLITLEQGKTLADAE-GDVFRGLQVVEHACSVTSLMMGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMF 183
Cdd:PRK13252 85 ELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRGGSF-VYTRREPLGVCAGIGAWNYPIQIACWKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 184 PMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRH 263
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 264 GKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEAKK--WLPELVEHAKNLRVnaGD--QPG 339
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTN-GTRVFVQKSIKaaFEARLLERVERIRI--GDpmDPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 340 ADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLD 419
Cdd:PRK13252 321 TNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDED 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 420 EAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNfyGKQGIQFYTQLK 497
Cdd:PRK13252 401 EVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwgESPAEMP---VGGYKQSGIGREN--GIATLEHYTQIK 475
|
..
gi 515870065 498 TI 499
Cdd:PRK13252 476 SV 477
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
42-459 |
4.83e-81 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 261.79 E-value: 4.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 42 LFIGGKFVESKsDKwIDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTS-------------VLSRQQKEIA 107
Cdd:PRK03137 39 LIIGGERITTE-DK-IVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSpedrarillraaaIIRRRKHEFS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 108 KLITLEQGKTLADAEGDVFRGLQVVE-HACSVTSLMMGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMA 186
Cdd:PRK03137 117 AWLVKEAGKPWAEADADTAEAIDFLEyYARQMLKLADGKPVESRPGEHNRYFYI-PLGVGVVISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 187 MVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFER------ 259
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVgDYLVDHPKTRFITFTGSREVGLRIYERaakvqp 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 260 GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEA-KKWLPELVEHAKNLRVNAGDQP 338
Cdd:PRK03137 276 GQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVyDEVLEKVVELTKELTVGNPEDN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 339 gADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETL 418
Cdd:PRK03137 356 -AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGY----FIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDF 429
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 515870065 419 DEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:PRK03137 430 DHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFN 470
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
57-500 |
9.74e-80 |
|
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: 256.59 E-value: 9.74e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 57 IDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADT------SVLSR-------QQKEIAKLITLEQGKTLADAEG 123
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALpphermAILERaadllkkRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 124 DVFRGLQVVEHACSVTSLMMGETMPS----ITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSE 199
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 200 RVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSrhGKRVQANMGAKNHGV 278
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLgDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 279 VMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNL 357
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEElYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 358 IDSGTKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIF 437
Cdd:cd07094 319 VEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515870065 438 TTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSfrgdtnFYGKQGIQF----YTQLKTIT 500
Cdd:cd07094 392 TRDLNVAFKAAEKLEVGGVMVNDSSAFRTDWMPFGGVKES------GVGREGVPYameeMTEEKTVV 452
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
59-501 |
1.07e-79 |
|
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: 256.10 E-value: 1.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQ-------------KEIAKLITLEQGKTLADAEGDV 125
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKallkladaieenaEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 126 FRGlqVVEH-------ACSVTSLMMGETMPSITKdmdlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPS 198
Cdd:cd07092 81 LPG--AVDNfrffagaARTLEGPAAGEYLPGHTS----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 199 ERVPGATMLLAKLLQDsGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHG 277
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 278 VVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVC 355
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTA-ACRVYVHESvyDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 356 NLIDsGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTA 435
Cdd:cd07092 313 GFVE-RAPAHARVLTGGRRAEGPGY----FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 436 IFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMfSFTGSRSSfrGdtnfYGKQ----GIQFYTQLKTITS 501
Cdd:cd07092 388 VWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEM-PHGGFKQS--G----YGKDlsiyALEDYTRIKHVMV 450
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
59-500 |
9.18e-79 |
|
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: 254.21 E-value: 9.18e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADT-------------SVLSRQQKEIAKLITLEQGKTL-ADAEGD 124
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATparergkllariaDALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 125 VFRGLQVVEHACSVTSLMMGETMPsITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 204
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 205 TMLLAKLLQDSgAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDA 283
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYgEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 284 NKENTLNQLV-GAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLI 358
Cdd:cd07108 239 DLDDAVDGAIaGMRFTRQGQSCTA-GSRLFVHEDiyDAFLEKLVAKLSKLKI--GDplDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 359 DSGTKE-GASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIF 437
Cdd:cd07108 316 DLGLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515870065 438 TTNGATARKYAHLVDVGQVGVNVPIpVPLPMFSFTGSRSSFRGDTnfYGKQG-IQFYTQLKTIT 500
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGG-GQQPGQSYGGFKQSGLGRE--ASLEGmLEHFTQKKTVN 456
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
40-499 |
1.94e-77 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 251.29 E-value: 1.94e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 40 VKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQKE----IAKLI----- 110
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVSGSKRGRclskLADLMernld 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 111 ------TLEQGKT-LADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMF 183
Cdd:cd07143 87 ylasieALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLT-YTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 184 PMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSR 262
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 263 HG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGDQPG 339
Cdd:cd07143 246 SNlKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCA-GSRIYVQEGiyDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 340 ADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLD 419
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGY----FIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 420 EAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPlPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 499
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLH-HQVPFGGYKQSGIGRE--LGEYALENYTQIKAV 477
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
80-500 |
2.22e-77 |
|
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: 249.80 E-value: 2.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 80 DAAIASCKRAFPAWADTS-------------VLSRQQKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGET 146
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPpserrdillkaadLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 147 MPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIH 226
Cdd:cd07105 83 IPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 227 GQ----HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQ 302
Cdd:cd07105 163 HSpedaPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 303 RCMalSTA-VLVGE--AKKWLPELVEHAKNLRvnagdQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRkikVKG 379
Cdd:cd07105 243 ICM--STErIIVHEsiADEFVEKLKAAAEKLF-----AGPVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGL---ADE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 380 YENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:cd07105 313 SPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 515870065 460 VPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 500
Cdd:cd07105 393 GMTVHDEPTLPHGGVKSS--GYGRFNGKWGIDEFTETKWIT 431
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
59-499 |
2.55e-77 |
|
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: 250.24 E-value: 2.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWA-DTS-------------VLSRQQKEIAKLITLEQGKTLADAEG- 123
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDaeerarclrqlheALEARKEELRALLVAEVGAPVMTARAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 124 ------DVFRGlqVVEHACS--------VTSLMMGETMPSITKDmdlysyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVC 189
Cdd:cd07089 81 qvdgpiGHLRY--FADLADSfpwefdlpVPALRGGPGRRVVRRE--------PVGVVAAITPWNFPFFLNLAKLAPALAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 190 GNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQ 268
Cdd:cd07089 151 GNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVgEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 269 ANMGAKNHGVVMPDANkentLNQLVGAAFG----AAGQRCmALSTAVLVGEAKKwlPELVEHAKN----LRVNAGDQPGA 340
Cdd:cd07089 231 LELGGKSANIVLDDAD----LAAAAPAAVGvcmhNAGQGC-ALTTRLLVPRSRY--DEVVEALAAafeaLPVGDPADPGT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 341 DLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDE 420
Cdd:cd07089 304 VMGPLISAAQRDRVEGYIARGRDEGARLVTGGGR--PAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 421 AIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTnfYGKQGIQFYTQL 496
Cdd:cd07089 382 AVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINggggYGPDAP-----FGGYKQSGLGRE--NGIEGLEEFLET 454
|
...
gi 515870065 497 KTI 499
Cdd:cd07089 455 KSI 457
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
59-459 |
2.31e-76 |
|
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: 247.67 E-value: 2.31e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQK-------------EIAKLITLEQGKTLADAEGDV 125
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMlrelatrlrehaeELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 126 FRGLQVVEHACSVTSLMMGETMPSITKDMdLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT 205
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNL-HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 206 MLLAKLLQDSgAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDAN 284
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 285 KENTLNQLV-GAAFGAAGQRCMALSTAvLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSG 361
Cdd:cd07107 239 PEAAADAAVaGMNFTWCGQSCGSTSRL-FVHESiyDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 362 TKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNG 441
Cdd:cd07107 318 KREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410
....*....|....*...
gi 515870065 442 ATARKYAHLVDVGQVGVN 459
Cdd:cd07107 398 SQAHRTARRVEAGYVWIN 415
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
46-502 |
2.58e-76 |
|
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: 247.99 E-value: 2.58e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 46 GKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQ-------------KEIAKLITL 112
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEilekaaqileerrDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 113 EQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNT 192
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 193 FLMKPSERVP--GATmLLAKLLQDSGAPDGTLNIIHGqheAVNFICD----HPDIKAISFVGSNKAGEYIFERGSRHGKR 266
Cdd:cd07151 161 VVLKPASDTPitGGL-LLAKIFEEAGLPKGVLNVVVG---AGSEIGDafveHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 267 VQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVnaGDQ--PGADL 342
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINR-IIVHEDvyDEFVEKFVERVKALPY--GDPsdPDTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 343 GPLITPQAKERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAI 422
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEAL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 423 QIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNvPIPV-PLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTITS 501
Cdd:cd07151 387 ELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVnDEPHVPFGGEKNS--GLGRFNGEWALEEFTTDKWISV 463
|
.
