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Conserved domains on  [gi|1093586273|gb|OHX99647|]
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thiamine biosynthesis protein ApbE [Brucella abortus]

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 ...
18-306 3.99e-114

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


:

Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 332.11  E-value: 3.99e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  18 MRTRWSAIFYAAADFDIAPLRRALQQAVDEVDMQMSTWKPDSDLMRLNRAPVGVWVEVPARLMEVLRLAIEIGRATGGAF 97
Cdd:COG1477     1 MGTTVSITLYGPDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  98 DAAMGDAVKAWGFGPMEA---DQRLISEALAGPRvaaHDALELDISAMRVRK-RAAVTLDLNGIAKGYGVDRLADTLESF 173
Cdd:COG1477    81 DPTVGPLVNLWGFGPDKArvpSAAEIAAALALVG---YRKVELDEEGGTVRLaRPGMQLDLGGIAKGYAVDRAAELLRAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273 174 GIHSGLVGIDGEMRALELRPDGTPWAIAVEMPDyNRRAPHSVLALHNGAVATSGDYRHWVVAGGHRLSHTMDPHRGAPLS 253
Cdd:COG1477   158 GVTNALVNLGGDIRALGTKPDGRPWRVGIEDPR-DPGAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVE 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1093586273 254 TPPASVTVVAKTCAQADAFATALMVLGPIAGSKLAQSL-GLDVLFLLRDGETIR 306
Cdd:COG1477   237 HGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLpGLEALLIDRDGKVFA 290
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
18-306 3.99e-114

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 332.11  E-value: 3.99e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  18 MRTRWSAIFYAAADFDIAPLRRALQQAVDEVDMQMSTWKPDSDLMRLNRAPVGVWVEVPARLMEVLRLAIEIGRATGGAF 97
Cdd:COG1477     1 MGTTVSITLYGPDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  98 DAAMGDAVKAWGFGPMEA---DQRLISEALAGPRvaaHDALELDISAMRVRK-RAAVTLDLNGIAKGYGVDRLADTLESF 173
Cdd:COG1477    81 DPTVGPLVNLWGFGPDKArvpSAAEIAAALALVG---YRKVELDEEGGTVRLaRPGMQLDLGGIAKGYAVDRAAELLRAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273 174 GIHSGLVGIDGEMRALELRPDGTPWAIAVEMPDyNRRAPHSVLALHNGAVATSGDYRHWVVAGGHRLSHTMDPHRGAPLS 253
Cdd:COG1477   158 GVTNALVNLGGDIRALGTKPDGRPWRVGIEDPR-DPGAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVE 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1093586273 254 TPPASVTVVAKTCAQADAFATALMVLGPIAGSKLAQSL-GLDVLFLLRDGETIR 306
Cdd:COG1477   237 HGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLpGLEALLIDRDGKVFA 290
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
20-292 1.69e-80

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: 243.89  E-value: 1.69e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  20 TRWSAIFYAAADFDIAPLRRALQQAVDEVDMQMSTWKPDSDLMRLNRAPVGvWVEVPARLMEVLRLAIEIGRATGGAFDA 99
Cdd:pfam02424   2 TTVSITVYGPDEAAAEALEAAIDAELDRLEALLSTYRPDSELSRLNRAGAG-PVKVSPELFELLERALEISELSGGAFDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273 100 AMGdavkawgfgpmeadqrlisealagprvaahdaleldisamrvrkraAVTLDLNGIAKGYGVDRLADTLESFGIHSGL 179
Cdd:pfam02424  81 TVG----------------------------------------------PLVLDLGGIAKGYAVDRAAELLKAKGVTSAL 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273 180 VGIDGEMRALELRPDGTPWAIAVEMPDynRRAPHSVLALHNGAVATSGDYRHWVVaGGHRLSHTMDPHRGAPLSTPPASV 259
Cdd:pfam02424 115 VNLGGDIRALGTKPDGSPWRVGIQDPR--DPDSLAVLELSDKAVATSGDYERYFE-DGKRYHHIIDPRTGYPVANGLASV 191
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1093586273 260 TVVAkTCAQADAFATALMVLGPIAGSKLAQSLG 292
Cdd:pfam02424 192 TVIA-DAMLADALATALFVLGPEKGLALLEKLP 223
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
13-304 5.07e-52

