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Conserved domains on  [gi|1198878507|ref|WP_086994570|]
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GMC family oxidoreductase [Pseudoalteromonas sp. JB197]

Protein Classification

GMC family oxidoreductase( domain architecture ID 11455227)

GMC (glucose-methanol-choline) family oxidoreductase is a flavoprotein that catalyzes the oxidation of an alcohol moiety to the corresponding aldehyde with the concomitant reduction of flavin adenine dinucleotide (FAD)

EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0050660
PubMed:  23578136|1542121
SCOP:  3000055

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 1-533 0e+00

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: 706.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507   1 MNTTFDYIVVGAGSAGCVIASRLSENANVSVCLIEAGSSDNTAFVQMPAGVAASVPYGINSWHYNTVAQKELNNRCGFMP 80
Cdd:COG2303     1 MLEEYDYVIVGAGSAGCVLANRLSEDAGLRVLLLEAGGRDDDPLIRMPAGYAKLLGNPRYDWRYETEPQPGLNGRRLYWP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507  81 RGKVLGGSSSINAMVYIRGNKYDYDQWAANGNSGWDYDSLLPYFIKAENNKTFTNsELHGTQGPLHVQELNEPSPVNQCF 160
Cdd:COG2303    81 RGKVLGGSSSINGMIYVRGQPEDFDLWAQLGNQGWGYDDVLPYFKRAEDNERGAD-AYHGRSGPLPVSDPPLPNPLSDAF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 161 LNACVEQGVSLNNDINATEQQGARLSQVTQHNGERCSAAKAYLTPHLKRANLTVLTNSHVNKVIINNNMAQGVQIERNKQ 240
Cdd:COG2303   160 IEAAEELGIPRADDFNGGACEGCGFCQVTCRNGARWSAARAYLPPALKRPNLTVRTGALVTRILFDGGRATGVEYRDDGE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 241 VVNLYANNEVILSAGAINSPQLLMLSGVGPSNHLLAHNIKVIVPLEGVGANLHDHLTVVPLYRAKTSKgtfglSIPGAAR 320
Cdd:COG2303   240 EHTVRAAREVILAAGAINSPQLLLLSGIGPASHLREHGIPVVHDLPGVGRNLQDHLEVSVVFRFKEPV-----TLNKSLR 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 321 VLKGCIDWFSKRQGCLTTNFAESHAFIKLFDDSPAPDVQLEFV-LGLVDDHSR-KLHTGHGYSIHSSIMRPKSRGAVKLA 398
Cdd:COG2303   315 KARIGLQYLLTRSGPLTSNVAEAGGFFRSDPGLERPDLQFHFLpLGLTPRWGKkALHDGHGFTAHVEQLRPESRGRVTLD 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 399 DSDPRSAPLIDPNYLSHPDDIKVMLQGLKKTLQIMQSSAFDAIRGDMVYPLDINNDEQLIEFIRQTADTEYHPVGTCKMG 478
Cdd:COG2303   395 SADPLGAPLIRPNYLSDENDRRVLVAGVRLAREIAAQPALAPYRGEEILPGPDVQSDEELAFIRARAYTIYHPVGTCRMG 474

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1198878507 479 NDPLAVVDNELRVYAIQGLRVVDASIMPSIITGNTNAAVIAIAEKAADLIKQANP 533
Cdd:COG2303   475 TDPDSVVDPRLRVHGVENLRVVDASVMPTITSGNTNAPTIMLAEKAADMILGDYL 529
 
Name Accession Description Interval E-value
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 1-533 0e+00

