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Conserved domains on  [gi|502841625|ref|WP_013076601|]
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FAD:protein FMN transferase [Kyrpidia tusciae]

Protein Classification

FAD:protein FMN transferase( domain architecture ID 10003878)

FAD:protein FMN-transferase catalyzes the attachment of an FMN moiety to a threonine residue of a protein via a phosphoester bond in bacterial flavoproteins

CATH:  3.10.520.20
EC:  2.7.1.180
PubMed:  23558683
SCOP:  4003899

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
11-324 2.93e-66

FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 210.39  E-value: 2.93e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625  11 MASPIRIRLDFPGNHRQEDAEAAteiwdmAKDEFASVVKALSRFDPNSELSRLNQSPG-QWVATSPLLREALQKAREAYE 89
Cdd:COG1477    1 MGTTVSITLYGPDEAQAEAALAA------AFAELDRLEALLSTYRPDSELSRLNRAAGgEPVKVSPELAELLERALEISE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625  90 YTGGVFDPRIlrslealgytgAPVVplstggrgdgtdsmrgAAASFDSDGDKFPEP-----------WADpapwVEFD-- 156
Cdd:COG1477   75 LSDGAFDPTV-----------GPLV----------------NLWGFGPDKARVPSAaeiaaalalvgYRK----VELDee 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625 157 GDRVRIEAP---LDLGGLGKSLAVDRVRKSILNHPAagrmKGFLVNAGGDLYAWGTREDGEHWRVGIEDPTAPATILAVL 233
Cdd:COG1477  124 GGTVRLARPgmqLDLGGIAKGYAVDRAAELLRAAGV----TNALVNLGGDIRALGTKPDGRPWRVGIEDPRDPGAVLAVL 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625 234 GLPlSTAVCTSSIARRRWIHHGRPVHHLIDPATGQPAESPYLSVTCAYPDPITAEIITKVLFIRPAQSlriwpWPEYI-- 311
Cdd:COG1477  200 ELS-DGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEHGLASVTVIAPDAMLADALATALFVLGPEK-----GLALAer 273
                        330
                 ....*....|....*....
gi 502841625 312 ------WWVTTDVRLHATP 324
Cdd:COG1477  274 lpgleaLLIDRDGKVFASP 292
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
11-324 2.93e-66

FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 210.39  E-value: 2.93e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625  11 MASPIRIRLDFPGNHRQEDAEAAteiwdmAKDEFASVVKALSRFDPNSELSRLNQSPG-QWVATSPLLREALQKAREAYE 89
Cdd:COG1477    1 MGTTVSITLYGPDEAQAEAALAA------AFAELDRLEALLSTYRPDSELSRLNRAAGgEPVKVSPELAELLERALEISE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625  90 YTGGVFDPRIlrslealgytgAPVVplstggrgdgtdsmrgAAASFDSDGDKFPEP-----------WADpapwVEFD-- 156
Cdd:COG1477   75 LSDGAFDPTV-----------GPLV----------------NLWGFGPDKARVPSAaeiaaalalvgYRK----VELDee 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625 157 GDRVRIEAP---LDLGGLGKSLAVDRVRKSILNHPAagrmKGFLVNAGGDLYAWGTREDGEHWRVGIEDPTAPATILAVL 233
Cdd:COG1477  124 GGTVRLARPgmqLDLGGIAKGYAVDRAAELLRAAGV----TNALVNLGGDIRALGTKPDGRPWRVGIEDPRDPGAVLAVL 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625 234 GLPlSTAVCTSSIARRRWIHHGRPVHHLIDPATGQPAESPYLSVTCAYPDPITAEIITKVLFIRPAQSlriwpWPEYI-- 311
Cdd:COG1477  200 ELS-DGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEHGLASVTVIAPDAMLADALATALFVLGPEK-----GLALAer 273
                        330
                 ....*....|....*....
gi 502841625 312 ------WWVTTDVRLHATP 324
Cdd:COG1477  274 lpgleaLLIDRDGKVFASP 292
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
13-305 3.59e-51

ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella typhimurium. ApbE is involved in thiamine synthesis. It acts as an FAD:protein FMN-transferase, catalysing the attachment of an FMN residue to a threonine residue of a protein via a phosphoester bond in such bacterial flavoproteins.


