|
Name |
Accession |
Description |
Interval |
E-value |
| BetA |
COG2303 |
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ... |
58-622 |
6.06e-177 |
|
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441878 [Multi-domain] Cd Length: 531 Bit Score: 512.45 E-value: 6.06e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 58 YDFIVIGAGAAGCTLAARLSENPQVSVALIEAGGV-ENIAHLTPVVAGYLQQTSS-NWGYKSVPQKlschGMNNNECALP 135
Cdd:COG2303 5 YDYVIVGAGSAGCVLANRLSEDAGLRVLLLEAGGRdDDPLIRMPAGYAKLLGNPRyDWRYETEPQP----GLNGRRLYWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 136 RGKILGGTSSINYMIYNRGNRRDFDAWAAAGNPGWSYDEVLPYFLRSEHAQLQGleqSPYHNHSGPLSVEYVRFRSQMVD 215
Cdd:COG2303 81 RGKVLGGSSSINGMIYVRGQPEDFDLWAQLGNQGWGYDDVLPYFKRAEDNERGA---DAYHGRSGPLPVSDPPLPNPLSD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 216 AFVEASVESGLPRT-DYNGESQLGVSYVQANTLNGRRHSAYSAYIKPVRDlRSNLQIFTFSQVTRILIDEatKSAYGVEF 294
Cdd:COG2303 158 AFIEAAEELGIPRAdDFNGGACEGCGFCQVTCRNGARWSAARAYLPPALK-RPNLTVRTGALVTRILFDG--GRATGVEY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 295 HYKNKAYTFKARKEVILSAGSFNSPQLLMLSGIGPEDNLRGIGIPLIKALP-VGKRMFDHMchFGPTFVTNTTGQTTFTS 373
Cdd:COG2303 235 RDDGEEHTVRAAREVILAAGAINSPQLLLLSGIGPASHLREHGIPVVHDLPgVGRNLQDHL--EVSVVFRFKEPVTLNKS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 374 RVTPAELISFLLAGN-PATRMssigGVEALAFLktqRSNLPNDWPDIELIMVTGSLASDEGtglklganfKDEIydrmyr 452
Cdd:COG2303 313 LRKARIGLQYLLTRSgPLTSN----VAEAGGFF---RSDPGLERPDLQFHFLPLGLTPRWG---------KKAL------ 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 453 elaqAQQDHFTLLIMQFHPKSVGRLWLKDRNPLGWPKIDPKYFVAEEDVEYLLDGIKASLRIIEMPAMQRIGARllkRTV 532
Cdd:COG2303 371 ----HDGHGFTAHVEQLRPESRGRVTLDSADPLGAPLIRPNYLSDENDRRVLVAGVRLAREIAAQPALAPYRGE---EIL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 533 PGcEGHQFASDDYWrcsIRTLSYTLHHQVATCRMGaeSDPTTVVNHQLKVHGVRKLRVVDTSIIPFPPTAHTNAAAFMIG 612
Cdd:COG2303 444 PG-PDVQSDEELAF---IRARAYTIYHPVGTCRMG--TDPDSVVDPRLRVHGVENLRVVDASVMPTITSGNTNAPTIMLA 517
|
570
....*....|
gi 24642035 613 EKAADMIRTD 622
Cdd:COG2303 518 EKAADMILGD 527
|
|
| PRK02106 |
PRK02106 |
choline dehydrogenase; Validated |
58-620 |
3.46e-132 |
|
choline dehydrogenase; Validated
Pssm-ID: 235000 [Multi-domain] Cd Length: 560 Bit Score: 398.82 E-value: 3.46e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 58 YDFIVIGAGAAGCTLAARLSENPQVSVALIEAGGVENIA----HLTPVVAGYLQQTSSNWGYKSVPQKlschGMNNNECA 133
Cdd:PRK02106 6 YDYIIIGAGSAGCVLANRLSEDPDVSVLLLEAGGPDYRWdffiQMPAALAFPLQGKRYNWAYETEPEP----HMNNRRME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 134 LPRGKILGGTSSINYMIYNRGNRRDFDAWAA-AGNPGWSYDEVLPYFLRSEHAQLQGleqSPYHNHSGPLSVEY-VRFRS 211
Cdd:PRK02106 82 CPRGKVLGGSSSINGMVYIRGNAMDYDNWAElPGLEGWSYADCLPYFKKAETRDGGE---DDYRGGDGPLSVTRgKPGTN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 212 QMVDAFVEASVESGLPRT-DYNGESQLGVSYVQANTLNGRRHSAYSAYIKPVRDlRSNLQIFTFSQVTRILIDEatKSAY 290
Cdd:PRK02106 159 PLFQAFVEAGVQAGYPRTdDLNGYQQEGFGPMDRTVTNGRRWSAARAYLDPALK-RPNLTIVTHALTDRILFEG--KRAV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 291 GVEFHYKNKAYTFKARKEVILSAGSFNSPQLLMLSGIGPEDNLRGIGIPLIKALP-VGKRMFDHM-------CHfgptfv 362
Cdd:PRK02106 236 GVEYERGGGRETARARREVILSAGAINSPQLLQLSGIGPAEHLKELGIPVVHDLPgVGENLQDHLevyiqyeCK------ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 363 tnttgqttftsrvtpaELISFllagNPAT---RMSSIG--------------GVEALAFLktqRSNLPNDWPDIEL---- 421
Cdd:PRK02106 310 ----------------QPVSL----YPALkwwNKPKIGaewlftgtglgasnHFEAGGFI---RSRAGVDWPNIQYhflp 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 422 --IMVTGSLASDEgtglklganfkdeiydrmyrelaqaqqDHFTLLIMQFHPKSVGRLWLKDRNPLGWPKIDPKYFVAEE 499