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: 706.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507   1 MNTTFDYIVVGAGSAGCVIASRLSENANVSVCLIEAGSSDNTAFVQMPAGVAASVPYGINSWHYNTVAQKELNNRCGFMP 80
Cdd:COG2303     1 MLEEYDYVIVGAGSAGCVLANRLSEDAGLRVLLLEAGGRDDDPLIRMPAGYAKLLGNPRYDWRYETEPQPGLNGRRLYWP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507  81 RGKVLGGSSSINAMVYIRGNKYDYDQWAANGNSGWDYDSLLPYFIKAENNKTFTNsELHGTQGPLHVQELNEPSPVNQCF 160
Cdd:COG2303    81 RGKVLGGSSSINGMIYVRGQPEDFDLWAQLGNQGWGYDDVLPYFKRAEDNERGAD-AYHGRSGPLPVSDPPLPNPLSDAF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 161 LNACVEQGVSLNNDINATEQQGARLSQVTQHNGERCSAAKAYLTPHLKRANLTVLTNSHVNKVIINNNMAQGVQIERNKQ 240
Cdd:COG2303   160 IEAAEELGIPRADDFNGGACEGCGFCQVTCRNGARWSAARAYLPPALKRPNLTVRTGALVTRILFDGGRATGVEYRDDGE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 241 VVNLYANNEVILSAGAINSPQLLMLSGVGPSNHLLAHNIKVIVPLEGVGANLHDHLTVVPLYRAKTSKgtfglSIPGAAR 320
Cdd:COG2303   240 EHTVRAAREVILAAGAINSPQLLLLSGIGPASHLREHGIPVVHDLPGVGRNLQDHLEVSVVFRFKEPV-----TLNKSLR 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 321 VLKGCIDWFSKRQGCLTTNFAESHAFIKLFDDSPAPDVQLEFV-LGLVDDHSR-KLHTGHGYSIHSSIMRPKSRGAVKLA 398
Cdd:COG2303   315 KARIGLQYLLTRSGPLTSNVAEAGGFFRSDPGLERPDLQFHFLpLGLTPRWGKkALHDGHGFTAHVEQLRPESRGRVTLD 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 399 DSDPRSAPLIDPNYLSHPDDIKVMLQGLKKTLQIMQSSAFDAIRGDMVYPLDINNDEQLIEFIRQTADTEYHPVGTCKMG 478
Cdd:COG2303   395 SADPLGAPLIRPNYLSDENDRRVLVAGVRLAREIAAQPALAPYRGEEILPGPDVQSDEELAFIRARAYTIYHPVGTCRMG 474

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1198878507 479 NDPLAVVDNELRVYAIQGLRVVDASIMPSIITGNTNAAVIAIAEKAADLIKQANP 533
Cdd:COG2303   475 TDPDSVVDPRLRVHGVENLRVVDASVMPTITSGNTNAPTIMLAEKAADMILGDYL 529
PRK02106 PRK02106
choline dehydrogenase; Validated
 1-529 0e+00

choline dehydrogenase; Validated


Pssm-ID: 235000 [Multi-domain]  Cd Length: 560  Bit Score: 601.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507   1 MNTTFDYIVVGAGSAGCVIASRLSENANVSVCLIEAGSSDNTA--FVQMPAGVAasvpYGINS----WHYNTVAQKELNN 74
Cdd:PRK02106    2 TTMEYDYIIIGAGSAGCVLANRLSEDPDVSVLLLEAGGPDYRWdfFIQMPAALA----FPLQGkrynWAYETEPEPHMNN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507  75 RCGFMPRGKVLGGSSSINAMVYIRGNKYDYDQWAAN-GNSGWDYDSLLPYFIKAENNKtFTNSELHGTQGPLHVQELNEP 153
Cdd:PRK02106   78 RRMECPRGKVLGGSSSINGMVYIRGNAMDYDNWAELpGLEGWSYADCLPYFKKAETRD-GGEDDYRGGDGPLSVTRGKPG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 154 -SPVNQCFLNACVEQGVSLNNDINATEQQGARLSQVTQHNGERCSAAKAYLTPHLKRANLTVLTNSHVNKVIINNNMAQG 232
Cdd:PRK02106  157 tNPLFQAFVEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTNGRRWSAARAYLDPALKRPNLTIVTHALTDRILFEGKRAVG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 233 VQIERNKQVVNLYANNEVILSAGAINSPQLLMLSGVGPSNHLLAHNIKVIVPLEGVGANLHDHLTV---------VPLYR 303
Cdd:PRK02106  237 VEYERGGGRETARARREVILSAGAINSPQLLQLSGIGPAEHLKELGIPVVHDLPGVGENLQDHLEVyiqyeckqpVSLYP 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 304 A--KTSKGTFGLSipgaarvlkgcidWFSKRQGCLTTNFAESHAFIKLFDDSPAPDVQLEFVLGLVDDHSRKLHTGHGYS 381
Cdd:PRK02106  317 AlkWWNKPKIGAE-------------WLFTGTGLGASNHFEAGGFIRSRAGVDWPNIQYHFLPVAIRYDGSNAVKGHGFQ 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 382 IHSSIMRPKSRGAVKLADSDPRSAPLIDPNYLSHPDDIKVMLQGLKKTLQIMQSSAFDAIRGDMVYP-LDINNDEQLIEF 460
Cdd:PRK02106  384 AHVGPMRSPSRGSVKLKSADPRAHPSILFNYMSTEQDWREFRDAIRLTREIMAQPALDPYRGREISPgADVQTDEEIDAF 463