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 174.94  E-value: 5.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  13 LNGPTMRTRWSAIFYAAADFDIAPLRRALQQAVDEVDMQMSTWKPDSDLMRLNRAPVGVWVEVPARLMEVLRLAIEIGRA 92
Cdd:PRK10461   37 LEGKTMGTFWRVSIPGIDAKRSAELQEKIQTQLDADDQLLSTYKKDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  93 TGGAFDAAMGDAVKAWGFGPMEA-----DQRLISEALA--GPR------VAAHDALELDISAMRVrkraavtlDLNGIAK 159
Cdd:PRK10461  117 TDGAMDITVGPLVNLWGFGPEKQpvqipSQEQIDAAKAktGLQhltvinQSHQQYLQKDLPDLYV--------DLSTVGE 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273 160 GYGVDRLADTLESFGIHSGLVGIDGEMRALELRPDGTPWAIAVEMPDYNRRAPHSVLALHNGAVATSGDYRHWVVAGGHR 239
Cdd:PRK10461  189 GYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPTDKENAVQAVVDINGHGISTSGSYRNYYELDGKR 268
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093586273 240 LSHTMDPHRGAPLSTPPASVTVVAKTCAQADAFATALMVLGPIAGSKLAQSLGLDVLFLLRDGET 304
Cdd:PRK10461  269 LSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRREGLAVYMITKEGDG 333
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
18-306 3.99e-114

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 332.11  E-value: 3.99e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  18 MRTRWSAIFYAAADFDIAPLRRALQQAVDEVDMQMSTWKPDSDLMRLNRAPVGVWVEVPARLMEVLRLAIEIGRATGGAF 97
Cdd:COG1477     1 MGTTVSITLYGPDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  98 DAAMGDAVKAWGFGPMEA---DQRLISEALAGPRvaaHDALELDISAMRVRK-RAAVTLDLNGIAKGYGVDRLADTLESF 173
Cdd:COG1477    81 DPTVGPLVNLWGFGPDKArvpSAAEIAAALALVG---YRKVELDEEGGTVRLaRPGMQLDLGGIAKGYAVDRAAELLRAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273 174 GIHSGLVGIDGEMRALELRPDGTPWAIAVEMPDyNRRAPHSVLALHNGAVATSGDYRHWVVAGGHRLSHTMDPHRGAPLS 253
Cdd:COG1477   158 GVTNALVNLGGDIRALGTKPDGRPWRVGIEDPR-DPGAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVE 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1093586273 254 TPPASVTVVAKTCAQADAFATALMVLGPIAGSKLAQSL-GLDVLFLLRDGETIR 306
Cdd:COG1477   237 HGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLpGLEALLIDRDGKVFA 290
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
20-292 1.69e-80

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: 243.89  E-value: 1.69e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  20 TRWSAIFYAAADFDIAPLRRALQQAVDEVDMQMSTWKPDSDLMRLNRAPVGvWVEVPARLMEVLRLAIEIGRATGGAFDA 99
Cdd:pfam02424   2 TTVSITVYGPDEAAAEALEAAIDAELDRLEALLSTYRPDSELSRLNRAGAG-PVKVSPELFELLERALEISELSGGAFDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273 100 AMGdavkawgfgpmeadqrlisealagprvaahdaleldisamrvrkraAVTLDLNGIAKGYGVDRLADTLESFGIHSGL 179
Cdd:pfam02424  81 TVG----------------------------------------------PLVLDLGGIAKGYAVDRAAELLKAKGVTSAL 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273 180 VGIDGEMRALELRPDGTPWAIAVEMPDynRRAPHSVLALHNGAVATSGDYRHWVVaGGHRLSHTMDPHRGAPLSTPPASV 259
Cdd:pfam02424 115 VNLGGDIRALGTKPDGSPWRVGIQDPR--DPDSLAVLELSDKAVATSGDYERYFE-DGKRYHHIIDPRTGYPVANGLASV 191
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1093586273 260 TVVAkTCAQADAFATALMVLGPIAGSKLAQSLG 292
Cdd:pfam02424 192 TVIA-DAMLADALATALFVLGPEKGLALLEKLP 223
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
13-304 5.07e-52