Cdd:PRK02106 367 vaIRYDGSNAVKG---------------------------HGFQAHVGPMRSPSRGSVKLKSADPRAHPSILFNYMSTEQ 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 500 DVEYLLDGIKASLRIIEMPAMQRIGARLLKrtvPGCEghqFASD---DYWrcsIRTLSYTLHHQVATCRMGAesDPTTVV 576
Cdd:PRK02106 420 DWREFRDAIRLTREIMAQPALDPYRGREIS---PGAD---VQTDeeiDAF---VREHAETAYHPSCTCKMGT--DPMAVV 488
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 24642035 577 NHQLKVHGVRKLRVVDTSIIPFPPTAHTNAAAFMIGEKAADMIR 620
Cdd:PRK02106 489 DPEGRVHGVEGLRVVDASIMPTITNGNLNAPTIMIAEKAADLIR 532
|
|
| betA |
TIGR01810 |
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied ... |
59-620 |
2.31e-100 |
|
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied choline into the intermediate glycine betaine aldehyde, as part of a two-step oxidative reaction leading to the formation of osmoprotectant betaine. This enzymatic system can be found in both gram-positive and gram-negative bacteria. As in Escherichia coli, Staphylococcus xylosus, and Sinorhizobium meliloti, this enzyme is found associated in a transciptionally co-induced gene cluster with betaine aldehyde dehydrogenase, the second catalytic enzyme in this reaction. Other gram-positive organisms have been shown to employ a different enzymatic system, utlizing a soluable choline oxidase or type III alcohol dehydrogenase instead of choline dehydrogenase. This enzyme is a member of the GMC oxidoreductase family (pfam00732 and pfam05199), sharing a common evoluntionary origin and enzymatic reaction with alcohol dehydrogenase. Outgrouping from this model, Caulobacter crescentus shares sequence homology with choline dehydrogenase, yet other genes participating in this enzymatic reaction have not currently been identified. [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 273814 [Multi-domain] Cd Length: 532 Bit Score: 316.05 E-value: 2.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 59 DFIVIGAGAAGCTLAARLSENPQVSVALIEAGG----VENIAHLTPVVAGYLQQTSSNWGYKSVPQKLschgMNNNECAL 134
Cdd:TIGR01810 1 DYIIIGGGSAGSVLAGRLSEDVSNSVLVLEAGGsdypWDLLIQMPAALAYPAGNKRYNWIYETEPEPH----MNNRRVGH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 135 PRGKILGGTSSINYMIYNRGNRRDFDAWAAA-GNPGWSYDEVLPYFLRSEHAQLQgleQSPYHNHSGPLSVEYVRFRSQM 213
Cdd:TIGR01810 77 ARGKVLGGSSSINGMIYQRGNPMDYEKWAKPeGMESWDYADCLPYYKRLETTFGG---EKPYRGHDGPIKVRRGPADNPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 214 VDAFVEASVESGLPRT-DYNGESQLGVSYVQANTLNGRRHSAYSAYIKPVRDlRSNLQIFTFSQVTRILIDeaTKSAYGV 292
Cdd:TIGR01810 154 FQAFIEAGVEAGYNKTpDVNGFRQEGFGPMDSTVHNGRRVSAARAYLHPAMK-RPNLEVQTRAFVTKINFE--GNRATGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 293 EFHYKNKAYTFKARKEVILSAGSFNSPQLLMLSGIGPEDNLRGIGIPLIKALP-VGKRMFDHMCHFgptfvtnttgqtTF 371
Cdd:TIGR01810 231 EFKKGGRKEHTEANKEVILSAGAINSPQLLQLSGIGDAEHLRELGIEPRIHLPgVGENLQDHLEVY------------VQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 372 TSRVTPAELISFLlagnPATRMSSIG--------GV------EALAFLktqRSNLPNDWPDIELIMVTGSLASDeGTglk 437
Cdd:TIGR01810 299 HACKQPVSLYPSL----NWLKQPFIGaqwlfgrkGAgasnhfEGGGFV---RSNDDVDYPNIQYHFLPVAIRYD-GT--- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 438 lganfkdeiydrmyrelAQAQQDHFTLLIMQFHPKSVGRLWLKDRNPLGWPKIDPKYFVAEEDVEYLLDGIKASLRIIEM 517
Cdd:TIGR01810 368 -----------------KAPKAHGFQVHVGPMYSNSRGHVKIKSKDPFEKPEIVFNYMSHEEDWREFREAIRVTREILKQ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 518 PAMQRIGARLLKrtvPGCEGHQFASDDYWrcsIRTLSYTLHHQVATCRMGAESDPTTVVNHQLKVHGVRKLRVVDTSIIP 597
Cdd:TIGR01810 431 KALDPYRGGEIS---PGPEVQTDEEIDEF---VRRHGETALHPCGTCKMGPASDEMSVVDPETRVHGMEGLRVVDASIMP 504
|
570 580
....*....|....*....|...