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1198878507 461 IRQTADTEYHPVGTCKMGNDPLAVVDNELRVYAIQGLRVVDASIMPSIITGNTNAAVIAIAEKAADLIK 529
Cdd:PRK02106  464 VREHAETAYHPSCTCKMGTDPMAVVDPEGRVHGVEGLRVVDASIMPTITNGNLNAPTIMIAEKAADLIR 532
betA TIGR01810
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied ...
 6-533 1.72e-156

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: 457.03  E-value: 1.72e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507   6 DYIVVGAGSAGCVIASRLSENANVSVCLIEAGSSD--NTAFVQMPAGVAASVPYGINSWHYNTVAQKELNNRCGFMPRGK 83
Cdd:TIGR01810   1 DYIIIGGGSAGSVLAGRLSEDVSNSVLVLEAGGSDypWDLLIQMPAALAYPAGNKRYNWIYETEPEPHMNNRRVGHARGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507  84 VLGGSSSINAMVYIRGNKYDYDQWAAN-GNSGWDYDSLLPYFIKAENnkTFTNSE-LHGTQGPLHVQELNEPSPVNQCFL 161
Cdd:TIGR01810  81 VLGGSSSINGMIYQRGNPMDYEKWAKPeGMESWDYADCLPYYKRLET--TFGGEKpYRGHDGPIKVRRGPADNPLFQAFI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 162 NACVEQGVSLNNDINATEQQGARLSQVTQHNGERCSAAKAYLTPHLKRANLTVLTNSHVNKVIINNNMAQGVQIERNKQV 241
Cdd:TIGR01810 159 EAGVEAGYNKTPDVNGFRQEGFGPMDSTVHNGRRVSAARAYLHPAMKRPNLEVQTRAFVTKINFEGNRATGVEFKKGGRK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 242 VNLYANNEVILSAGAINSPQLLMLSGVGPSNHLLAHNIKVIVPLEGVGANLHDHLTVvplYRAKTSKGTFGLSiPGAARV 321
Cdd:TIGR01810 239 EHTEANKEVILSAGAINSPQLLQLSGIGDAEHLRELGIEPRIHLPGVGENLQDHLEV---YVQHACKQPVSLY-PSLNWL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 322 LKGCI--DWFSKRQGCLTTNFAESHAFIKLFDDSPAPDVQLEFVLGLVDDHSRKLHTGHGYSIHSSIMRPKSRGAVKLAD 399
Cdd:TIGR01810 315 KQPFIgaQWLFGRKGAGASNHFEGGGFVRSNDDVDYPNIQYHFLPVAIRYDGTKAPKAHGFQVHVGPMYSNSRGHVKIKS 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 400 SDPRSAPLIDPNYLSHPDDIKVMLQGLKKTLQIMQSSAFDAIRGDMVYP-LDINNDEQLIEFIRQTADTEYHPVGTCKMG 478
Cdd:TIGR01810 395 KDPFEKPEIVFNYMSHEEDWREFREAIRVTREILKQKALDPYRGGEISPgPEVQTDEEIDEFVRRHGETALHPCGTCKMG 474

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1198878507 479 --NDPLAVVDNELRVYAIQGLRVVDASIMPSIITGNTNAAVIAIAEKAADLIKQANP 533
Cdd:TIGR01810 475 paSDEMSVVDPETRVHGMEGLRVVDASIMPRITNGNLNAPVIMMGEKAADIIRGKKP 531
GMC_oxred_C pfam05199
GMC oxidoreductase; This domain found associated with pfam00732.
 389-524 1.41e-49

GMC oxidoreductase; This domain found associated with pfam00732.