gi 515870065 502 Q 502
Cdd:cd07151 464 Q 464
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
59-500 |
3.33e-76 |
|
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: 247.26 E-value: 3.33e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 59 IHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTS-------------VLSRQQKEIAKLITLEQGKTLADAEGDV 125
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTgaerakylraiaeGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 126 ---------FRGL--QVVEHAcsvtslmmGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFL 194
Cdd:cd07110 81 ddvagcfeyYADLaeQLDAKA--------ERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 195 MKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGA 273
Cdd:cd07110 153 LKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTgDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 274 KNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAK 351
Cdd:cd07110 233 KSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSR-LLVHEsiADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 352 ERVCNLIDSGTKEGASILLDGRKikVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYG 431
Cdd:cd07110 312 EKVLSFIARGKEEGARLLCGGRR--PAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYG 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 432 NGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVpLPMFSFTG-SRSSFRGDtnfYGKQGIQFYTQLKTIT 500
Cdd:cd07110 390 LAAAVISRDAERCDRVAEALEAGIVWINCSQPC-FPQAPWGGyKRSGIGRE---LGEWGLDNYLEVKQIT 455
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
57-500 |
1.96e-74 |
|
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: 242.65 E-value: 1.96e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 57 IDIHNPATNEVIGRVPQATKAEMDAAIASckrafpAWADTSVLSRQQK----------------EIAKLITLEQGKTLAD 120
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALREALAL------AASYRSTLTRYQRsailnkaaallearreEFARLITLESGLCLKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 121 AEGDVFRGLQVVEHACSVTSLMMGETMPS-IT---KDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMK 196
Cdd:cd07146 75 TRYEVGRAADVLRFAAAEALRDDGESFSCdLTangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 197 PSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSrhGKRVQANMGAKN 275
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 276 HGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAK 351
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKR-ILVHEsvADEFVDLLVEKSAALVV--GDpmDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 352 ERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYG 431
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYG 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515870065 432 NGTAIFTTNGATARKYAHLVDVGQVGVNvpiPVP---LPMFSFTGSRSSFRGdtnfyGKQGIQ----FYTQLKTIT 500
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVN---EVPgfrSELSPFGGVKDSGLG-----GKEGVReamkEMTNVKTYS 450
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
41-499 |
4.44e-74 |
|
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: 242.63 E-value: 4.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSR------------QQKE-IA 107
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERanilnkiadrieENLElLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 108 KLITLEQGK-----TLAD--AEGDVFRGLQVVEHACSVTSLMMGETMPSitkdmdlYSYRLPLGVCAGIAPFNFPAMIPL 180
Cdd:cd07559 82 VAETLDNGKpiretLAADipLAIDHFRYFAGVIRAQEGSLSEIDEDTLS-------YHFHEPLGVVGQIIPWNFPLLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 181 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFER 259
Cdd:cd07559 155 WKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFgSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 260 GSRHGKRVQANMGAKNHGVVMPDANKE--NTLNQLVGAAFGAA---GQRCMALSTAvLVGEA--KKWLPELVEHAKNLRV 332
Cdd:cd07559 234 AAENLIPVTLELGGKSPNIFFDDAMDAddDFDDKAEEGQLGFAfnqGEVCTCPSRA-LVQESiyDEFIERAVERFEAIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 333 NAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVV 412
Cdd:cd07559 313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 413 LETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNFygKQGI 490
Cdd:cd07559 393 ITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCyhQYPAHAP---FGGYKKSGIGRETH--KMML 467
|
....*....
gi 515870065 491 QFYTQLKTI 499
Cdd:cd07559 468 DHYQQTKNI 476
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
41-499 |
6.29e-73 |
|
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: 239.28 E-value: 6.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSR-------------QQKEIA 107
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERanilnkiadiideNKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 108 KLITLEQGK-----TLAD--AEGDVFRGLQVVEHACSVTSLMMGETMPSITKdmdlysyRLPLGVCAGIAPFNFPAMIPL 180
Cdd:cd07117 82 MVETLDNGKpiretRAVDipLAADHFRYFAGVIRAEEGSANMIDEDTLSIVL-------REPIGVVGQIIPWNFPFLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 181 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFER 259
Cdd:cd07117 155 WKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKgSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 260 GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQ 337
Cdd:cd07117 234 AAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSR-IFVQEGiyDEFVAKLKEKFENVKVGNPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 338 PGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETET 417
Cdd:cd07117 313 PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 418 LDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV--PIPVPLPmfsFTGSRSSFRGDTNFygKQGIQFYTQ 495
Cdd:cd07117 393 EDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTynQIPAGAP---FGGYKKSGIGRETH--KSMLDAYTQ 467
|
....
gi 515870065 496 LKTI 499
Cdd:cd07117 468 MKNI 471
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
39-463 |
1.55e-72 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 238.27 E-value: 1.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 39 TVKLFIGGKFVESKSDKWiDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTS-------------VLSRQQKE 105
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQ-PVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTpkeraeallkladAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 106 IAKLITLEQGK----TLAD---AEGDVFR---GLqvvehACSVTSLMMGETMPSITkdmdlySY--RLPLGVCAGIAPFN 173
Cdd:PRK13473 81 FARLESLNCGKplhlALNDeipAIVDVFRffaGA-----ARCLEGKAAGEYLEGHT------SMirRDPVGVVASIAPWN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 174 FPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKA 252
Cdd:PRK13473 150 YPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 253 GEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNL 330
Cdd:PRK13473 229 GKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTA-ACRIYAQRGiyDDLVAKLAAAVATL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 331 RVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEG-ASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPV 409
Cdd:PRK13473 308 KVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGY----YYEPTLLAGARQDDEIVQREVFGPV 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 515870065 410 LVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIP 463
Cdd:PRK13473 384 VSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM 437
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
66-503 |
4.08e-72 |
|
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: 236.42 E-value: 4.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 66 EVIGRVPQATKAEMDAAIASCKRAFPAWADTS-------------VLSRQQKEIAKLITLEQGKTLADAEGDVFRGLQVV 132
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPpreraavlrraadLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 133 EHACSVTSLMMGETMPSITKDMDlYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGAT-MLLAKL 211
Cdd:cd07152 82 HEAAGLPTQPQGEILPSAPGRLS-LARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 212 LQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQ 291
Cdd:cd07152 161 FEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 292 LVGAAFGAAGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIL 369
Cdd:cd07152 241 GAWGAFLHQGQICMA-AGRHLVHEsvADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 370 LDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAH 449
Cdd:cd07152 320 AGGTY-------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 515870065 450 LVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGdTNFYGKQGIQFYTQlktitSQW 503
Cdd:cd07152 393 RLRTGMLHINDQTVNDEPHNPFGGMGASGNG-SRFGGPANWEEFTQ-----WQW 440
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
57-486 |
6.89e-72 |
|
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: 235.99 E-value: 6.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 57 IDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQ-------------QKEIAKLITLEQGKTLADAEG 123
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAaillhcvarleerFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 124 DVFRGLQVVEHACSVTSLMMGETMPsitkdMDLYS---------YRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFL 194
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLP-----LDISArgegrqglvRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 195 MKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRhgKRVQANMGAK 274
Cdd:cd07147 156 LKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 275 NHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQA 350
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQR-VLVHRSvyDEFKSRLVARVKALKT--GDpkDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 351 KERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPY 430
Cdd:cd07147 311 AERVEGWVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKF 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 515870065 431 GNGTAIFTTNGATARKYAHLVDVGQVGVN-VPipvplpmfsftgsrsSFRGDTNFYG 486
Cdd:cd07147 384 GLQAGVFTRDLEKALRAWDELEVGGVVINdVP---------------TFRVDHMPYG 425
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
79-459 |
2.13e-71 |
|
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: 233.89 E-value: 2.13e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 79 MDAAIASCKRAFPAWADTSVLSR-------------QQKEIAKLITLEQGKTLADAEGDVFRGLQV----VEHACSvtsL 141
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERaallrkladllreRKDELARLITLEMGKPIAEARAEVEKCAWIcryyAENAEA---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 142 MMGETMPsiTKDMDLYSYRLPLGVCAGIAPFNFPamipLW-MF----PMAMVcGNTFLMKPSERVPGATMLLAKLLQDSG 216
Cdd:cd07100 78 LADEPIE--TDAGKAYVRYEPLGVVLGIMPWNFP----FWqVFrfaaPNLMA-GNTVLLKHASNVPGCALAIEELFREAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 217 APDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAA 296
Cdd:cd07100 151 FPEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 297 FGAAGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDG 372
Cdd:cd07100 231 LQNAGQSCIA-AKRFIVHEdvYDEFLEKFVEAMAALKV--GDpmDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 373 RKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVD 452
Cdd:cd07100 308 KRPDGPGA----FYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLE 383
|
....*..