gi 24642035 598 FPPTAHTNAAAFMIGEKAADMIR 620
Cdd:TIGR01810 505 RITNGNLNAPVIMMGEKAADIIR 527
|
|
| GMC_oxred_N |
pfam00732 |
GMC oxidoreductase; This family of proteins bind FAD as a cofactor. |
128-355 |
1.26e-46 |
|
GMC oxidoreductase; This family of proteins bind FAD as a cofactor.
Pssm-ID: 366272 [Multi-domain] Cd Length: 218 Bit Score: 163.61 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 128 NNNECALPRGKILGGTSSINYMIYNRGNRRDFDAWA-AAGNPGWSYDEVLPYFLRSEhaqlqgleqspyhnhsGPLSV-- 204
Cdd:pfam00732 15 NGRRMILPAGSTVGGGSSVNWSACIRTPAAVLDEWAsEFGLEGWGYDDYLPYMDKVE----------------GPLGVtt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 205 --EYVRFRSQmvdAFVEASVESGLPRT----DYNGESQLGVSYVQANTlnGRRHSAYSAYIKPVrdLRSNLQIFTFSQVT 278
Cdd:pfam00732 79 kgIEESPLNQ---ALLKAAEELGYPVEavprNSNGCHYCGFCGLGCPT--GAKQSTARTWLRPA--LERNLRILTGAKAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24642035 279 RILIDEATKSAYGVEF--HYKNKAYTFKARKEVILSAGSFNSPQLLMLSGIGPEDNlrgigiplikalPVGKRMFDHMC 355
Cdd:pfam00732 152 KIIILGRGGRAVGVEArdGGGGIKRLITAAKEVVVAAGALNTPPLLLRSGLGKNPH------------PVGKNLQLHPV 218
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| BetA |
COG2303 |
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ... |
58-622 |
6.06e-177 |
|
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441878 [Multi-domain] Cd Length: 531 Bit Score: 512.45 E-value: 6.06e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 58 YDFIVIGAGAAGCTLAARLSENPQVSVALIEAGGV-ENIAHLTPVVAGYLQQTSS-NWGYKSVPQKlschGMNNNECALP 135
Cdd:COG2303 5 YDYVIVGAGSAGCVLANRLSEDAGLRVLLLEAGGRdDDPLIRMPAGYAKLLGNPRyDWRYETEPQP----GLNGRRLYWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 136 RGKILGGTSSINYMIYNRGNRRDFDAWAAAGNPGWSYDEVLPYFLRSEHAQLQGleqSPYHNHSGPLSVEYVRFRSQMVD 215
Cdd:COG2303 81 RGKVLGGSSSINGMIYVRGQPEDFDLWAQLGNQGWGYDDVLPYFKRAEDNERGA---DAYHGRSGPLPVSDPPLPNPLSD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 216 AFVEASVESGLPRT-DYNGESQLGVSYVQANTLNGRRHSAYSAYIKPVRDlRSNLQIFTFSQVTRILIDEatKSAYGVEF 294
Cdd:COG2303 158 AFIEAAEELGIPRAdDFNGGACEGCGFCQVTCRNGARWSAARAYLPPALK-RPNLTVRTGALVTRILFDG--GRATGVEY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 295 HYKNKAYTFKARKEVILSAGSFNSPQLLMLSGIGPEDNLRGIGIPLIKALP-VGKRMFDHMchFGPTFVTNTTGQTTFTS 373
Cdd:COG2303 235 RDDGEEHTVRAAREVILAAGAINSPQLLLLSGIGPASHLREHGIPVVHDLPgVGRNLQDHL--EVSVVFRFKEPVTLNKS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 374 RVTPAELISFLLAGN-PATRMssigGVEALAFLktqRSNLPNDWPDIELIMVTGSLASDEGtglklganfKDEIydrmyr 452
Cdd:COG2303 313 LRKARIGLQYLLTRSgPLTSN----VAEAGGFF---RSDPGLERPDLQFHFLPLGLTPRWG---------KKAL------ 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 453 elaqAQQDHFTLLIMQFHPKSVGRLWLKDRNPLGWPKIDPKYFVAEEDVEYLLDGIKASLRIIEMPAMQRIGARllkRTV 532
Cdd:COG2303 371 ----HDGHGFTAHVEQLRPESRGRVTLDSADPLGAPLIRPNYLSDENDRRVLVAGVRLAREIAAQPALAPYRGE---EIL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 533 PGcEGHQFASDDYWrcsIRTLSYTLHHQVATCRMGaeSDPTTVVNHQLKVHGVRKLRVVDTSIIPFPPTAHTNAAAFMIG 612