Pssm-ID: 398739 [Multi-domain]  Cd Length: 143  Bit Score: 167.19  E-value: 1.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 389 PKSRGAVKLADSDPRSAPLIDPNYLSHPDDIKVMLQGLKKTLQIMQSSAFDAIRGDMVYPLDI------NNDEQLIEFIR 462
Cdd:pfam05199   1 PRSRGRVTLSSSDPTGLPVIDPNYLSDPADLAALRAALRLARRILAAAGLVLGVELTPGPVPEvsdaavTSDDELLAYIR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1198878507 463 QTADTEYHPVGTCKMGNDPL-AVVDNELRVYAIQGLRVVDASIMPSIITGNTNAAVIAIAEKA 524
Cdd:pfam05199  81 AAASTSYHPMGTCRMGADPDdAVVDPDLRVHGVDNLRVVDASVFPSSPSGNPTLTIYALAERA 143
 
Name Accession Description Interval E-value
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 1-533 0e+00

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: 706.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507   1 MNTTFDYIVVGAGSAGCVIASRLSENANVSVCLIEAGSSDNTAFVQMPAGVAASVPYGINSWHYNTVAQKELNNRCGFMP 80
Cdd:COG2303     1 MLEEYDYVIVGAGSAGCVLANRLSEDAGLRVLLLEAGGRDDDPLIRMPAGYAKLLGNPRYDWRYETEPQPGLNGRRLYWP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507  81 RGKVLGGSSSINAMVYIRGNKYDYDQWAANGNSGWDYDSLLPYFIKAENNKTFTNsELHGTQGPLHVQELNEPSPVNQCF 160
Cdd:COG2303    81 RGKVLGGSSSINGMIYVRGQPEDFDLWAQLGNQGWGYDDVLPYFKRAEDNERGAD-AYHGRSGPLPVSDPPLPNPLSDAF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 161 LNACVEQGVSLNNDINATEQQGARLSQVTQHNGERCSAAKAYLTPHLKRANLTVLTNSHVNKVIINNNMAQGVQIERNKQ 240
Cdd:COG2303   160 IEAAEELGIPRADDFNGGACEGCGFCQVTCRNGARWSAARAYLPPALKRPNLTVRTGALVTRILFDGGRATGVEYRDDGE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 241 VVNLYANNEVILSAGAINSPQLLMLSGVGPSNHLLAHNIKVIVPLEGVGANLHDHLTVVPLYRAKTSKgtfglSIPGAAR 320
Cdd:COG2303   240 EHTVRAAREVILAAGAINSPQLLLLSGIGPASHLREHGIPVVHDLPGVGRNLQDHLEVSVVFRFKEPV-----TLNKSLR 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 321 VLKGCIDWFSKRQGCLTTNFAESHAFIKLFDDSPAPDVQLEFV-LGLVDDHSR-KLHTGHGYSIHSSIMRPKSRGAVKLA 398
Cdd:COG2303   315 KARIGLQYLLTRSGPLTSNVAEAGGFFRSDPGLERPDLQFHFLpLGLTPRWGKkALHDGHGFTAHVEQLRPESRGRVTLD 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 399 DSDPRSAPLIDPNYLSHPDDIKVMLQGLKKTLQIMQSSAFDAIRGDMVYPLDINNDEQLIEFIRQTADTEYHPVGTCKMG 478
Cdd:COG2303   395 SADPLGAPLIRPNYLSDENDRRVLVAGVRLAREIAAQPALAPYRGEEILPGPDVQSDEELAFIRARAYTIYHPVGTCRMG 474