gi 515870065 453 VGQVGVN 459
Cdd:cd07100 384 AGMVFIN 390
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
58-499 |
1.72e-70 |
|
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: 232.49 E-value: 1.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 58 DIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPA--WADTS------VLSR-------QQKEIAKLITLEQGKTLADA- 121
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSpaerkaVLLRladlieaHRDELALLETLDMGKPISDAl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 122 EGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERV 201
Cdd:cd07112 85 AVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALIT-REPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 202 PGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSR-HGKRVQANMGAKNHGVV 279
Cdd:cd07112 164 PLTALRLAELALEAGLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 280 MPDA-NKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERV 354
Cdd:cd07112 244 FADApDLDAAAEAAAAGIFWNQGEVCSAGSR-LLVHEsiKDEFLEKVVAAAREWKP--GDplDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 355 CNLIDSGTKEGASILLDGRKIKVKGyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGT 434
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515870065 435 AIFTTNGATARKYAHLVDVGQVGVN----VPIPVPlpmfsFTGSRSSFRGDTNfyGKQGIQFYTQLKTI 499
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNcfdeGDITTP-----FGGFKQSGNGRDK--SLHALDKYTELKTT 460
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
60-500 |
5.30e-70 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 230.96 E-value: 5.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 60 HNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSV-------------LSRQQKEIAKLITLEQGKTLADAEGDVF 126
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVegraqrllrwkraLADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 127 RGLQVVEHACSVTSLMMGE---TMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPG 203
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPrkvPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 204 ATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPdIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDA 283
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 284 NKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSG 361
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVER-VYVHESvyDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 362 TKEGASILLDGRKIKVKGyengNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNG 441
Cdd:cd07099 319 VAKGAKALTGGARSNGGG----PFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 442 ATARKYAHLVDVGQVGVN-VPIPVPLPMFSFTGSRSSfrGDTNFYGKQGIQFYTQLKTIT 500
Cdd:cd07099 395 ARAEAIARRLEAGAVSINdVLLTAGIPALPFGGVKDS--GGGRRHGAEGLREFCRPKAIA 452
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
37-463 |
3.10e-69 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 230.39 E-value: 3.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 37 VPTVKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPA-----WADTS-------------V 98
Cdd:PLN02467 5 VPRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTgavrakylraiaaK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 99 LSRQQKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRL---PLGVCAGIAPFNFP 175
Cdd:PLN02467 85 ITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKGYVlkePLGVVGLITPWNYP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 176 AMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGE 254
Cdd:PLN02467 165 LLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLgTEAGAPLASHPGVDKIAFTGSTATGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 255 YIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRV 332
Cdd:PLN02467 245 KIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSR-LLVHEriASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 333 NAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGrkIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVV 412
Cdd:PLN02467 324 SDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGG--KRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCV 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 515870065 413 LETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIP 463
Cdd:PLN02467 402 KTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQP 452
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
57-461 |
4.67e-69 |
|
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: 229.02 E-value: 4.67e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 57 IDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADT-------------SVLSRQQKEIAKLITLEQGKTLADAEG 123
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVpapkrgeivrqigDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 124 DVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP- 202
Cdd:cd07130 94 EVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPl 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 203 ---GATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFER-GSRHGkRVQANMGAKNHGV 278
Cdd:cd07130 174 taiAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAvAARFG-RSLLELGGNNAII 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 279 VMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVnaGD--QPGADLGPLITPQAKERV 354
Cdd:cd07130 253 VMEDADLDLAVRAVLFAAVGTAGQRCTTTRR-LIVHEsiYDEVLERLKKAYKQVRI--GDplDDGTLVGPLHTKAAVDNY 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 355 CNLIDSGTKEGASILLDGRKIKvkgyENGNFVGPTIISnVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGT 434
Cdd:cd07130 330 LAAIEEAKSQGGTVLFGGKVID----GPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSS 404
|
410 420
....*....|....*....|....*....
gi 515870065 435 AIFTTNGATARKY--AHLVDVGQVGVNVP 461
Cdd:cd07130 405 SIFTTDLRNAFRWlgPKGSDCGIVNVNIG 433
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
42-459 |
2.35e-68 |
|
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: 227.28 E-value: 2.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 42 LFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTS-------------VLSRQQKEIAK 108
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPghvrarhlyriarHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 109 LITLEQGKTLADA-EGDVFRGLQVVEHACSVTSLMmgetmpsitkDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAM 187
Cdd:cd07111 104 LESLDNGKPIRESrDCDIPLVARHFYHHAGWAQLL----------DTELAGWK-PVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 188 VCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 267
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 268 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPL 345
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSR-LLVQEsvAEELIRKLKERMSHLRVGDPLDKAIDMGAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 346 ITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIV 425
Cdd:cd07111 332 VDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGP----FYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALA 407
|
410 420 430
....*....|....*....|....*....|....
gi 515870065 426 NNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWIN 441
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
41-499 |
4.25e-68 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 226.61 E-value: 4.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFP--AWADTSVLSRQQ-------------KE 105
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRillrfadllekhaDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 106 IAKLITLEQGKTLADAE-GDVFRGLQVVEHACSVTSLMMGETMPSitkDMDLYSYRL--PLGVCAGIAPFNFPAMIPLWM 182
Cdd:cd07142 85 LAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPA---DGPHHVYTLhePIGVVGQIIPWNFPLLMFAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 183 FPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNF-ICDHPDIKAISFVGSNKAGEYIFERGS 261
Cdd:cd07142 162 VGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAaIASHMDVDKVAFTGSTEVGKIIMQLAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 262 RHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEakKWLPELVEHAKN--LRVNAGD-- 336
Cdd:cd07142 242 KSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCA-GSRTFVHE--SIYDEFVEKAKAraLKRVVGDpf 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 337 QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETE 416
Cdd:cd07142 319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGY----YIQPTIFSDVKDDMKIARDEIFGPVQSILKFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 417 TLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVpIPVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQL 496
Cdd:cd07142 395 TVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNC-YDVFDASIPFGGYKMSGIGREK--GIYALNNYLQV 471
|
...
gi 515870065 497 KTI 499
Cdd:cd07142 472 KAV 474
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
61-500 |
2.09e-67 |
|
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: 224.14 E-value: 2.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 61 NPATNEVIGRVPQATKAEMDAAIASCKRAF--PAWAD------------TSVLSRQQKEIAKLITLEQGKTLADAEGDVF 126
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAHdprlrarvllelADAFEANAERLARLLALENGKILGEARFEIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 127 RGLQVVEHACSVTSLMMGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATM 206
Cdd:cd07120 83 GAISELRYYAGLARTEAGRMIEPEPGSFSLVL-REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 207 LLAKLLQD-SGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDAN 284
Cdd:cd07120 162 AIIRILAEiPSLPAGVVNLFTESgSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 285 KENTLNQLVGAAFGAAGQRCMALSTaVLVGE--AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGT 362
Cdd:cd07120 242 LDAALPKLERALTIFAGQFCMAGSR-VLVQRsiADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 363 KEGASILLDGRKIkVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGA 442
Cdd:cd07120 321 AAGAEVVLRGGPV-TEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 515870065 443 TARKYAHLVDVGQVGVNVPIPVpLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLKTIT 500
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKL-FAEAEEGGYRQSGLGRLH--GVAALEDFIEYKHIY 454
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
37-459 |
8.46e-64 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 215.84 E-value: 8.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 37 VPTV---KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFP--AWADTSVLSRQQ-------- 103
Cdd:PLN02766 15 VPEIkftKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRimmkfadl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 104 -----KEIAKLITLEQGKTLADAEG-DVFRGLQVVEHACSVTSLMMGETMpSITKDMDLYSYRLPLGVCAGIAPFNFPAM 177
Cdd:PLN02766 95 ieehiEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETL-KMSRQLQGYTLKEPIGVVGHIIPWNFPST 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 178 IPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYI 256
Cdd:PLN02766 174 MFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 257 FERGSRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVN 333
Cdd:PLN02766 254 MQAAATSNlKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVA-SSRVYVQEGiyDEFVKKLVEKAKDWVVG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 334 AGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVL 413
Cdd:PLN02766 333 DPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGY----YIEPTIFTDVTEDMKIAQDEIFGPVMSLM 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 515870065 414 ETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:PLN02766 409 KFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
60-499 |
2.20e-62 |
|
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: 210.95 E-value: 2.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 60 HNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSV-------------LSRQQKEIAKLITLEQGKTLADAEGDVF 126
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLeerkaivtravelLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 127 RGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATM 206
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 207 LLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKE 286
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 287 NTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKE 364
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIER-IYVHESiyDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 365 GASILLDGRKIKVkGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATA 444
Cdd:cd07102 320 GARALIDGALFPE-DKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 515870065 445 RKYAHLVDVGQVGVNvPIPVPLPMFSFTGSRSSFRGDTnfYGKQGIQFYTQLKTI 499
Cdd:cd07102 399 EALGEQLETGTVFMN-RCDYLDPALAWTGVKDSGRGVT--LSRLGYDQLTRPKSY 450
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
41-499 |
5.37e-62 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 210.91 E-value: 5.37e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPA--WADTS-------------VLSRQQKE 105
Cdd:PRK09847 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSpakrkavlnkladLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 106 IAKLITLEQGKTLADA-EGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSyRLPLGVCAGIAPFNFPAMIPLWMFP 184
Cdd:PRK09847 101 LALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIV-REPVGVIAAIVPWNFPLLLTCWKLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 185 MAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIF-ERGSR 262
Cdd:PRK09847 180 PALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTRTGKQLLkDAGDS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 263 HGKRVQANMGAKNHGVVMPDANKentLNQLVGAA----FGAAGQRCMAlSTAVLVGE--AKKWLPELVEHAKNLRVNAGD 336
Cdd:PRK09847 260 NMKRVWLEAGGKSANIVFADCPD---LQQAASATaagiFYNQGQVCIA-GTRLLLEEsiADEFLALLKQQAQNWQPGHPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 337 QPGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRKIKVKGYengnfVGPTIISNVKPNMTCYKEEIFGPVLVVLETE 416
Cdd:PRK09847 336 DPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAA-----IGPTIFVDVDPNASLSREEIFGPVLVVTRFT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 417 TLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV----PIPVPlpmfsFTGSRSSFRG-DTNFYgkqGIQ 491
Cdd:PRK09847 410 SEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgDMTVP-----FGGYKQSGNGrDKSLH---ALE 481
|
....*...
gi 515870065 492 FYTQLKTI 499
Cdd:PRK09847 482 KFTELKTI 489
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
41-504 |
8.31e-61 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 208.89 E-value: 8.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAF--------PAWADTSVLSR-------QQKE 105
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFdegpwpkmTAYERSRILLRfadllekHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 106 IAKLITLEQGKTLADAEG-DVFRGLQVVEHACSVTSLMMGETMPSitkDMDLYSYRL--PLGVCAGIAPFNFPAMIPLWM 182
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPA---DGPHHVQTLhePIGVAGQIIPWNFPLLMFAWK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 183 FPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGS 261
Cdd:PLN02466 216 VGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 262 RHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAvLVGEakKWLPELVEHAKN--LRVNAGD-- 336
Cdd:PLN02466 296 KSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT-FVHE--RVYDEFVEKAKAraLKRVVGDpf 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 337 QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETE 416
Cdd:PLN02466 373 KKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGY----YIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 417 TLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN------VPIPvplpmfsFTGSRSSFRGDTNfyGKQGI 490
Cdd:PLN02466 449 DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfdvfdAAIP-------FGGYKMSGIGREK--GIYSL 519
|
490
....*....|....
