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Conserved domains on  [gi|1477047717|gb|RIH54618|]
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FAD:protein FMN transferase ApbE [Shigella boydii]

Protein Classification

FAD:protein FMN transferase( domain architecture ID 10013530)

FAD:protein FMN transferase catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
1-350 0e+00

thiamine biosynthesis lipoprotein ApbE; Provisional


:

Pssm-ID: 182478  Cd Length: 350  Bit Score: 756.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717   1 MEISFTRVALLAAALFFVGCDQKPQPAKTHATEVTVLEGKTMGTFWRASIPGIDAKRSAELKEKIQTQLDADDQLLSTYK 80
Cdd:PRK10461    1 MEISFTRVALLAAALLLVGCDQAPQPAKTHATEATVLEGKTMGTFWRVSIPGIDAKRSAELQEKIQTQLDADDQLLSTYK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717  81 KDSALMRFNDSQSLSPWPVSEAMAEIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEQQPVQIPSQEQIDEMKAKTGLQH 160
Cdd:PRK10461   81 KDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEKQPVQIPSQEQIDAAKAKTGLQH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 161 LTVINQSHQQYLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALNSRGMNGEGLPWRVAIQKPTDKENA 240
Cdd:PRK10461  161 LTVINQSHQQYLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPTDKENA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 241 VQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADAWDTGLMVLGPEKAKEVVRRE 320
Cdd:PRK10461  241 VQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRRE 320
                         330       340       350
                  ....*....|....*....|....*....|
gi 1477047717 321 GLAVYMITKEGDSFKTWMSPQFKSFLVSEK 350
Cdd:PRK10461  321 GLAVYMITKEGDGFKTWMSPQFKSFLVSEK 350
 
Name Accession Description Interval E-value
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
1-350 0e+00

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 756.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717   1 MEISFTRVALLAAALFFVGCDQKPQPAKTHATEVTVLEGKTMGTFWRASIPGIDAKRSAELKEKIQTQLDADDQLLSTYK 80
Cdd:PRK10461    1 MEISFTRVALLAAALLLVGCDQAPQPAKTHATEATVLEGKTMGTFWRVSIPGIDAKRSAELQEKIQTQLDADDQLLSTYK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717  81 KDSALMRFNDSQSLSPWPVSEAMAEIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEQQPVQIPSQEQIDEMKAKTGLQH 160
Cdd:PRK10461   81 KDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEKQPVQIPSQEQIDAAKAKTGLQH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 161 LTVINQSHQQYLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALNSRGMNGEGLPWRVAIQKPTDKENA 240
Cdd:PRK10461  161 LTVINQSHQQYLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPTDKENA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 241 VQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADAWDTGLMVLGPEKAKEVVRRE 320
Cdd:PRK10461  241 VQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRRE 320
                         330       340       350
                  ....*....|....*....|....*....|
gi 1477047717 321 GLAVYMITKEGDSFKTWMSPQFKSFLVSEK 350
Cdd:PRK10461  321 GLAVYMITKEGDGFKTWMSPQFKSFLVSEK 350
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
42-342 3.84e-128

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 368.70  E-value: 3.84e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717  42 MGTFWRASIPGIDAKRSAELKEKIQTQLDADDQLLSTYKKDSALMRFNDSQSLSPWPVSEAMAEIVTTSLRIGAKTDGAM 121
Cdd:COG1477     1 MGTTVSITLYGPDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 122 DITVGPLVNLWGFGPEQQpvQIPSQEQIDEMKAKTGLQHLTVinQSHQQYLQKDLPDLYVDLSTVGEGYAADHLARLMEQ 201
Cdd:COG1477    81 DPTVGPLVNLWGFGPDKA--RVPSAAEIAAALALVGYRKVEL--DEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 202 EGISRYLVSVGGALNSRGMNGEGLPWRVAIQKPTDkENAVQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPI 281
Cdd:COG1477   157 AGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPRD-PGAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPV 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1477047717 282 EHNLVSVTVIAPTALEADAWDTGLMVLGPEKAKEVVRRE-GLAVYMITKEGdsfKTWMSPQF 342
Cdd:COG1477   236 EHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLpGLEALLIDRDG---KVFASPGF 294
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
43-321 6.23e-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: 243.51  E-value: 6.23e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717  43 GTFWRASIPGIDAKRSAELKEKIQTQLDADDQLLSTYKKDSALMRFNDSQSlSPWPVSEAMAEIVTTSLRIGAKTDGAMD 122
Cdd:pfam02424   1 GTTVSITVYGPDEAAAEALEAAIDAELDRLEALLSTYRPDSELSRLNRAGA-GPVKVSPELFELLERALEISELSGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 123 ITVGPLVnlwgfgpeqqpvqipsqeqidemkaktglqhltvinqshqqylqkdlpdlyVDLSTVGEGYAADHLARLMEQE 202
Cdd:pfam02424  80 ITVGPLV---------------------------------------------------LDLGGIAKGYAVDRAAELLKAK 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 203 GISRYLVSVGGALNSRGMNGEGLPWRVAIQKPTDKEnaVQAVVDINGHGISTSGSYRNYYElDGKRLSHVIDPQTGRPIE 282
Cdd:pfam02424 109 GVTSALVNLGGDIRALGTKPDGSPWRVGIQDPRDPD--SLAVLELSDKAVATSGDYERYFE-DGKRYHHIIDPRTGYPVA 185
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1477047717 283 HNLVSVTVIAPtALEADAWDTGLMVLGPEKAKEVVRREG 321
Cdd:pfam02424 186 NGLASVTVIAD-AMLADALATALFVLGPEKGLALLEKLP 223
 