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1198878507 479 NDPLAVVDNELRVYAIQGLRVVDASIMPSIITGNTNAAVIAIAEKAADLIKQANP 533
Cdd:COG2303   475 TDPDSVVDPRLRVHGVENLRVVDASVMPTITSGNTNAPTIMLAEKAADMILGDYL 529
PRK02106 PRK02106
choline dehydrogenase; Validated
 1-529 0e+00

choline dehydrogenase; Validated


Pssm-ID: 235000 [Multi-domain]  Cd Length: 560  Bit Score: 601.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507   1 MNTTFDYIVVGAGSAGCVIASRLSENANVSVCLIEAGSSDNTA--FVQMPAGVAasvpYGINS----WHYNTVAQKELNN 74
Cdd:PRK02106    2 TTMEYDYIIIGAGSAGCVLANRLSEDPDVSVLLLEAGGPDYRWdfFIQMPAALA----FPLQGkrynWAYETEPEPHMNN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507  75 RCGFMPRGKVLGGSSSINAMVYIRGNKYDYDQWAAN-GNSGWDYDSLLPYFIKAENNKtFTNSELHGTQGPLHVQELNEP 153
Cdd:PRK02106   78 RRMECPRGKVLGGSSSINGMVYIRGNAMDYDNWAELpGLEGWSYADCLPYFKKAETRD-GGEDDYRGGDGPLSVTRGKPG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 154 -SPVNQCFLNACVEQGVSLNNDINATEQQGARLSQVTQHNGERCSAAKAYLTPHLKRANLTVLTNSHVNKVIINNNMAQG 232
Cdd:PRK02106  157 tNPLFQAFVEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTNGRRWSAARAYLDPALKRPNLTIVTHALTDRILFEGKRAVG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 233 VQIERNKQVVNLYANNEVILSAGAINSPQLLMLSGVGPSNHLLAHNIKVIVPLEGVGANLHDHLTV---------VPLYR 303
Cdd:PRK02106  237 VEYERGGGRETARARREVILSAGAINSPQLLQLSGIGPAEHLKELGIPVVHDLPGVGENLQDHLEVyiqyeckqpVSLYP 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 304 A--KTSKGTFGLSipgaarvlkgcidWFSKRQGCLTTNFAESHAFIKLFDDSPAPDVQLEFVLGLVDDHSRKLHTGHGYS 381
Cdd:PRK02106  317 AlkWWNKPKIGAE-------------WLFTGTGLGASNHFEAGGFIRSRAGVDWPNIQYHFLPVAIRYDGSNAVKGHGFQ 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 382 IHSSIMRPKSRGAVKLADSDPRSAPLIDPNYLSHPDDIKVMLQGLKKTLQIMQSSAFDAIRGDMVYP-LDINNDEQLIEF 460
Cdd:PRK02106  384 AHVGPMRSPSRGSVKLKSADPRAHPSILFNYMSTEQDWREFRDAIRLTREIMAQPALDPYRGREISPgADVQTDEEIDAF 463

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1198878507 461 IRQTADTEYHPVGTCKMGNDPLAVVDNELRVYAIQGLRVVDASIMPSIITGNTNAAVIAIAEKAADLIK 529
Cdd:PRK02106  464 VREHAETAYHPSCTCKMGTDPMAVVDPEGRVHGVEGLRVVDASIMPTITNGNLNAPTIMIAEKAADLIR 532
betA TIGR01810
choline dehydrogenase; Choline dehydrogenase catalyzes the conversion of exogenously supplied ...
 6-533 1.72e-156