gi 515870065 491 QFYTQLKTITSQWK 504
Cdd:PLN02466 520 NNYLQVKAVVTPLK 533
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
43-497 |
1.08e-60 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 207.45 E-value: 1.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 43 FIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSR-------------QQKEIAKL 109
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERanilrrwfnlmmeHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 110 ITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFP-AMIPLWMFPmAMV 188
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPaAMITRKAGP-ALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 189 CGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRV 267
Cdd:PRK11241 173 AGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 268 QANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCM-ALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLI 346
Cdd:PRK11241 253 SLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVcANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 347 TPQAKERVCNLIDSGTKEGASILLDGRKIKVkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVN 426
Cdd:PRK11241 333 DEKAVAKVEEHIADALEKGARVVCGGKAHEL----GGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515870065 427 NNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIpVPLPMFSFTGSRSSFRGDTNfyGKQGIQFYTQLK 497
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI-ISNEVAPFGGIKASGLGREG--SKYGIEDYLEIK 476
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
105-504 |
5.37e-59 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 200.73 E-value: 5.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 105 EIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPA-MIPLWMF 183
Cdd:PRK10090 14 EISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFfLIARKMA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 184 PmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSR 262
Cdd:PRK10090 94 P-ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGNPKVAMVSMTGSVSAGEKIMAAAAK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 263 HGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRC-MALSTAVLVGEAKKWLPELVEHAKNLRV-NAGDQPGA 340
Cdd:PRK10090 173 NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCnCAERVYVQKGIYDQFVNRLGEAMQAVQFgNPAERNDI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 341 DLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDE 420
Cdd:PRK10090 253 AMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGY----YYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 421 AIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNvpipvplpmfsftgsRSSFRGDTNFY------------GKQ 488
Cdd:PRK10090 329 AIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN---------------RENFEAMQGFHagwrksgiggadGKH 393
|
410
....*....|....*.
gi 515870065 489 GIQFYTQLKTITSQWK 504
Cdd:PRK10090 394 GLHEYLQTQVVYLQSD 409
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
60-501 |
1.11e-58 |
|
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: 201.00 E-value: 1.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 60 HNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSR-------------QQKEIAKLITLEQGKTLADAEGDVF 126
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERaavflrfhdlvleRRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 127 RGLQVVEH-ACSVTSLMMGE----TMPSITKDMDLYSyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERV 201
Cdd:cd07101 81 DVAIVARYyARRAERLLKPRrrrgAIPVLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 202 PGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIkaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVM 280
Cdd:cd07101 158 ALTALWAVELLIEAGLPRDLWQVVTGPGSEVgGAIVDNADY--VMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 281 PDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLI 358
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIER-IYVHESvyDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 359 DSGTKEGASILLDGRKIKVKG---YEngnfvgPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTA 435
Cdd:cd07101 315 DDAVAKGATVLAGGRARPDLGpyfYE------PTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNAS 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515870065 436 IFTTNGATARKYAHLVDVGQVGVNVPI-----PVPLPMFSFTGSRSSFRgdtnfYGKQGIQFYTQLKTITS 501
Cdd:cd07101 389 VWTRDGARGRRIAARLRAGTVNVNEGYaaawaSIDAPMGGMKDSGLGRR-----HGAEGLLKYTETQTVAV 454
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
43-462 |
3.49e-58 |
|
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: 201.27 E-value: 3.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 43 FIGGKfvESKSDKWIDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSV-------------LSRQQKEIAK 108
Cdd:cd07125 36 IINGE--ETETGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVeeraeilekaadlLEANRGELIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 109 LITLEQGKTLADAEGDV--------FRGLQVVEhacsvtsLMMGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPL 180
Cdd:cd07125 114 LAAAEAGKTLADADAEVreaidfcrYYAAQARE-------LFSDPELPGPTGELNGLELH-GRGVFVCISPWNFPLAIFT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 181 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFE- 258
Cdd:cd07125 186 GQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAKLINRa 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 259 RGSRHGKRVQ--ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAG 335
Cdd:cd07125 266 LAERDGPILPliAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEiAERFIEMLKGAMASLKVGDP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 336 DQPGADLGPLITPQAKERVCNLIDSGTKEGASIlldgrKIKVKGYENGNFVGPTIISNVKPNmtCYKEEIFGPVLVVL-- 413
Cdd:cd07125 346 WDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLI-----APAPLDDGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIrf 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 515870065 414 ETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPI 462
Cdd:cd07125 419 KAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNI 467
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
60-459 |
1.51e-57 |
|
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: 198.29 E-value: 1.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 60 HNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTS------VLS-------RQQKEIAKLITLEQGKTLADAegdvf 126
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSfaerrkVLRsllkyilENQEEICRVACRDTGKTMVDA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 127 rglqvvehacsvtslMMGETMPSITKdMD-------------------LYSYRL------PLGVCAGIAPFNFP------ 175
Cdd:cd07098 76 ---------------SLGEILVTCEK-IRwtlkhgekalrpesrpgglLMFYKRarveyePLGVVGAIVSWNYPfhnllg 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 176 AMIPlwmfpmAMVCGNTFLMKPSERVPGATM----LLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNK 251
Cdd:cd07098 140 PIIA------ALFAGNAIVVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 252 AGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKN 329
Cdd:cd07098 214 VGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIER-VIVHEKiyDKLLEILTDRVQA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 330 LRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPV 409
Cdd:cd07098 293 LRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPV 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 515870065 410 LVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:cd07098 373 MVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIN 422
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
78-463 |
1.04e-56 |
|
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: 195.18 E-value: 1.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 78 EMDAAIASCKRAFPAWADTSVLSRQ-------------QKEIAKLITLEQGKTLADAEGDVfrGLQVVEHACSVTSLMmg 144
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAailrrfaellkanKEELARLISRETGKPLWEAQTEV--AAMAGKIDISIKAYH-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 145 ETMPSITKDMD----LYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDG 220
Cdd:cd07095 77 ERTGERATPMAqgraVLRHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 221 TLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFER-GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA 299
Cdd:cd07095 156 VLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 300 AGQRCMALSTAVLVG--EAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKv 377
Cdd:cd07095 236 AGQRCTCARRLIVPDgaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 378 kgyENGNFVGPTIIsNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVG 457
Cdd:cd07095 315 ---AGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVN 390
|
....*.
gi 515870065 458 VNVPIP 463
Cdd:cd07095 391 WNRPTT 396
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
49-502 |
5.63e-56 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 195.48 E-value: 5.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 49 VESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSR-------------QQKEIAKLITLEQG 115
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERaavllrfhdlvleNREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 116 KTLADAEGDVfrgLQVVehacsVTSLMMGETMPSITKD----------MDLYSYRLPLGVCAGIAPFNFPA------MIP 179
Cdd:PRK09407 106 KARRHAFEEV---LDVA-----LTARYYARRAPKLLAPrrragalpvlTKTTELRQPKGVVGVISPWNYPLtlavsdAIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 180 lwmfpmAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIkaISFVGSNKAGEYIFE 258
Cdd:PRK09407 178 ------ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVgTALVDNADY--LMFTGSTATGRVLAE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 259 RGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAGDQ 337
Cdd:PRK09407 250 QAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESiYDEFVRAFVAAVRAMRLGAGYD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 338 PGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKG---YEngnfvgPTIISNVKPNMTCYKEEIFGPVLVVLE 414
Cdd:PRK09407 330 YSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGplfYE------PTVLTGVTPDMELAREETFGPVVSVYP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 415 TETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIpvpLPMFSFTGSRSSFRGDTNF---YGKQGIQ 491
Cdd:PRK09407 404 VADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGY---AAAWGSVDAPMGGMKDSGLgrrHGAEGLL 480
|
490
....*....|.
gi 515870065 492 FYTQLKTITSQ 502
Cdd:PRK09407 481 KYTESQTIATQ 491
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
41-459 |
1.89e-53 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 187.67 E-value: 1.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 41 KLFIGGKFVESKSDKWiDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFpawaDTSVLSRQQKEIAKliTLEQGKTLAD 120
Cdd:TIGR04284 2 RLLIDGKLVAGSAGTF-PTVNPATEEVLGVAADATAADMDAAIAAARRAF----DETDWSRDTALRVR--CLRQLRDALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 121 AEGDVFRGLQVVEHACSVTsLMMGETMPSITKDM----DL---YSY-------------------RLPLGVCAGIAPFNF 174
Cdd:TIGR04284 75 AHVEELRELTIAEVGAPRM-LTAGAQLEGPVDDLgfaaDLaesYAWttdlgvaspmgiptrrtlrREAVGVVGAITPWNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 175 PAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLL-QDSGAPDGTLNII-HGQHEAVNFICDHPDIKAISFVGSNKA 252
Cdd:TIGR04284 154 PHQINLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIaEHTDFPPGVVNIVtSSDHRLGALLAKDPRVDMVSFTGSTAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 253 GEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQlvgAAFGA---AGQRCmALSTAVLVGEAKkwLPELVEHAK- 328
Cdd:TIGR04284 234 GRAVMADAAATLKKVFLELGGKSAFIVLDDADLAAACSM---AAFTVcmhAGQGC-AITTRLVVPRAR--YDEAVAAAAa 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 329 ---NLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikVKGYENGNFVGPTIISNVKPNMTCYKEEI 405
Cdd:TIGR04284 308 tmgSIKPGDPADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGR--PADRDRGFFVEPTVIAGLDNNARVAREEI 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 515870065 406 FGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:TIGR04284 386 FGPVLTVIAHDGDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVN 439
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
61-459 |
4.40e-53 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 186.61 E-value: 4.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 61 NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQK-------------EIAKLITLEQGKTLADAEGDVFR 127
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKlrdigkalrarseEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 128 GLQV----VEHACSvtslmMGETMPSITKDMD-LYSYRlPLGVCAGIAPFNFPamipLWMF-----PMaMVCGNTFLMKP 197
Cdd:PRK13968 93 SANLcdwyAEHGPA-----MLKAEPTLVENQQaVIEYR-PLGTILAIMPWNFP----LWQVmrgavPI-LLAGNGYLLKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 198 SERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHG 277
Cdd:PRK13968 162 APNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 278 VVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL-VGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCN 356
Cdd:PRK13968 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIeEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 357 LIDSGTKEGASILLDGRKIKVKGyengNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAI 436
Cdd:PRK13968 322 QVEATLAEGARLLLGGEKIAGAG----NYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATI 397
|
410 420
....*....|....*....|...