Cdd:COG2303 444 PG-PDVQSDEELAF---IRARAYTIYHPVGTCRMG--TDPDSVVDPRLRVHGVENLRVVDASVMPTITSGNTNAPTIMLA 517
|
570
....*....|
gi 24642035 613 EKAADMIRTD 622
Cdd:COG2303 518 EKAADMILGD 527
|
|
| PRK02106 |
PRK02106 |
choline dehydrogenase; Validated |
58-620 |
3.46e-132 |
|
choline dehydrogenase; Validated
Pssm-ID: 235000 [Multi-domain] Cd Length: 560 Bit Score: 398.82 E-value: 3.46e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 58 YDFIVIGAGAAGCTLAARLSENPQVSVALIEAGGVENIA----HLTPVVAGYLQQTSSNWGYKSVPQKlschGMNNNECA 133
Cdd:PRK02106 6 YDYIIIGAGSAGCVLANRLSEDPDVSVLLLEAGGPDYRWdffiQMPAALAFPLQGKRYNWAYETEPEP----HMNNRRME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 134 LPRGKILGGTSSINYMIYNRGNRRDFDAWAA-AGNPGWSYDEVLPYFLRSEHAQLQGleqSPYHNHSGPLSVEY-VRFRS 211
Cdd:PRK02106 82 CPRGKVLGGSSSINGMVYIRGNAMDYDNWAElPGLEGWSYADCLPYFKKAETRDGGE---DDYRGGDGPLSVTRgKPGTN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 212 QMVDAFVEASVESGLPRT-DYNGESQLGVSYVQANTLNGRRHSAYSAYIKPVRDlRSNLQIFTFSQVTRILIDEatKSAY 290
Cdd:PRK02106 159 PLFQAFVEAGVQAGYPRTdDLNGYQQEGFGPMDRTVTNGRRWSAARAYLDPALK-RPNLTIVTHALTDRILFEG--KRAV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 291 GVEFHYKNKAYTFKARKEVILSAGSFNSPQLLMLSGIGPEDNLRGIGIPLIKALP-VGKRMFDHM-------CHfgptfv 362
Cdd:PRK02106 236 GVEYERGGGRETARARREVILSAGAINSPQLLQLSGIGPAEHLKELGIPVVHDLPgVGENLQDHLevyiqyeCK------ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 363 tnttgqttftsrvtpaELISFllagNPAT---RMSSIG--------------GVEALAFLktqRSNLPNDWPDIEL---- 421
Cdd:PRK02106 310 ----------------QPVSL----YPALkwwNKPKIGaewlftgtglgasnHFEAGGFI---RSRAGVDWPNIQYhflp 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 422 --IMVTGSLASDEgtglklganfkdeiydrmyrelaqaqqDHFTLLIMQFHPKSVGRLWLKDRNPLGWPKIDPKYFVAEE 499
Cdd:PRK02106 367 vaIRYDGSNAVKG---------------------------HGFQAHVGPMRSPSRGSVKLKSADPRAHPSILFNYMSTEQ 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 500 DVEYLLDGIKASLRIIEMPAMQRIGARLLKrtvPGCEghqFASD---DYWrcsIRTLSYTLHHQVATCRMGAesDPTTVV 576
Cdd:PRK02106 420 DWREFRDAIRLTREIMAQPALDPYRGREIS---PGAD---VQTDeeiDAF---VREHAETAYHPSCTCKMGT--DPMAVV 488
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 24642035 577 NHQLKVHGVRKLRVVDTSIIPFPPTAHTNAAAFMIGEKAADMIR 620
Cdd:PRK02106 489 DPEGRVHGVEGLRVVDASIMPTITNGNLNAPTIMIAEKAADLIR 532
|
|
| betA |
TIGR01810 |
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied ... |
59-620 |
2.31e-100 |
|
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied choline into the intermediate glycine betaine aldehyde, as part of a two-step oxidative reaction leading to the formation of osmoprotectant betaine. This enzymatic system can be found in both gram-positive and gram-negative bacteria. As in Escherichia coli, Staphylococcus xylosus, and Sinorhizobium meliloti, this enzyme is found associated in a transciptionally co-induced gene cluster with betaine aldehyde dehydrogenase, the second catalytic enzyme in this reaction. Other gram-positive organisms have been shown to employ a different