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: 457.03  E-value: 1.72e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507   6 DYIVVGAGSAGCVIASRLSENANVSVCLIEAGSSD--NTAFVQMPAGVAASVPYGINSWHYNTVAQKELNNRCGFMPRGK 83
Cdd:TIGR01810   1 DYIIIGGGSAGSVLAGRLSEDVSNSVLVLEAGGSDypWDLLIQMPAALAYPAGNKRYNWIYETEPEPHMNNRRVGHARGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507  84 VLGGSSSINAMVYIRGNKYDYDQWAAN-GNSGWDYDSLLPYFIKAENnkTFTNSE-LHGTQGPLHVQELNEPSPVNQCFL 161
Cdd:TIGR01810  81 VLGGSSSINGMIYQRGNPMDYEKWAKPeGMESWDYADCLPYYKRLET--TFGGEKpYRGHDGPIKVRRGPADNPLFQAFI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 162 NACVEQGVSLNNDINATEQQGARLSQVTQHNGERCSAAKAYLTPHLKRANLTVLTNSHVNKVIINNNMAQGVQIERNKQV 241
Cdd:TIGR01810 159 EAGVEAGYNKTPDVNGFRQEGFGPMDSTVHNGRRVSAARAYLHPAMKRPNLEVQTRAFVTKINFEGNRATGVEFKKGGRK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 242 VNLYANNEVILSAGAINSPQLLMLSGVGPSNHLLAHNIKVIVPLEGVGANLHDHLTVvplYRAKTSKGTFGLSiPGAARV 321
Cdd:TIGR01810 239 EHTEANKEVILSAGAINSPQLLQLSGIGDAEHLRELGIEPRIHLPGVGENLQDHLEV---YVQHACKQPVSLY-PSLNWL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 322 LKGCI--DWFSKRQGCLTTNFAESHAFIKLFDDSPAPDVQLEFVLGLVDDHSRKLHTGHGYSIHSSIMRPKSRGAVKLAD 399
Cdd:TIGR01810 315 KQPFIgaQWLFGRKGAGASNHFEGGGFVRSNDDVDYPNIQYHFLPVAIRYDGTKAPKAHGFQVHVGPMYSNSRGHVKIKS 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 400 SDPRSAPLIDPNYLSHPDDIKVMLQGLKKTLQIMQSSAFDAIRGDMVYP-LDINNDEQLIEFIRQTADTEYHPVGTCKMG 478
Cdd:TIGR01810 395 KDPFEKPEIVFNYMSHEEDWREFREAIRVTREILKQKALDPYRGGEISPgPEVQTDEEIDEFVRRHGETALHPCGTCKMG 474

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1198878507 479 --NDPLAVVDNELRVYAIQGLRVVDASIMPSIITGNTNAAVIAIAEKAADLIKQANP 533
Cdd:TIGR01810 475 paSDEMSVVDPETRVHGMEGLRVVDASIMPRITNGNLNAPVIMMGEKAADIIRGKKP 531
GMC_oxred_C pfam05199
GMC oxidoreductase; This domain found associated with pfam00732.
 389-524 1.41e-49

GMC oxidoreductase; This domain found associated with pfam00732.


Pssm-ID: 398739 [Multi-domain]  Cd Length: 143  Bit Score: 167.19  E-value: 1.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 389 PKSRGAVKLADSDPRSAPLIDPNYLSHPDDIKVMLQGLKKTLQIMQSSAFDAIRGDMVYPLDI------NNDEQLIEFIR 462
Cdd:pfam05199   1 PRSRGRVTLSSSDPTGLPVIDPNYLSDPADLAALRAALRLARRILAAAGLVLGVELTPGPVPEvsdaavTSDDELLAYIR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1198878507 463 QTADTEYHPVGTCKMGNDPL-AVVDNELRVYAIQGLRVVDASIMPSIITGNTNAAVIAIAEKA 524
Cdd:pfam05199  81 AAASTSYHPMGTCRMGADPDdAVVDPDLRVHGVDNLRVVDASVFPSSPSGNPTLTIYALAERA 143
GMC_oxred_N pfam00732
GMC oxidoreductase; This family of proteins bind FAD as a cofactor.
 73-297 4.53e-49

GMC oxidoreductase; This family of proteins bind FAD as a cofactor.