gi 515870065 437 FTTNGATARKYAHLVDVGQVGVN 459
Cdd:PRK13968 398 FTTDETQARQMAARLECGGVFIN 420
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
42-459 |
1.96e-52 |
|
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: 185.47 E-value: 1.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 42 LFIGGKFVESKSDKWIdiHNP-ATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSV-------------LSRQQKEIA 107
Cdd:cd07083 21 LVIGGEWVDTKERMVS--VSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQedrarlllkaadlLRRRRRELI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 108 KLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMG--ETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPM 185
Cdd:cd07083 99 ATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIFTGMIVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 186 AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFERGSRHG 264
Cdd:cd07083 178 PVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAARLA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 265 ------KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLV-GEAKKWLPELVEHAKNLRVNAGDQ 337
Cdd:cd07083 258 pgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTqGAYEPVLERLLKRAERLSVGPPEE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 338 PGADLGPLITPQAKERVCNLIDSGTKEGaSILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVL--ET 415
Cdd:cd07083 338 NGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGY----FVAPTVVEEVPPKARIAQEEIFGPVLSVIryKD 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 515870065 416 ETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:cd07083 413 DDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYIN 456
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
61-499 |
4.62e-52 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 183.40 E-value: 4.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 61 NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSR-------------QQKEIAKLITLEQGKTLADAEGDVF- 126
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRarwanaaadlleaEADQVAALMTLEMGKTLASAKAEALk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 127 --RGLQ-VVEHAcsvTSLMMGET--MPSITKDMDLYSYRlPLGVCAGIAPFNFPamipLWMF-----PmAMVCGNTFLMK 196
Cdd:PRK09406 87 caKGFRyYAEHA---EALLADEPadAAAVGASRAYVRYQ-PLGVVLAVMPWNFP----LWQVvrfaaP-ALMAGNVGLLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 197 PSERVPGATMLLAKLLQDSGAPDG---TLNIIHGQHEAvnfICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGA 273
Cdd:PRK09406 158 HASNVPQTALYLADLFRRAGFPDGcfqTLLVGSGAVEA---ILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 274 KNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVL---VGEAkkWLPELVEHAKNLRVNAGDQPGADLGPLITPQA 350
Cdd:PRK09406 235 SDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVhadVYDA--FAEKFVARMAALRVGDPTDPDTDVGPLATEQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 351 KERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPY 430
Cdd:PRK09406 313 RDEVEKQVDDAVAAGATILCGGKRPDGPGW----FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTF 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515870065 431 GNGTAIFTTNGATARKYAHLVDVGQVGVNvPIPVPLPMFSFTGSRSSfrGdtnfYGKQ----GIQFYTQLKTI 499
Cdd:PRK09406 389 GLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPELPFGGVKRS--G----YGRElsahGIREFCNIKTV 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
41-503 |
2.78e-51 |
|
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: 182.31 E-value: 2.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPA--WADTS-------------VLSRQQKE 105
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNardrgrlmyrladLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 106 IAKLITLEQGK--TLAdAEGDVFRGLQVVEHACSVTSLMMGETMP--SITKDMDL-YSYRLPLGVCAGIAPFNFPAMIPL 180
Cdd:cd07140 87 LATIESLDSGAvyTLA-LKTHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRNLtLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 181 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIFER 259
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 260 GSRHG-KRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEA--KKWLPELVEHAKNLRVNAGD 336
Cdd:cd07140 246 CAVSNlKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA-AGRLFVEESihDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 337 QPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYengnFVGPTIISNVKPNMTCYKEEIFGPVLVV--LE 414
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFGPIMIIskFD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 415 TETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNV--PIPVPLPMFSFtgSRSSFRGDtnfYGKQGIQF 492
Cdd:cd07140 401 DGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTynKTDVAAPFGGF--KQSGFGKD---LGEEALNE 475
|
490
....*....|.
gi 515870065 493 YTQLKTITSQW 503
Cdd:cd07140 476 YLKTKTVTIEY 486
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
43-459 |
2.26e-47 |
|
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: 171.48 E-value: 2.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 43 FIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQ--KEIAKLI---------- 110
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANilNKIADRMeanlemlava 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 111 -TLEQGKTLADAEG-------DVFRGLQVVEHACSvtslmmgETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWM 182
Cdd:cd07116 84 eTWDNGKPVRETLAadiplaiDHFRYFAGCIRAQE-------GSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 183 FPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGS 261
Cdd:cd07116 157 LAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGfGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 262 RHGKRVQANMGAKNHGVVMPD-ANKENTL--NQLVGAAFGA--AGQRCMALSTAvLVGEA--KKWLPELVEHAKNLRVNA 334
Cdd:cd07116 236 ENIIPVTLELGGKSPNIFFADvMDADDAFfdKALEGFVMFAlnQGEVCTCPSRA-LIQESiyDRFMERALERVKAIKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 335 GDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKpNMTCYKEEIFGPVLVVLE 414
Cdd:cd07116 315 PLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTT 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 515870065 415 TETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:cd07116 394 FKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN 438
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
61-461 |
4.27e-47 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 171.17 E-value: 4.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 61 NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQ-------------KEIAKLITLEQGKTLADAEGDVFR 127
Cdd:PLN02315 40 NPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEivrqigdalraklDYLGRLVSLEMGKILAEGIGEVQE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 128 GLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVP----G 203
Cdd:PLN02315 120 IIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPlitiA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 204 ATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFER-GSRHGKRVqANMGAKNHGVVMPD 282
Cdd:PLN02315 200 MTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTvNARFGKCL-LELSGNNAIIVMDD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 283 ANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDS 360
Cdd:PLN02315 279 ADIQLAVRSVLFAAVGTAGQRCTTCRR-LLLHESiyDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 361 GTKEGASILLDGRKIKvkgyENGNFVGPTIISnVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTN 440
Cdd:PLN02315 358 IKSQGGKILTGGSAIE----SEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRN 432
|
410 420
....*....|....*....|...
gi 515870065 441 GATARKY--AHLVDVGQVGVNVP 461
Cdd:PLN02315 433 PETIFKWigPLGSDCGIVNVNIP 455
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
42-431 |
8.58e-47 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 169.75 E-value: 8.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 42 LFIGGKFVESKSDKwIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQ-------------KEIAK 108
Cdd:PRK09457 3 LWINGDWIAGQGEA-FESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAiverfaalleenkEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 109 LITLEQGKTLADAegdvfrglqvvehACSVTSlMMGETMPSITKdmdlYSYRL-----------------PLGVCAGIAP 171
Cdd:PRK09457 82 VIARETGKPLWEA-------------ATEVTA-MINKIAISIQA----YHERTgekrsemadgaavlrhrPHGVVAVFGP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 172 FNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNK 251
Cdd:PRK09457 144 YNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSAN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 252 AGeYIFER--GSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTAVLVGEAKK---WLPELVEH 326
Cdd:PRK09457 224 TG-YLLHRqfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTC-ARRLLVPQGAQgdaFLARLVAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 327 AKNLRVNAGD-QPGADLGPLITPQAKERVC----NLIDSgtkeGASILLDGRKIKvkgyENGNFVGPTIIsnvkpNMTCY 401
Cdd:PRK09457 302 AKRLTVGRWDaEPQPFMGAVISEQAAQGLVaaqaQLLAL----GGKSLLEMTQLQ----AGTGLLTPGII-----DVTGV 368
|
410 420 430
....*....|....*....|....*....|....
gi 515870065 402 K----EEIFGPVLVVLETETLDEAIQIVNNNPYG 431
Cdd:PRK09457 369 AelpdEEYFGPLLQVVRYDDFDEAIRLANNTRFG 402
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
57-492 |
3.79e-42 |
|
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: 156.42 E-value: 3.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 57 IDIHNPATNEVIGRVPQATKAEMDAAIASCKRAF-------PAWADTSVLSR-------QQKEIAKLITLEQGKTLADAE 122
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFldrnnwlPAHERIAILERladlmeeRADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 123 GDVFRGLQVVEHACSVTSLMMGETMPsitkdMDL---------YSYRLPLGVCAGIAPFNFPA-MIPLWMFPmAMVCGNT 192
Cdd:cd07148 81 VEVTRAIDGVELAADELGQLGGREIP-----MGLtpasagriaFTTREPIGVVVAISAFNHPLnLIVHQVAP-AIAAGCP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 193 FLMKPSERVPGATMLLAKLLQDSGAPDGTLN-IIHGQHEAVNFICDhPDIKAISFVGSNKAGEYIFERGSRhGKRVqanm 271
Cdd:cd07148 155 VIVKPALATPLSCLAFVDLLHEAGLPEGWCQaVPCENAVAEKLVTD-PRVAFFSFIGSARVGWMLRSKLAP-GTRC---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 272 gAKNHG-----VVMPDANKENTLNQLVGAAFGAAGQRCMALSTA-VLVGEAKKWLPELVEHAKNLRVnaGDQ--PGADLG 343
Cdd:cd07148 229 -ALEHGgaapvIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVfVPAEIADDFAQRLAAAAEKLVV--GDPtdPDTEVG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 344 PLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYEngnfvgPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQ 423
Cdd:cd07148 306 PLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTYA------PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIA 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515870065 424 IVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSfrGdtnfYGKQGIQF 492
Cdd:cd07148 380 QANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDWMPFAGRRQS--G----YGTGGIPY 442
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
41-490 |
1.05e-41 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 156.07 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 41 KLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADT-------------SVLSRQQKEIA 107
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTplwkraellhkaaAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 108 KLITLEQGKTLADAEGDVFRGLQVVEHAC-------SVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPL 180
Cdd:PLN00412 97 ECLVKEIAKPAKDAVTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 181 WMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQ-HEAVNFICDHPDIKAISFVG-------SNKA 252
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKgSEIGDFLTMHPGVNCISFTGgdtgiaiSKKA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 253 GEYifergsrhgkRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALStAVLVGE--AKKWLPELVEHAKNL 330
Cdd:PLN00412 257 GMV----------PLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVK-VVLVMEsvADALVEKVNAKVAKL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 331 RVNAGDQpGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKikvkgyeNGNFVGPTIISNVKPNMTCYKEEIFGPVL 410
Cdd:PLN00412 326 TVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNVRPDMRIAWEEPFGPVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 411 VVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPiPVPLP-MFSFTGSRSSfrgdtnFYGKQG 489
Cdd:PLN00412 398 PVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA-PARGPdHFPFQGLKDS------GIGSQG 470
|
.