enzymatic system, utlizing a soluable choline oxidase or type III alcohol dehydrogenase instead of choline dehydrogenase. This enzyme is a member of the GMC oxidoreductase family (pfam00732 and pfam05199), sharing a common evoluntionary origin and enzymatic reaction with alcohol dehydrogenase. Outgrouping from this model, Caulobacter crescentus shares sequence homology with choline dehydrogenase, yet other genes participating in this enzymatic reaction have not currently been identified. [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 273814 [Multi-domain] Cd Length: 532 Bit Score: 316.05 E-value: 2.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 59 DFIVIGAGAAGCTLAARLSENPQVSVALIEAGG----VENIAHLTPVVAGYLQQTSSNWGYKSVPQKLschgMNNNECAL 134
Cdd:TIGR01810 1 DYIIIGGGSAGSVLAGRLSEDVSNSVLVLEAGGsdypWDLLIQMPAALAYPAGNKRYNWIYETEPEPH----MNNRRVGH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 135 PRGKILGGTSSINYMIYNRGNRRDFDAWAAA-GNPGWSYDEVLPYFLRSEHAQLQgleQSPYHNHSGPLSVEYVRFRSQM 213
Cdd:TIGR01810 77 ARGKVLGGSSSINGMIYQRGNPMDYEKWAKPeGMESWDYADCLPYYKRLETTFGG---EKPYRGHDGPIKVRRGPADNPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 214 VDAFVEASVESGLPRT-DYNGESQLGVSYVQANTLNGRRHSAYSAYIKPVRDlRSNLQIFTFSQVTRILIDeaTKSAYGV 292
Cdd:TIGR01810 154 FQAFIEAGVEAGYNKTpDVNGFRQEGFGPMDSTVHNGRRVSAARAYLHPAMK-RPNLEVQTRAFVTKINFE--GNRATGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 293 EFHYKNKAYTFKARKEVILSAGSFNSPQLLMLSGIGPEDNLRGIGIPLIKALP-VGKRMFDHMCHFgptfvtnttgqtTF 371
Cdd:TIGR01810 231 EFKKGGRKEHTEANKEVILSAGAINSPQLLQLSGIGDAEHLRELGIEPRIHLPgVGENLQDHLEVY------------VQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 372 TSRVTPAELISFLlagnPATRMSSIG--------GV------EALAFLktqRSNLPNDWPDIELIMVTGSLASDeGTglk 437
Cdd:TIGR01810 299 HACKQPVSLYPSL----NWLKQPFIGaqwlfgrkGAgasnhfEGGGFV---RSNDDVDYPNIQYHFLPVAIRYD-GT--- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 438 lganfkdeiydrmyrelAQAQQDHFTLLIMQFHPKSVGRLWLKDRNPLGWPKIDPKYFVAEEDVEYLLDGIKASLRIIEM 517
Cdd:TIGR01810 368 -----------------KAPKAHGFQVHVGPMYSNSRGHVKIKSKDPFEKPEIVFNYMSHEEDWREFREAIRVTREILKQ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 518 PAMQRIGARLLKrtvPGCEGHQFASDDYWrcsIRTLSYTLHHQVATCRMGAESDPTTVVNHQLKVHGVRKLRVVDTSIIP 597
Cdd:TIGR01810 431 KALDPYRGGEIS---PGPEVQTDEEIDEF---VRRHGETALHPCGTCKMGPASDEMSVVDPETRVHGMEGLRVVDASIMP 504
|
570 580
....*....|....*....|...
gi 24642035 598 FPPTAHTNAAAFMIGEKAADMIR 620
Cdd:TIGR01810 505 RITNGNLNAPVIMMGEKAADIIR 527
|
|
| Rv0697 |
TIGR03970 |
dehydrogenase, Rv0697 family; This model describes a set of dehydrogenases belonging to the ... |
59-620 |
6.07e-72 |
|
dehydrogenase, Rv0697 family; This model describes a set of dehydrogenases belonging to the glucose-methanol-choline oxidoreductase (GMC oxidoreductase) family. Members of the present family are restricted to Actinobacterial genome contexts containing also members of families TIGR03962 and TIGR03969 (the mycofactocin system), and are proposed to be uniform in function.