Pssm-ID: 366272 [Multi-domain]  Cd Length: 218  Bit Score: 168.61  E-value: 4.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507  73 NNRCGFMPRGKVLGGSSSINAMVYIRGNKYDYDQWAAN-GNSGWDYDSLLPYFIKAEnnktftnselhgtqGPLHVQ-EL 150
Cdd:pfam00732  15 NGRRMILPAGSTVGGGSSVNWSACIRTPAAVLDEWASEfGLEGWGYDDYLPYMDKVE--------------GPLGVTtKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 151 NEPSPVNQCFLNACVEQGVSLNN-DINATEQQGARLSQVTQHNGERCSAAKAYLTPHLKRaNLTVLTNSHVNKVIINNN- 228
Cdd:pfam00732  81 IEESPLNQALLKAAEELGYPVEAvPRNSNGCHYCGFCGLGCPTGAKQSTARTWLRPALER-NLRILTGAKAEKIIILGRg 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1198878507 229 -MAQGVQIERNKQVV--NLYANNEVILSAGAINSPQLLMLSGVGPSNHllahnikvivpleGVGANLHDHLT 297
Cdd:pfam00732 160 gRAVGVEARDGGGGIkrLITAAKEVVVAAGALNTPPLLLRSGLGKNPH-------------PVGKNLQLHPV 218
PLN02785 PLN02785
Protein HOTHEAD
 2-518 6.20e-39

Protein HOTHEAD


Pssm-ID: 215420 [Multi-domain]  Cd Length: 587  Bit Score: 149.96  E-value: 6.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507   2 NTTFDYIVVGAGSAGCVIASRLSENanVSVCLIEAGSSD----NTAFVQ-MPAGVAASVPyginswhyNTVAQKELNNRC 76
Cdd:PLN02785   53 DSAYDYIVVGGGTAGCPLAATLSQN--FSVLLLERGGVPfgnaNVSFLEnFHIGLADTSP--------TSASQAFISTDG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507  77 GFMPRGKVLGGSSSINAMVYIRGNKyDYDQWAangnsGWDYDSLlpyfikaenNKTFTNSELHGTQGPlhvqelnEPSPV 156
Cdd:PLN02785  123 VINARARVLGGGTCINAGFYSRAST-RFIQKA-----GWDAKLV---------NESYPWVERQIVHWP-------KVAPW 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 157 NQCFLNACVEQGVSLNNDINATEQQGARLS-QVTQHNGERCSAAK--AYLTPHlkraNLTVLTNSHVNKVIINNN----M 229
Cdd:PLN02785  181 QAALRDSLLEVGVSPFNGFTYDHVYGTKVGgTIFDEFGRRHTAAEllAAGNPN----KLRVLLHATVQKIVFDTSgkrpR 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 230 AQGVQI--ERNKQVVNLYANN---EVILSAGAINSPQLLMLSGVGPSNHLLAHNIKVIVPLEGVGANLHD---HLTVVPL 301
Cdd:PLN02785  257 ATGVIFkdENGNQHQAFLSNNkgsEIILSAGAIGSPQMLLLSGIGPKKELKKHKIPVVLHNEHVGKGMADnpmNSIFVPS 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 302 YRA--KTSKGTFGLSIPGaarVLKGCIDWFSKRQGCLTTNFAESHAFIKLFDDSPAPDVQLEFVLGLVDDHSRKLHTG-H 378
Cdd:PLN02785  337 KAPveQSLIQTVGITKMG---VYIEASSGFGQSPDSIHCHHGIMSAEIGQLSTIPPKQRTPEAIQAYIHRKKNLPHEAfN 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 379 GYSIHSSIMRPKSRGAVKLADSDPRSAPLIDPNYLSHPDDIKVMLQGLKKTLQIMQSSAFDAIRGDMVYPLD-------- 450
Cdd:PLN02785  414 GGFILEKIAGPISTGHLSLINTNVDDNPSVTFNYFKHPQDLQRCVYGIRTIEKIVKTNHFTNFTQCDKQTMEkvlnmsvk 493

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1198878507 451 ---------INNDEQLIEFIRQTADTEYHPVGTCKMGNdplaVVDNELRVYAIQGLRVVDASIMPSIITGNTNAAVI 518
Cdd:PLN02785  494 aninlipkhTNDTKSLEQFCKDTVITIWHYHGGCHVGK----VVDQNYKVLGVSRLRVIDGSTFDESPGTNPQATVM 566
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
1-41 1.49e-04