gi 515870065 490 I 490
Cdd:PLN00412 471 I 471
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
40-437 |
7.38e-40 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 151.59 E-value: 7.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 40 VKLFIGGKfvESKSDKWIDIHNPAT-NEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQ--KEIAKLIT----- 111
Cdd:cd07123 33 IPLVIGGK--EVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAifLKAADLLSgkyry 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 112 -------LEQGKTLADAEGDV-------FR----------GLQVVEHACSVTSLMmgetmpsitkdmdlySYRlPL-GVC 166
Cdd:cd07123 111 elnaatmLGQGKNVWQAEIDAacelidfLRfnvkyaeelyAQQPLSSPAGVWNRL---------------EYR-PLeGFV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 167 AGIAPFNFPAM------IPLWMfpmamvcGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHP 239
Cdd:cd07123 175 YAVSPFNFTAIggnlagAPALM-------GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVgDTVLASP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 240 DIKAISFVGSNKAGEYIFER-GSRHGK-----RVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTA-VL 312
Cdd:cd07123 248 HLAGLHFTGSTPTFKSLWKQiGENLDRyrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAyVP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 313 VGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKE-GASILLDGRKIKVKGYengnFVGPTII 391
Cdd:cd07123 328 ESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGY----FVEPTVI 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 515870065 392 SNVKPNMTCYKEEIFGPVLVVL--ETETLDEAIQIVNN-NPYGNGTAIF 437
Cdd:cd07123 404 ETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELVDTtSPYALTGAIF 452
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
56-459 |
3.01e-37 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 146.88 E-value: 3.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 56 WIDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQ----------QKEIAKLITL---EQGKTLADA 121
Cdd:PRK11904 563 ARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAaileraadllEANRAELIALcvrEAGKTLQDA 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 122 EGDVfRglqvvE-------HACSVTSLM-MGETMPSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTF 193
Cdd:PRK11904 643 IAEV-R-----EavdfcryYAAQARRLFgAPEKLPGPTGESNELRLH-GRGVFVCISPWNFPLAIFLGQVAAALAAGNTV 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 194 LMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIfERG--SRHGKRVQ-- 268
Cdd:PRK11904 716 IAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVgAALTADPRIAGVAFTGSTETARII-NRTlaARDGPIVPli 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 269 ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALStaVL-VGE--AKKWLPELVEHAKNLRVnaGD--QPGADLG 343
Cdd:PRK11904 795 AETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALR--VLfVQEdiADRVIEMLKGAMAELKV--GDprLLSTDVG 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 344 PLITPQAKERVCNLIDSGTKEG---ASILLDGrkikvkGYENGNFVGPTIISnvKPNMTCYKEEIFGPVLVVL--ETETL 418
Cdd:PRK11904 871 PVIDAEAKANLDAHIERMKREArllAQLPLPA------GTENGHFVAPTAFE--IDSISQLEREVFGPILHVIryKASDL 942
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 515870065 419 DEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:PRK11904 943 DKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
162-459 |
3.77e-35 |
|
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: 136.50 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 162 PLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGtLNIIHGQHEAVNFICDHP 239
Cdd:cd07087 100 PLGVVLIIGPWNYPLQ--LALAPLigAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEA-VAVVEGGVEVATALLAEP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 240 -DIkaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEAKK 318
Cdd:cd07087 177 fDH--IFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY-VLVHESIK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 319 wlPELVEHAKNlRVNA--GDQPG--ADLGPLITPQAKERVCNLIDSGTkegasILLDGRKIKVKGYengnfVGPTIISNV 394
Cdd:cd07087 254 --DELIEELKK-AIKEfyGEDPKesPDYGRIINERHFDRLASLLDDGK-----VVIGGQVDKEERY-----IAPTILDDV 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 395 KPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNP-----YgngtaIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPkplalY-----LFSEDKAVQERVLAETSSGGVCVN 385
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
162-459 |
1.51e-34 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 135.93 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 162 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLqDSGAPDGTLNIIHGQHEAVNFICDHP-D 240
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-TKYLDPSYVRVIEGGVEVTTELLKEPfD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 241 IkaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEA--KK 318
Cdd:PTZ00381 188 H--IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDY-VLVHRSikDK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 319 WLPELVEHAKNLrvnAGDQP--GADLGPLITPQAKERVCNLIDSgtkegasillDGRKIKVKGY--ENGNFVGPTIISNV 394
Cdd:PTZ00381 265 FIEALKEAIKEF---FGEDPkkSEDYSRIVNEFHTKRLAELIKD----------HGGKVVYGGEvdIENKYVAPTIIVNP 331
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515870065 395 KPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:PTZ00381 332 DLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN 396
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
59-459 |
8.06e-34 |
|
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: 133.88 E-value: 8.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 59 IHNPAT-NEVIGRVPQATKAEMDAAIASCKRAFPAWADTS-------------VLSRQQKEIAKLITLEQGKTLADAEGD 124
Cdd:TIGR01238 55 VTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPakeraakldrladLLELHMPELMALCVREAGKTIHNAIAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 125 VFRGLQVVEHACSvtslmmgetmpSITKDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGA 204
Cdd:TIGR01238 135 VREAVDFCRYYAK-----------QVRDVLGEFSVE-SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 205 TMLLAKLLQDSGAPDGTLNIIHGQHEAVN-FICDHPDIKAISFVGSNKAGEYI----FERGSRHGKRVqANMGAKNHGVV 279
Cdd:TIGR01238 203 AYRAVELMQEAGFPAGTIQLLPGRGADVGaALTSDPRIAGVAFTGSTEVAQLInqtlAQREDAPVPLI-AETGGQNAMIV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 280 MPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVEHA-KNLRVNAGDQPGADLGPLITPQAKERVCNLI 358
Cdd:TIGR01238 282 DSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAmQELKVGVPHLLTTDVGPVIDAEAKQNLLAHI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 359 DSGTKEGASILLDGRKIKVKgYENGNFVGPTIISnvKPNMTCYKEEIFGPVL--VVLETETLDEAIQIVNNNPYGNGTAI 436
Cdd:TIGR01238 362 EHMSQTQKKIAQLTLDDSRA-CQHGTFVAPTLFE--LDDIAELSEEVFGPVLhvVRYKARELDQIVDQINQTGYGLTMGV 438
|
410 420
....*....|....*....|...
gi 515870065 437 FTTNGATARKYAHLVDVGQVGVN 459
Cdd:TIGR01238 439 HSRIETTYRWIEKHARVGNCYVN 461
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
162-459 |
8.51e-33 |
|
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: 130.04 E-value: 8.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 162 PLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHEAVNFICDHP 239
Cdd:cd07134 100 PKGVCLIISPWNYPFN--LAFGPLvsAIAAGNTAILKPSELTPHTSAVIAKIIREAFDED-EVAVFEGDAEVAQALLELP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 240 dIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEAKKw 319
Cdd:cd07134 177 -FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY-VFVHESVK- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 320 lPELVEH-----AKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGrkikvKGYENGNFVGPTIISNV 394
Cdd:cd07134 254 -DAFVEHlkaeiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG-----QFDAAQRYIAPTVLTNV 327
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515870065 395 KPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:cd07134 328 TPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN 392
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
50-459 |
2.31e-30 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 126.21 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 50 ESKSDKWIDIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSV-------------LSRQQKEIAKLITLEQG 115
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVeeraaileraadlLEAHRAELMALLVREAG 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 116 KTLADAEGDVfRglqvvE-------HACSVTSLMMGETmpsitkdmdlySYRlPLGVCAGIAPFNFP---------Amip 179
Cdd:COG4230 645 KTLPDAIAEV-R-----EavdfcryYAAQARRLFAAPT-----------VLR-GRGVFVCISPWNFPlaiftgqvaA--- 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 180 lwmfpmAMVCGNTFLMKPSERVPgatmLLA----KLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAge 254
Cdd:COG4230 704 ------ALAAGNTVLAKPAEQTP----LIAaravRLLHEAGVPADVLQLLPGDGETVgAALVADPRIAGVAFTGSTET-- 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 255 yifergsrhGKRVQANMGAKNHGVVMPDAnkEnT--LN-----------QLVG----AAFGAAGQRCMALStaVL-VGE- 315
Cdd:COG4230 772 ---------ARLINRTLAARDGPIVPLIA--E-TggQNamivdssalpeQVVDdvlaSAFDSAGQRCSALR--VLcVQEd 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 316 -AKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASIlldgRKIKV-KGYENGNFVGPTI--I 391
Cdd:COG4230 838 iADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLV----HQLPLpEECANGTFVAPTLieI 913
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 392 SNVKPnmtcYKEEIFGPVLVVL--ETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN 459
Cdd:COG4230 914 DSISD----LEREVFGPVLHVVryKADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
59-431 |
1.33e-29 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 123.82 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 59 IHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSV-------------LSRQQKEIAKLITLEQGKTLADAEGD 124
Cdd:PRK11905 571 VLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAaeraaileraadlMEAHMPELFALAVREAGKTLANAIAE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 125 V--------FRGLQVvehacsvtslmmgetmpsitKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMK 196
Cdd:PRK11905 651 VreavdflrYYAAQA--------------------RRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAK 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 197 PSERVPgatmLLA----KLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGSNKAGEYIfER--GSRHGKRVQ- 268
Cdd:PRK11905 711 PAEQTP----LIAaravRLLHEAGVPKDALQLLPGDGRTVgAALVADPRIAGVMFTGSTEVARLI-QRtlAKRSGPPVPl 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 269 -ANMGAKNHGVVMPDANKEntlnQLVGA----AFGAAGQRCMALStaVL-VGE--AKKWLPELVEHAKNLRVNAGDQPGA 340
Cdd:PRK11905 786 iAETGGQNAMIVDSSALPE----QVVADviasAFDSAGQRCSALR--VLcLQEdvADRVLTMLKGAMDELRIGDPWRLST 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 341 DLGPLITPQAKERVCNLIDSGTKEGASIlldgRKIKV-KGYENGNFVGPTIISnvKPNMTCYKEEIFGPVLVVL--ETET 417
Cdd:PRK11905 860 DVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLpAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVrfKADE 933
|
410
....*....|....