Pssm-ID: 274888 [Multi-domain] Cd Length: 487 Bit Score: 240.10 E-value: 6.07e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 59 DFIVIGAGAAGCTLAARLSENPQVSVALIEAG-GVENIAHLTPVVAGYLQ-----QTSSNWGYKS----VPQKLSchgmn 128
Cdd:TIGR03970 2 DVLIVGAGSAGSVLAARLSEDPSCTVTVLEAGpGYRDPSRLPAQLTDGLRlpigpASPVVWRYGVeltdGPRRAS----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 129 nnecALPRGKILGGTSSINYMIYNRGNRRDFDAWAAagnPGWSYDEVLPYFLRSEhaqlQGLE-QSPYHNHSGPLSVEYV 207
Cdd:TIGR03970 77 ----QIVRGRVLGGSGAVNGGYFCRALPADFDAWPI---PGWSWDDVLPHFRAIE----TDLDfDGPLHGTAGPIPVRRT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 208 RFRSQMVDAFVEASVESGLP-RTDYNG---ESQLGVSYVQANTLNGRRHSAYSAYIKPVRDlRSNLQIFTFSQVTRILId 283
Cdd:TIGR03970 146 AELDGISAAFVAAALGAGFGwIADLNGsgpGLPGGVGAVPLNVDGGRRVSTAVAYLLPALK-RPNLTVEADTRVVRILF- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 284 EATKsAYGVEFHYKNKAYTFKARKeVILSAGSFNSPQLLMLSGIGPEDNLRGIGIPLIKALPVGKRMFDHmchfgPTFVT 363
Cdd:TIGR03970 224 SGTR-AVGVEVLGDGGPRTLRADR-VVLCAGAVESAHLLLLSGIGPAEQLRAAGIAVVLDLPVGSDFVDH-----PEWVL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 364 NTtgqttftsRVTPaelisfllagnPATRMSSIGGVEALafLKTQrsnlpndwpDIELIMVTGSlasdegtglklganFK 443
Cdd:TIGR03970 297 PY--------RWRP-----------THDRPPTSPVLETV--LNTA---------DIEIRPYTAG--------------FT 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 444 DEIYDRmyrelaQAQQDHFTLLIMQfhPKSVGRLWLKDRNPLGWPKIDPKYFVAEEDVEYLLDGIKASLRIIEMPAMQRI 523
Cdd:TIGR03970 333 ALVPGS------PRDDPHLGVALMR--PHSRGRIRLASADPADPPRIEHRYDSSAADRAALRAGAALAHELLGSPELGPL 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 524 GARLLKRtvpgceghqfaSDDYWrcsIRTLSYTLHHQVATCRMGAESDPTTVVNHQLKVHGVRKLRVVDTSIIPFPPTAH 603
Cdd:TIGR03970 405 LEPAVRE-----------GEASW---VLARLATSQHLCGSCRMGGRDDPGAVVDARCRVRGVEGLWVVDGSILPVIPSRG 470
|
570
....*....|....*..
gi 24642035 604 TNAAAFMIGEKAADMIR 620
Cdd:TIGR03970 471 PHATAVMVAERAAEFLG 487
|
|
| GMC_oxred_N |
pfam00732 |
GMC oxidoreductase; This family of proteins bind FAD as a cofactor. |
128-355 |
1.26e-46 |
|
GMC oxidoreductase; This family of proteins bind FAD as a cofactor.
Pssm-ID: 366272 [Multi-domain] Cd Length: 218 Bit Score: 163.61 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 128 NNNECALPRGKILGGTSSINYMIYNRGNRRDFDAWA-AAGNPGWSYDEVLPYFLRSEhaqlqgleqspyhnhsGPLSV-- 204
Cdd:pfam00732 15 NGRRMILPAGSTVGGGSSVNWSACIRTPAAVLDEWAsEFGLEGWGYDDYLPYMDKVE----------------GPLGVtt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 205 --EYVRFRSQmvdAFVEASVESGLPRT----DYNGESQLGVSYVQANTlnGRRHSAYSAYIKPVrdLRSNLQIFTFSQVT 278
Cdd:pfam00732 79 kgIEESPLNQ---ALLKAAEELGYPVEavprNSNGCHYCGFCGLGCPT--GAKQSTARTWLRPA--LERNLRILTGAKAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24642035 279 RILIDEATKSAYGVEF--HYKNKAYTFKARKEVILSAGSFNSPQLLMLSGIGPEDNlrgigiplikalPVGKRMFDHMC 355
Cdd:pfam00732 152 KIIILGRGGRAVGVEArdGGGGIKRLITAAKEVVVAAGALNTPPLLLRSGLGKNPH------------PVGKNLQLHPV 218
|
|
| GMC_oxred_C |
pfam05199 |
GMC oxidoreductase; This domain found associated with pfam00732. |
471-615 |
1.03e-42 |
|
GMC oxidoreductase; This domain found associated with pfam00732.