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 174.94  E-value: 5.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  13 LNGPTMRTRWSAIFYAAADFDIAPLRRALQQAVDEVDMQMSTWKPDSDLMRLNRAPVGVWVEVPARLMEVLRLAIEIGRA 92
Cdd:PRK10461   37 LEGKTMGTFWRVSIPGIDAKRSAELQEKIQTQLDADDQLLSTYKKDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  93 TGGAFDAAMGDAVKAWGFGPMEA-----DQRLISEALA--GPR------VAAHDALELDISAMRVrkraavtlDLNGIAK 159
Cdd:PRK10461  117 TDGAMDITVGPLVNLWGFGPEKQpvqipSQEQIDAAKAktGLQhltvinQSHQQYLQKDLPDLYV--------DLSTVGE 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273 160 GYGVDRLADTLESFGIHSGLVGIDGEMRALELRPDGTPWAIAVEMPDYNRRAPHSVLALHNGAVATSGDYRHWVVAGGHR 239
Cdd:PRK10461  189 GYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPTDKENAVQAVVDINGHGISTSGSYRNYYELDGKR 268
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093586273 240 LSHTMDPHRGAPLSTPPASVTVVAKTCAQADAFATALMVLGPIAGSKLAQSLGLDVLFLLRDGET 304
Cdd:PRK10461  269 LSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRREGLAVYMITKEGDG 333
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
41-278 4.84e-25

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 106.02  E-value: 4.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273   41 LQQAVDEVDMQMSTWKPDSDLMRLNRAPVGVWVEVPARLMEVLRLAIEIGRATGGAFDAAMGDAVK-----AWGFGPMEA 115
Cdd:PTZ00306    92 LRSAFQMVDTHLNSFNPNSEVSRVNRMPVGEKHQMSAHLKRVMACCQRVYNSSGGCFDPAAGPLVHelreaARRQKSVEA 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  116 DQrlISEALAGpRVAAHDALELDISA-MRVRKRAAVTLDLNGIAKGYGVDRLADTLESFGIHSGLVGIDGEMRALELRPD 194
Cdd:PTZ00306   172 EF--VIEELAG-RFTLTNSFAIDLEEgTIARKHEDAMLDLGGVNKGYTVDYVVDRLNAAGFDDVLFEWGGDCRASGVNVQ 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093586273  195 GTPWAIAVEMP---DYNRRAPHS-------------VLALHNGAVATSGDYRHWVVAGGHR-LSHTMD-PHRG--APLST 254
Cdd:PTZ00306   249 RQPWAVGIVRPpsvDEVRAAAKSgksappdhksllrVMSLNNEALCTSGDYENVLEGPASKvYSSTFDwKRRSllEPTES 328
                          250       260
                   ....*....|....*....|....
gi 1093586273  255 PPASVTVVAKTCAQADAFATALMV 278
Cdd:PTZ00306   329 ELAQVSVKCYSCMYADALATASLV 352
COG2122 COG2122
Uncharacterized conserved protein, UPF0280 family, ApbE superfamily [Function unknown];
258-276 7.13e-03

Uncharacterized conserved protein, UPF0280 family, ApbE superfamily [Function unknown];


Pssm-ID: 441725  Cd Length: 240  Bit Score: 37.49  E-value: 7.13e-03
                          10
                  ....*....|....*....
gi 1093586273 258 SVTVVAKTCAQADAFATAL 276
Cdd:COG2122   171 AVTVLARDAALADAAATAI 189
 
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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