gi 515870065 418 LDEAIQIVNNNPYG 431
Cdd:PRK11905 934 LDRVIDDINATGYG 947
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
162-438 |
2.60e-29 |
|
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: 120.02 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 162 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQdSGAPDGTLNIIHGQHEAVNFICDHPDI 241
Cdd:cd07135 108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVP-KYLDPDAFQVVQGGVPETTALLEQKFD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 242 KaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTaVLVGEAKkwLP 321
Cdd:cd07135 187 K-IFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDY-VLVDPSV--YD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 322 ELVEHAK---NLRVNAGDQPGADLGPLITPQAKERVCNLIDSgTKegASILLDGRKIKVKgyengNFVGPTIISNVKPNM 398
Cdd:cd07135 263 EFVEELKkvlDEFYPGGANASPDYTRIVNPRHFNRLKSLLDT-TK--GKVVIGGEMDEAT-----RFIPPTIVSDVSWDD 334
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 515870065 399 TCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFT 438
Cdd:cd07135 335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFT 374
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
58-431 |
5.87e-28 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 118.92 E-value: 5.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 58 DIHNPA-TNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSR-------------QQKEIAKLITLEQGKTLADAEG 123
Cdd:PRK11809 662 PVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERaaileraadlmeaQMQTLMGLLVREAGKTFSNAIA 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 124 DVfRglQVVE----HACSVTSlmmgetmpsitkDMDLYSYRlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSE 199
Cdd:PRK11809 742 EV-R--EAVDflryYAGQVRD------------DFDNDTHR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 200 RVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAV-NFICDHPDIKAISFVGS---------NKAGeyifeRGSRHGKRVQ- 268
Cdd:PRK11809 806 QTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVgAALVADARVRGVMFTGStevarllqrNLAG-----RLDPQGRPIPl 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 269 -ANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGE-AKKWLPELVEHAKNLRVNAGDQPGADLGPLI 346
Cdd:PRK11809 881 iAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDvADRTLKMLRGAMAECRMGNPDRLSTDIGPVI 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 347 TPQAKERVCNLIDSGTKEGASILLDGRKiKVKGYENGNFVGPTIISnvKPNMTCYKEEIFGPVLVVL--ETETLDEAIQI 424
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPVFQAARE-NSEDWQSGTFVPPTLIE--LDSFDELKREVFGPVLHVVryNRNQLDELIEQ 1037
|
....*..
gi 515870065 425 VNNNPYG 431
Cdd:PRK11809 1038 INASGYG 1044
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
157-446 |
7.30e-28 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 116.06 E-value: 7.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 157 YSYRLPLGVCAGIAPFNFPAMipLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSgAPDGTLNIIHGQHEAVNF 234
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQ--LALAPLigAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 235 IC----DHpdikaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAlSTA 310
Cdd:cd07136 172 LLdqkfDY-----IFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVA-PDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 311 VLVGEAKK--WLPELVEHAKNLRvnaGDQP--GADLGPLITPQAKERVCNLIDSGTkegasILLDGrkikvKGYENGNFV 386
Cdd:cd07136 246 VLVHESVKekFIKELKEEIKKFY---GEDPleSPDYGRIINEKHFDRLAGLLDNGK-----IVFGG-----NTDRETLYI 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515870065 387 GPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNP-----YgngtaIFTTNGATARK 446
Cdd:cd07136 313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPkplalY-----LFSEDKKVEKK 372
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
98-421 |
1.05e-26 |
|
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: 112.72 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 98 VLSRQQK---EIAKLITLEQGKT---LADAEGDV--FRGLQVVEHACSVTSLMMGEtmPSITKDMDLYSYRLPLGVCAGI 169
Cdd:cd07084 30 IIQRLAAksyDIAAGAVLVTGKGwmfAENICGDQvqLRARAFVIYSYRIPHEPGNH--LGQGLKQQSHGYRWPYGPVLVI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 170 APFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQHEAVNFICDHPDIKAISFVG 248
Cdd:cd07084 108 GAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLINGDGKTMQALLLHPNPKMVLFTG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 249 SNKAGEYIFERGsrHGKRVQANMGAKNHGVVMPDAN-KENTLNQLVGAAFGAAGQRCMALStAVLVGEAKKWLPeLVEHA 327
Cdd:cd07084 188 SSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQS-MLFVPENWSKTP-LVEKL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 328 KNLRVNAGDQpGADLGPLITPQAKERvcnlIDSGTKEGASILLDGRKIkVKGYENGNFVGPTIISNV----KPNMTCYK- 402
Cdd:cd07084 264 KALLARRKLE-DLLLGPVQTFTTLAM----IAHMENLLGSVLLFSGKE-LKNHSIPSIYGACVASALfvpiDEILKTYEl 337
|
330 340
....*....|....*....|.
gi 515870065 403 --EEIFGPVLVVLETETLDEA 421
Cdd:cd07084 338 vtEEIFGPFAIVVEYKKDQLA 358
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
162-499 |
2.18e-25 |
|
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: 108.65 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 162 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQ---DSGApdgtLNIIHGQHEAVNFICDH 238
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPeylDTKA----IKVIEGGVPETTALLEQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 239 PDIKaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA-AGQRCMALSTaVLVGEak 317
Cdd:cd07137 177 KWDK-IFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDY-VLVEE-- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 318 KWLPELVEHAKN-LRVNAGDQP--GADLGPLITPQAKERVCNLIDSgTKEGASILLDGRKIkvkgyENGNFVGPTIISNV 394
Cdd:cd07137 253 SFAPTLIDALKNtLEKFFGENPkeSKDLSRIVNSHHFQRLSRLLDD-PSVADKIVHGGERD-----EKNLYIEPTILLDP 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 395 KPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN-VPIPVPLPMFSFTG 473
Cdd:cd07137 327 PLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdTVVQYAIDTLPFGG 406
|
330 340
....*....|....*....|....*.
gi 515870065 474 SRSSfrGDTNFYGKQGIQFYTQLKTI 499
Cdd:cd07137 407 VGES--GFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
162-459 |
6.56e-23 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 101.02 E-value: 6.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 162 PLGVCAGIAPFNFP---AMIPLwmfPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHE------AV 232
Cdd:cd07133 101 PLGVVGIIVPWNYPlylALGPL---IAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED-EVAVVTGGADvaaafsSL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 233 NFicDHpdikaISFVGSnkageyifergSRHGKRVQAN-----------MGAKNHGVVMPDANKENTLNQLVGAAFGAAG 301
Cdd:cd07133 177 PF--DH-----LLFTGS-----------TAVGRHVMRAaaenltpvtleLGGKSPAIIAPDADLAKAAERIAFGKLLNAG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 302 QRCMAlSTAVLVGEAKkwLPELVEHAKNL------RVNAGDqpgaDLGPLITPQAKERVCNLIDSGTKEGASI------- 368
Cdd:cd07133 239 QTCVA-PDYVLVPEDK--LEEFVAAAKAAvakmypTLADNP----DYTSIINERHYARLQGLLEDARAKGARVielnpag 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 369 --LLDGRKIkvkgyengnfvGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNP-----YgngtaIFTTNG 441
Cdd:cd07133 312 edFAATRKL-----------PPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPrplalY-----YFGEDK 375
|
330
....*....|....*...
gi 515870065 442 ATARKYAHLVDVGQVGVN 459
Cdd:cd07133 376 AEQDRVLRRTHSGGVTIN 393
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
155-427 |
8.56e-22 |
|
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: 98.06 E-value: 8.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 155 DLYSYRLPLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEA- 231
Cdd:cd07132 93 DVYIYKEPLGVVLIIGAWNYP--LQLTLVPLvgAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVLGGVEETt 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 232 --VNFICDHpdikaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMA--- 306
Cdd:cd07132 171 elLKQRFDY-----IFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIApdy 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 307 -LSTavlvgeaKKWLPELVEHAKN-LRVNAGDQP--GADLGPLITPQAKERVCNLIDSGtkegasilldgrKIKVKGY-- 380
Cdd:cd07132 246 vLCT-------PEVQEKFVEALKKtLKEFYGEDPkeSPDYGRIINDRHFQRLKKLLSGG------------KVAIGGQtd 306
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 515870065 381 ENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNN 427
Cdd:cd07132 307 EKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINS 353
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
162-499 |
2.50e-19 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 90.88 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 162 PLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDgTLNIIHGQHEAVNFICDHPDI 241
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVVEGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 242 KaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGA-AGQRCMALSTAVlvgEAKKWL 320
Cdd:PLN02174 191 K-IFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYIL---TTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 321 PELVEHAK-NLRVNAGDQP--GADLGPLITPQAKERVCNLIDSgtKEGASILLDGRKikvKGYENGNfVGPTIISNVKPN 397
Cdd:PLN02174 267 PKVIDAMKkELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDE--KEVSDKIVYGGE---KDRENLK-IAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 398 MTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVN-VPIPVPLPMFSFTGSRS 476
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdIAVHLALHTLPFGGVGE 420
|
330 340
....*....|....*....|...