Pssm-ID: 398739 [Multi-domain] Cd Length: 143 Bit Score: 150.24 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 471 PKSVGRLWLKDRNPLGWPKIDPKYFVAEEDVEYLLDGIKASLRIIEMPAMqRIGARLLKRTVPGCEGHQFASDDYWRCSI 550
Cdd:pfam05199 1 PRSRGRVTLSSSDPTGLPVIDPNYLSDPADLAALRAALRLARRILAAAGL-VLGVELTPGPVPEVSDAAVTSDDELLAYI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24642035 551 RTLSYTLHHQVATCRMGAESDPTtVVNHQLKVHGVRKLRVVDTSIIPFPPTAHTNAAAFMIGEKA 615
Cdd:pfam05199 80 RAAASTSYHPMGTCRMGADPDDA-VVDPDLRVHGVDNLRVVDASVFPSSPSGNPTLTIYALAERA 143
|
|
| PLN02785 |
PLN02785 |
Protein HOTHEAD |
56-612 |
2.17e-24 |
|
Protein HOTHEAD
Pssm-ID: 215420 [Multi-domain] Cd Length: 587 Bit Score: 107.58 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 56 SNYDFIVIGAGAAGCTLAARLSENpqVSVALIEAGGV----ENIAHLTPVVAGyLQQTSSNwgykSVPQK-LSCHGMNNn 130
Cdd:PLN02785 54 SAYDYIVVGGGTAGCPLAATLSQN--FSVLLLERGGVpfgnANVSFLENFHIG-LADTSPT----SASQAfISTDGVIN- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 131 ecalPRGKILGGTSSINYMIYNRGNRRDFDawaaagNPGWSYDEVLPYFLRSEHAQLQGLEQSPYHnhsgplsveyVRFR 210
Cdd:PLN02785 126 ----ARARVLGGGTCINAGFYSRASTRFIQ------KAGWDAKLVNESYPWVERQIVHWPKVAPWQ----------AALR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 211 sqmvDAFVEASVesglprTDYNGESQLGVSYVQ-ANTL---NGRRHSAYS--AYIKPvrdlrSNLQIFTFSQVTRILIDE 284
Cdd:PLN02785 186 ----DSLLEVGV------SPFNGFTYDHVYGTKvGGTIfdeFGRRHTAAEllAAGNP-----NKLRVLLHATVQKIVFDT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 285 ATKS--AYGVEFHYKN----KAY-TFKARKEVILSAGSFNSPQLLMLSGIGPEDNLRGIGIPLI-KALPVGKRMFDhmch 356
Cdd:PLN02785 251 SGKRprATGVIFKDENgnqhQAFlSNNKGSEIILSAGAIGSPQMLLLSGIGPKKELKKHKIPVVlHNEHVGKGMAD---- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 357 fgptfvtnttgqttftsrvtpaelisfllagNPatrMSSIggvealaFLKTQRSnlpndwPDIELIMVTGslASDEGTGL 436
Cdd:PLN02785 327 -------------------------------NP---MNSI-------FVPSKAP------VEQSLIQTVG--ITKMGVYI 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 437 KLGANF---KDEI---YDRMYRELAQ------------AQQDHFT----LLIMQFH----------PKSVGRLWLKDRNP 484
Cdd:PLN02785 358 EASSGFgqsPDSIhchHGIMSAEIGQlstippkqrtpeAIQAYIHrkknLPHEAFNggfilekiagPISTGHLSLINTNV 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24642035 485 LGWPKIDPKYFVAEEDVEYLLDGIKASLRIIEMP-----------AMQRIGARLLKRTVPGCEGH--------QFASDDY 545
Cdd:PLN02785 438 DDNPSVTFNYFKHPQDLQRCVYGIRTIEKIVKTNhftnftqcdkqTMEKVLNMSVKANINLIPKHtndtksleQFCKDTV 517
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24642035 546 wrcsirtlsYTLHHQVATCRMGaesdptTVVNHQLKVHGVRKLRVVDTSIIPFPPTAHTNAAAFMIG 612
Cdd:PLN02785 518 ---------ITIWHYHGGCHVG------KVVDQNYKVLGVSRLRVIDGSTFDESPGTNPQATVMMMG 569
|
|
| Lycopene_cycl |
pfam05834 |
Lycopene cyclase protein; This family consists of lycopene beta and epsilon cyclase proteins. ... |
59-90 |
9.11e-05 |
|
Lycopene cyclase protein; This family consists of lycopene beta and epsilon cyclase proteins. Carotenoids with cyclic end groups are essential components of the photosynthetic membranes in all plants, algae, and cyanobacteria. These lipid-soluble compounds protect against photo-oxidation, harvest light for photosynthesis, and dissipate excess light energy absorbed by the antenna pigments. The cyclization of lycopene (psi, psi-carotene) is a key branch point in the pathway of carotenoid biosynthesis. Two types of cyclic end groups are found in higher plant carotenoids: the beta and epsilon rings. Carotenoids with two beta rings are ubiquitous, and those with one beta and one epsilon ring are common; however, carotenoids with two epsilon rings are rare.