Pssm-ID: 460554 [Multi-domain]  Cd Length: 227  Bit Score: 169.17  E-value: 3.59e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625   13 SPIRIRLDFPGNHRQEDAEAAteiwdmAKDEFASVVKALSRFDPNSELSRLNQSPGQWVATSPLLREALQKAREAYEYTG 92
Cdd:pfam02424   2 TTVSITVYGPDEAAAEALEAA------IDAELDRLEALLSTYRPDSELSRLNRAGAGPVKVSPELFELLERALEISELSG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625   93 GVFDPRIlrslealgytgAPVVplstggrgdgtdsmrgaaasfdsdgdkfpepwadpapwvefdgdrvrieapLDLGGLG 172
Cdd:pfam02424  76 GAFDITV-----------GPLV---------------------------------------------------LDLGGIA 93
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625  173 KSLAVDRVRKsILNhpAAGrMKGFLVNAGGDLYAWGTREDGEHWRVGIEDPTAPATIlAVLGLPlSTAVCTSSIARRRWI 252
Cdd:pfam02424  94 KGYAVDRAAE-LLK--AKG-VTSALVNLGGDIRALGTKPDGSPWRVGIQDPRDPDSL-AVLELS-DKAVATSGDYERYFE 167
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 502841625  253 hHGRPVHHLIDPATGQPAESPYLSVTCaYPDPITAEIITKVLFI-RPAQSLRIW 305
Cdd:pfam02424 168 -DGKRYHHIIDPRTGYPVANGLASVTV-IADAMLADALATALFVlGPEKGLALL 219
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
14-232 1.27e-12

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 68.65  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625   14 PIRIRLDFPGNHRQEDAEAATEiwDMAKDEFASVVKALSRFDPNSELSRLNQSP-GQWVATSPLLREALQKAREAYEYTG 92
Cdd:PTZ00306   68 PYTLKVVVAGPVARQDADAVAK--EVLRSAFQMVDTHLNSFNPNSEVSRVNRMPvGEKHQMSAHLKRVMACCQRVYNSSG 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625   93 GVFDPrilrslealgyTGAPVVplstggrgdgtDSMRGAAASFDSDGDKFP-----EPWADPApwvEFDGD-------RV 160
Cdd:PTZ00306  146 GCFDP-----------AAGPLV-----------HELREAARRQKSVEAEFVieelaGRFTLTN---SFAIDleegtiaRK 200
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502841625  161 RIEAPLDLGGLGKSLAVDRVrksiLNHPAAGRMKGFLVNAGGDLYAWGTREDGEHWRVGIEDPTAPATILAV 232
Cdd:PTZ00306  201 HEDAMLDLGGVNKGYTVDYV----VDRLNAAGFDDVLFEWGGDCRASGVNVQRQPWAVGIVRPPSVDEVRAA 268
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
11-324 2.93e-66

FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 210.39  E-value: 2.93e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625  11 MASPIRIRLDFPGNHRQEDAEAAteiwdmAKDEFASVVKALSRFDPNSELSRLNQSPG-QWVATSPLLREALQKAREAYE 89
Cdd:COG1477    1 MGTTVSITLYGPDEAQAEAALAA------AFAELDRLEALLSTYRPDSELSRLNRAAGgEPVKVSPELAELLERALEISE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625  90 YTGGVFDPRIlrslealgytgAPVVplstggrgdgtdsmrgAAASFDSDGDKFPEP-----------WADpapwVEFD-- 156
Cdd:COG1477   75 LSDGAFDPTV-----------GPLV----------------NLWGFGPDKARVPSAaeiaaalalvgYRK----VELDee 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625 157 GDRVRIEAP---LDLGGLGKSLAVDRVRKSILNHPAagrmKGFLVNAGGDLYAWGTREDGEHWRVGIEDPTAPATILAVL 233
Cdd:COG1477  124 GGTVRLARPgmqLDLGGIAKGYAVDRAAELLRAAGV----TNALVNLGGDIRALGTKPDGRPWRVGIEDPRDPGAVLAVL 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625 234 GLPlSTAVCTSSIARRRWIHHGRPVHHLIDPATGQPAESPYLSVTCAYPDPITAEIITKVLFIRPAQSlriwpWPEYI-- 311
Cdd:COG1477  200 ELS-DGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEHGLASVTVIAPDAMLADALATALFVLGPEK-----GLALAer 273
                        330
                 ....*....|....*....
gi 502841625 312 ------WWVTTDVRLHATP 324
Cdd:COG1477  274 lpgleaLLIDRDGKVFASP 292
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
13-305 3.59e-51

ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella typhimurium. ApbE is involved in thiamine synthesis. It acts as an FAD:protein FMN-transferase, catalysing the attachment of an FMN residue to a threonine residue of a protein via a phosphoester bond in such bacterial flavoproteins.


Pssm-ID: 460554 [Multi-domain]  Cd Length: 227  Bit Score: 169.17  E-value: 3.59e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625   13 SPIRIRLDFPGNHRQEDAEAAteiwdmAKDEFASVVKALSRFDPNSELSRLNQSPGQWVATSPLLREALQKAREAYEYTG 92
Cdd:pfam02424   2 TTVSITVYGPDEAAAEALEAA------IDAELDRLEALLSTYRPDSELSRLNRAGAGPVKVSPELFELLERALEISELSG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625   93 GVFDPRIlrslealgytgAPVVplstggrgdgtdsmrgaaasfdsdgdkfpepwadpapwvefdgdrvrieapLDLGGLG 172
Cdd:pfam02424  76 GAFDITV-----------GPLV---------------------------------------------------LDLGGIA 93
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625  173 KSLAVDRVRKsILNhpAAGrMKGFLVNAGGDLYAWGTREDGEHWRVGIEDPTAPATIlAVLGLPlSTAVCTSSIARRRWI 252
Cdd:pfam02424  94 KGYAVDRAAE-LLK--AKG-VTSALVNLGGDIRALGTKPDGSPWRVGIQDPRDPDSL-AVLELS-DKAVATSGDYERYFE 167
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 502841625  253 hHGRPVHHLIDPATGQPAESPYLSVTCaYPDPITAEIITKVLFI-RPAQSLRIW 305
Cdd:pfam02424 168 -DGKRYHHIIDPRTGYPVANGLASVTV-IADAMLADALATALFVlGPEKGLALL 219
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
14-232 1.27e-12

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 68.65  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625   14 PIRIRLDFPGNHRQEDAEAATEiwDMAKDEFASVVKALSRFDPNSELSRLNQSP-GQWVATSPLLREALQKAREAYEYTG 92
Cdd:PTZ00306   68 PYTLKVVVAGPVARQDADAVAK--EVLRSAFQMVDTHLNSFNPNSEVSRVNRMPvGEKHQMSAHLKRVMACCQRVYNSSG 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625   93 GVFDPrilrslealgyTGAPVVplstggrgdgtDSMRGAAASFDSDGDKFP-----EPWADPApwvEFDGD-------RV 160
Cdd:PTZ00306  146 GCFDP-----------AAGPLV-----------HELREAARRQKSVEAEFVieelaGRFTLTN---SFAIDleegtiaRK 200
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502841625  161 RIEAPLDLGGLGKSLAVDRVrksiLNHPAAGRMKGFLVNAGGDLYAWGTREDGEHWRVGIEDPTAPATILAV 232
Cdd:PTZ00306  201 HEDAMLDLGGVNKGYTVDYV----VDRLNAAGFDDVLFEWGGDCRASGVNVQRQPWAVGIVRPPSVDEVRAA 268
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
167-288 1.61e-07

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 52.06  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502841625 167 DLGGLGKSLAVDRV-----RKSILNhpaagrmkgFLVNAGGDLYAWGTREDGEHWRVGIEDPT----APATILAVLGLPL 237
Cdd:PRK10461 182 DLSTVGEGYAADHLarlmeQEGISR---------YLVSVGGALSSRGMNGEGQPWRVAIQKPTdkenAVQAVVDINGHGI 252
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 502841625 238 STavctSSIARRRWIHHGRPVHHLIDPATGQPAESPYLSVTCAYPDPITAE 288
Cdd:PRK10461 253 ST----SGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEAD 299
 
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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