gi 515870065 477 SFRGdtNFYGKQGIQFYTQLKTI 499
Cdd:PLN02174 421 SGMG--AYHGKFSFDAFSHKKAV 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
162-446 |
1.22e-15 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 79.39 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 162 PLGVCAGIAPFNFPamIPLWMFPM--AMVCGNTFLMKPSERVPGATMLLAKLLQ---DSGApdgtLNIIHGQHEAVNFIC 236
Cdd:PLN02203 108 PLGVVLIFSSWNFP--IGLSLEPLigAIAAGNAVVLKPSELAPATSAFLAANIPkylDSKA----VKVIEGGPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 237 DHPDIKaISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENT---LNQLVGAAFGA-AGQRCMALSTaVL 312
Cdd:PLN02203 182 QHKWDK-IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSLSSSRDTkvaVNRIVGGKWGScAGQACIAIDY-VL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 313 VGEakKWLPELVEHAKN-LRVNAGDQPG--ADLGPLITPQAKERVCNLIDSgTKEGASIL----LDGRKIkvkgyengnF 385
Cdd:PLN02203 260 VEE--RFAPILIELLKStIKKFFGENPResKSMARILNKKHFQRLSNLLKD-PRVAASIVhggsIDEKKL---------F 327
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515870065 386 VGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARK 446
Cdd:PLN02203 328 IEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRR 388
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
43-425 |
2.91e-13 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 71.76 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 43 FIGGKFVESKsdKWIDIHNPATNEVIGRVPQATKAEMDA---AIASCKRA-----------FPAWADTS-----VLSRQQ 103
Cdd:cd07126 2 LVAGKWKGAS--NYTTLLDPLNGDKFISVPDTDEDEINEfvdSLRQCPKSglhnplknperYLLYGDVShrvahELRKPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 104 KE--IAKLITLEQGKTLADAEGDVFRGLQVVEHAC--SVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIP 179
Cdd:cd07126 80 VEdfFARLIQRVAPKSDAQALGEVVVTRKFLENFAgdQVRFLARSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 180 LWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKageyIFER 259
Cdd:cd07126 160 ALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSK----VAER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 260 GSR--HGKrVQANMGAKNHGVVMPDANKENTLN-QLVGAAFGAAGQRCMALStavLVGEAKKWLPE-LVEHAKNLrvnAG 335
Cdd:cd07126 236 LALelHGK-VKLEDAGFDWKILGPDVSDVDYVAwQCDQDAYACSGQKCSAQS---ILFAHENWVQAgILDKLKAL---AE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 336 DQPGADL--GPLITpQAKERVCNLIDSGTK-EGASILLDGRKIK------VKG-YENGNFVGPTIISNVKPNMTCYKEEI 405
Cdd:cd07126 309 QRKLEDLtiGPVLT-WTTERILDHVDKLLAiPGAKVLFGGKPLTnhsipsIYGaYEPTAVFVPLEEIAIEENFELVTTEV 387
|
410 420
....*....|....*....|
gi 515870065 406 FGPVLVVleTETLDEAIQIV 425
Cdd:cd07126 388 FGPFQVV--TEYKDEQLPLV 405
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
80-453 |
1.02e-12 |
|
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: 69.88 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 80 DAAIASCKRAFPAWADTSVLSRQQ--KEIAKLItleqgktlaDAEGDvfrglQVVEHACSVTSL----MMGE-------- 145
Cdd:cd07129 2 DAAAAAAAAAFESYRALSPARRAAflEAIADEI---------EALGD-----ELVARAHAETGLpearLQGElgrttgql 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 146 ------------TMPSI-TKD--------MDLYSYRLPLGVCAGIAPFNFP-AmiplwmFPM-------AMVCGNTFLMK 196
Cdd:cd07129 68 rlfadlvregswLDARIdPADpdrqplprPDLRRMLVPLGPVAVFGASNFPlA------FSVaggdtasALAAGCPVVVK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 197 PSERVPGATMLLAKL----LQDSGAPDGTLNIIHG-QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSR--HGKRVQA 269
Cdd:cd07129 142 AHPAHPGTSELVARAiraaLRATGLPAGVFSLLQGgGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 270 NMGAKNHGVVMPDANKEN--TLNQ-LVGAAFGAAGQRCmaLSTAVLVGEAKKWLPELVEHAKNLrvnAGDQPGadlGPLI 346
Cdd:cd07129 222 ELGSVNPVFILPGALAERgeAIAQgFVGSLTLGAGQFC--TNPGLVLVPAGPAGDAFIAALAEA---LAAAPA---QTML 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 347 TPqakeRVCNLIDSGTKE-----GASILLDGRkikvkGYENGNFVGPTI--------ISNVKpnmtcYKEEIFGPVLVVL 413
Cdd:cd07129 294 TP----GIAEAYRQGVEAlaaapGVRVLAGGA-----AAEGGNQAAPTLfkvdaaafLADPA-----LQEEVFGPASLVV 359
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 515870065 414 ETETLDEAIQIVNNNPyGNGTA-IFTTNGATArKYAHLVDV 453
Cdd:cd07129 360 RYDDAAELLAVAEALE-GQLTAtIHGEEDDLA-LARELLPV 398
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
164-448 |
1.13e-08 |
|
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: 57.66 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 164 GVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQheaVNFICDHPDIK 242
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHLGEQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 243 -AISFVGSNKAGEYIfeRGS----RHGKRVQANMGAKNHGVVMPDAnKENT------LNQLVGAAFGAAGQRCMALSTAv 311
Cdd:cd07128 223 dVVAFTGSAATAAKL--RAHpnivARSIRFNAEADSLNAAILGPDA-TPGTpefdlfVKEVAREMTVKAGQKCTAIRRA- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 312 LVGEAKkwLPELVE--HAKNLRVNAGD--QPGADLGPLITPQAKERVCNLIDSgTKEGASILL---DGRKIKVKGYENGN 384
Cdd:cd07128 299 FVPEAR--VDAVIEalKARLAKVVVGDprLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFggpDRFEVVGADAEKGA 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515870065 385 FVGPTII--SNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNnpyGNG---TAIFTTNGATARKYA 448
Cdd:cd07128 376 FFPPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAAR---GRGslvASVVTNDPAFARELV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
164-425 |
2.70e-05 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 46.62 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 164 GVCAGIAPFNFPAMiPLW-MFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGA-PDGTLNIIHGQHEAvnfICDH--- 238
Cdd:PRK11903 150 GVALFINAFNFPAW-GLWeKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAG---LLDHlqp 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 239 PDIkaISFVGSNKAGEYIFERGS--RHGKRVQANMGAKNHGVVMPDANKEntlnqlvGAAFGA------------AGQRC 304
Cdd:PRK11903 226 FDV--VSFTGSAETAAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAAPG-------SEAFDLfvkevvremtvkSGQKC 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 305 MALSTaVLVGEAkkwLPELVEHAKNLR---VNAGD--QPGADLGPLITPQAKERVCNLIDsGTKEGASILLDGRKIKVKG 379
Cdd:PRK11903 297 TAIRR-IFVPEA---LYDAVAEALAARlakTTVGNprNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFALVD 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 515870065 380 YEN--GNFVGPTIISNVKPN--MTCYKEEIFGPVLVVLETETLDEAIQIV 425
Cdd:PRK11903 372 ADPavAACVGPTLLGASDPDaaTAVHDVEVFGPVATLLPYRDAAHALALA 421
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
131-325 |
4.64e-05 |
|
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: 45.68 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 131 VVEHACSVTSLMMGETmpsitkdmdlYSYRLPLGVCAGIAPFNFPAMIPLWMFpMAMVCGNTFLMKPSERVPGATMLLAK 210
Cdd:cd07077 79 SVGHIQDVLLPDNGET----------YVRAFPIGVTMHILPSTNPLSGITSAL-RGIATRNQCIFRPHPSAPFTNRALAL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 211 LLQDSGAPDGTLNII----HGQHEAVNFICDHPDIKAISFVGSNKAGEYIfeRGSRHGKRVQAnMGAKNHGVVMPDANKE 286
Cdd:cd07077 148 LFQAADAAHGPKILVlyvpHPSDELAEELLSHPKIDLIVATGGRDAVDAA--VKHSPHIPVIG-FGAGNSPVVVDETADE 224
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515870065 287 NTLNQLV--GAAF-GAAgqrCMALSTAVLVGEAKKWLPELVE 325
Cdd:cd07077 225 ERASGSVhdSKFFdQNA---CASEQNLYVVDDVLDPLYEEFK 263
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
65-280 |
5.42e-04 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 42.64 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 65 NEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRqqKEIAKLITLEQGKTLAD-------AEGDVFRGLQVVEHACS 137
Cdd:cd07081 2 DDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDAR--IDLAKLAVSETGMGRVEdkviknhFAAEYIYNVYKDEKTCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515870065 138 VTSlmmGETMPSITKDMDlysyrlPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQD--- 214
Cdd:cd07081 80 VLT---GDENGGTLIIAE------PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQaav 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515870065 215 -SGAPDGTLNIIHGQH-EAVNFICDHPDIKAISFVGsnkaGEYIFERGSRHGKRVQAnMGAKNHGVVM 280
Cdd:cd07081 151 aAGAPENLIGWIDNPSiELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIG-VGAGNTPVVI 213
|
|
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