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 44.37  E-value: 1.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1198878507   1 MNTTFDYIVVGAGSAGCVIASRLSENANVSVCLIE------AGSSDN 41
Cdd:COG0579     1 MMEMYDVVIIGAGIVGLALARELSRYEDLKVLVLEkeddvaQESSGN 47
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
3-45 5.22e-04

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 42.20  E-value: 5.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1198878507   3 TTFDYIVVGAGSAGCVIASRLSEnANVSVCLIEAG------SSDNTAFV 45
Cdd:COG0665     1 ATADVVVIGGGIAGLSTAYHLAR-RGLDVTVLERGrpgsgaSGRNAGQL 48
Lycopene_cycl pfam05834
Lycopene cyclase protein; This family consists of lycopene beta and epsilon cyclase proteins. ...
 6-39 7.89e-04

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: 42.02  E-value: 7.89e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1198878507   6 DYIVVGAGSAGCVIASRLSENA-NVSVCLIEAGSS 39
Cdd:pfam05834   1 DVVIIGAGPAGLSLAARLAAAKpGLSVVLIEPGPS 35
PRK06175 PRK06175
L-aspartate oxidase; Provisional
 147-281 9.91e-04

L-aspartate oxidase; Provisional


Pssm-ID: 180442 [Multi-domain]  Cd Length: 433  Bit Score: 41.59  E-value: 9.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507 147 VQELNEPSPVNqcfLNACVEQGVSL---NNDINATeQQGA----RLSQVTQHNGErcSAAKAYLTPHLKRANLTVLTNSH 219
Cdd:PRK06175   78 VKILANESIEN---INKLIDMGLNFdkdEKELSYT-KEGAhsvnRIVHFKDNTGK--KVEKILLKKVKKRKNITIIENCY 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1198878507 220 VNKVIINNNMAQGVQIERNKQVVNLYANNeVILSAGAI-----NSPQLLMLSGVGPSNhLLAHNIKV 281
Cdd:PRK06175  152 LVDIIENDNTCIGAICLKDNKQINIYSKV-TILATGGIgglfkNSTNQRIITGDGIAI-AIRNNIKI 216
PLN02661 PLN02661
Putative thiazole synthesis
 6-35 4.02e-03

Putative thiazole synthesis


Pssm-ID: 178267  Cd Length: 357  Bit Score: 39.43  E-value: 4.02e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1198878507   6 DYIVVGAGSAGCVIASRLSENANVSVCLIE 35
Cdd:PLN02661   94 DVVIVGAGSAGLSCAYELSKNPNVKVAIIE 123
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 6-84 6.10e-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: 38.92  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198878507   6 DYIVVGAGSAGCVIASRLSEnANVSVCLIEAG-------SSDNTAFVQmpAGVAASVPYGINSWHYNTVA-----QKELN 73
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELAR-RGLSVTLLERGddpgsgaSGRNAGLIH--PGLRYLEPSELARLALEALDlweelEEELG 77

                          90
                  ....*....|.
gi 1198878507  74 NRCGFMPRGKV 84
Cdd:pfam01266  78 IDCGFRRCGVL 88
PRK06370 PRK06370
FAD-containing oxidoreductase;
1-35 7.95e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 38.64  E-value: 7.95e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1198878507   1 MNTTFDYIVVGAGSAGCVIASRLSEnANVSVCLIE 35
Cdd:PRK06370    2 PAQRYDAIVIGAGQAGPPLAARAAG-LGMKVALIE 35
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 2-37 8.26e-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: 38.91  E-value: 8.26e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1198878507   2 NTTFDYIVVGAGSAGCVIASRLSEnANVSVCLIEAG 37
Cdd:COG1249     1 MKDYDLVVIGAGPGGYVAAIRAAQ-LGLKVALVEKG 35
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
9-63 8.54e-03

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 35.20  E-value: 8.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1198878507   9 VVGAGSAGCVIASRLSEnANVSVCLIEAGSSdntafvqmPAGVAAS-------VPYGINSWH 63
Cdd:pfam13450   1 IVGAGLAGLVAAALLAK-RGFRVLVLEKRDR--------LGGNAYSyrvpgyvFDYGAHIFH 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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