Pssm-ID: 310433 [Multi-domain] Cd Length: 380 Bit Score: 45.10 E-value: 9.11e-05
10 20 30
....*....|....*....|....*....|...
gi 24642035 59 DFIVIGAGAAGCTLAARLSEN-PQVSVALIEAG 90
Cdd:pfam05834 1 DVVIIGAGPAGLSLAARLAAAkPGLSVVLIEPG 33
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
58-89 |
1.15e-04 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 44.75 E-value: 1.15e-04
10 20 30
....*....|....*....|....*....|..
gi 24642035 58 YDFIVIGAGAAGCTLAARLSENPQVSVALIEA 89
Cdd:COG0579 5 YDVVIIGAGIVGLALARELSRYEDLKVLVLEK 36
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
58-88 |
1.43e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 44.81 E-value: 1.43e-04
10 20 30
....*....|....*....|....*....|.
gi 24642035 58 YDFIVIGAGAAGCTLAARLSENPQvSVALIE 88
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGM-KVALIE 35
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
58-92 |
1.85e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 44.13 E-value: 1.85e-04
10 20 30
....*....|....*....|....*....|....*
gi 24642035 58 YDFIVIGAGAAGCTLAARLSENpQVSVALIEAGGV 92
Cdd:COG0665 3 ADVVVIGGGIAGLSTAYHLARR-GLDVTVLERGRP 36
|
|
| PLN02661 |
PLN02661 |
Putative thiazole synthesis |
59-88 |
8.20e-04 |
|
Putative thiazole synthesis
Pssm-ID: 178267 Cd Length: 357 Bit Score: 42.12 E-value: 8.20e-04
10 20 30
....*....|....*....|....*....|
gi 24642035 59 DFIVIGAGAAGCTLAARLSENPQVSVALIE 88
Cdd:PLN02661 94 DVVIVGAGSAGLSCAYELSKNPNVKVAIIE 123
|
|
| NadB |
COG0029 |
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ... |
57-113 |
1.16e-03 |
|
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439800 [Multi-domain] Cd Length: 521 Bit Score: 42.02 E-value: 1.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 24642035 57 NYDFIVIGAGAAGCTLAARLSENPQVSValieaggveniahltpVVAGYLQQTSSNW 113
Cdd:COG0029 4 KTDVLVIGSGIAGLSAALKLAERGRVTL----------------LTKGELGESNTRW 44
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
59-90 |
2.70e-03 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 40.46 E-value: 2.70e-03
10 20 30
....*....|....*....|....*....|..
gi 24642035 59 DFIVIGAGAAGCTLAARLSENPQvSVALIEAG 90
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGL-SVTLLERG 31
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
59-96 |
2.92e-03 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 40.35 E-value: 2.92e-03
10 20 30
....*....|....*....|....*....|....*...
gi 24642035 59 DFIVIGAGAAGCTLAARLSENPQvSVALIEAGGVENIA 96
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGL-KVAVVEKGQPFGGA 37
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
57-92 |
3.18e-03 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 40.46 E-value: 3.18e-03
10 20 30
....*....|....*....|....*....|....*....
gi 24642035 57 NYDFIVIGAGAAGCTLAARLSENpQVSVALIEA---GGV 92
Cdd:COG1249 3 DYDLVVIGAGPGGYVAAIRAAQL-GLKVALVEKgrlGGT 40
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
57-88 |
6.35e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 39.35 E-value: 6.35e-03
10 20 30
....*....|....*....|....*....|..
gi 24642035 57 NYDFIVIGAGAAGCTLAARLSENPQvSVALIE 88
Cdd:PRK07251 3 TYDLIVIGFGKAGKTLAAKLASAGK-KVALVE 33
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
62-90 |
6.36e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 35.58 E-value: 6.36e-03
10 20
....*....|....*....|....*....
gi 24642035 62 VIGAGAAGCTLAARLSENpQVSVALIEAG 90
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKR-GFRVLVLEKR 28
|
|
|