Name Accession Description Interval E-value
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
1-350 0e+00

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 756.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717   1 MEISFTRVALLAAALFFVGCDQKPQPAKTHATEVTVLEGKTMGTFWRASIPGIDAKRSAELKEKIQTQLDADDQLLSTYK 80
Cdd:PRK10461    1 MEISFTRVALLAAALLLVGCDQAPQPAKTHATEATVLEGKTMGTFWRVSIPGIDAKRSAELQEKIQTQLDADDQLLSTYK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717  81 KDSALMRFNDSQSLSPWPVSEAMAEIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEQQPVQIPSQEQIDEMKAKTGLQH 160
Cdd:PRK10461   81 KDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEKQPVQIPSQEQIDAAKAKTGLQH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 161 LTVINQSHQQYLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALNSRGMNGEGLPWRVAIQKPTDKENA 240
Cdd:PRK10461  161 LTVINQSHQQYLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPTDKENA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 241 VQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADAWDTGLMVLGPEKAKEVVRRE 320
Cdd:PRK10461  241 VQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRRE 320
                         330       340       350
                  ....*....|....*....|....*....|
gi 1477047717 321 GLAVYMITKEGDSFKTWMSPQFKSFLVSEK 350
Cdd:PRK10461  321 GLAVYMITKEGDGFKTWMSPQFKSFLVSEK 350
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
42-342 3.84e-128

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 368.70  E-value: 3.84e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717  42 MGTFWRASIPGIDAKRSAELKEKIQTQLDADDQLLSTYKKDSALMRFNDSQSLSPWPVSEAMAEIVTTSLRIGAKTDGAM 121
Cdd:COG1477     1 MGTTVSITLYGPDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 122 DITVGPLVNLWGFGPEQQpvQIPSQEQIDEMKAKTGLQHLTVinQSHQQYLQKDLPDLYVDLSTVGEGYAADHLARLMEQ 201
Cdd:COG1477    81 DPTVGPLVNLWGFGPDKA--RVPSAAEIAAALALVGYRKVEL--DEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 202 EGISRYLVSVGGALNSRGMNGEGLPWRVAIQKPTDkENAVQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPI 281
Cdd:COG1477   157 AGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPRD-PGAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPV 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1477047717 282 EHNLVSVTVIAPTALEADAWDTGLMVLGPEKAKEVVRRE-GLAVYMITKEGdsfKTWMSPQF 342
Cdd:COG1477   236 EHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLpGLEALLIDRDG---KVFASPGF 294
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
43-321 6.23e-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: 243.51  E-value: 6.23e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717  43 GTFWRASIPGIDAKRSAELKEKIQTQLDADDQLLSTYKKDSALMRFNDSQSlSPWPVSEAMAEIVTTSLRIGAKTDGAMD 122
Cdd:pfam02424   1 GTTVSITVYGPDEAAAEALEAAIDAELDRLEALLSTYRPDSELSRLNRAGA-GPVKVSPELFELLERALEISELSGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 123 ITVGPLVnlwgfgpeqqpvqipsqeqidemkaktglqhltvinqshqqylqkdlpdlyVDLSTVGEGYAADHLARLMEQE 202
Cdd:pfam02424  80 ITVGPLV---------------------------------------------------LDLGGIAKGYAVDRAAELLKAK 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717 203 GISRYLVSVGGALNSRGMNGEGLPWRVAIQKPTDKEnaVQAVVDINGHGISTSGSYRNYYElDGKRLSHVIDPQTGRPIE 282
Cdd:pfam02424 109 GVTSALVNLGGDIRALGTKPDGSPWRVGIQDPRDPD--SLAVLELSDKAVATSGDYERYFE-DGKRYHHIIDPRTGYPVA 185
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1477047717 283 HNLVSVTVIAPtALEADAWDTGLMVLGPEKAKEVVRREG 321
Cdd:pfam02424 186 NGLASVTVIAD-AMLADALATALFVLGPEKGLALLEKLP 223
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
59-307 5.08e-11

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 64.03  E-value: 5.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717   59 AELKEKIQTQLDADDQLLSTYKKDSALMRFNDSQSLSPWPVSEAMAEIVTTSLRIGAKTDGAMDITVGPLVN-LWGFGPE 137
Cdd:PTZ00306    86 AVAKEVLRSAFQMVDTHLNSFNPNSEVSRVNRMPVGEKHQMSAHLKRVMACCQRVYNSSGGCFDPAAGPLVHeLREAARR 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717  138 QQPVqiPSQEQIDEMKAKTGLQHLTVINQSHQQYLQKDlPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALNS 217
Cdd:PTZ00306   166 QKSV--EAEFVIEELAGRFTLTNSFAIDLEEGTIARKH-EDAMLDLGGVNKGYTVDYVVDRLNAAGFDDVLFEWGGDCRA 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477047717  218 RGMNGEGLPWRVAIQKPTDKENAVQA----------------VVDINGHGISTSGSYRNY-YELDGKRLSHVIDPQTG-- 278
Cdd:PTZ00306   243 SGVNVQRQPWAVGIVRPPSVDEVRAAaksgksappdhksllrVMSLNNEALCTSGDYENVlEGPASKVYSSTFDWKRRsl 322
                          250       260       270
                   ....*....|....*....|....*....|
gi 1477047717  279 -RPIEHNLVSVTVIAPTALEADAWDTGLMV 307
Cdd:PTZ00306   323 lEPTESELAQVSVKCYSCMYADALATASLV 352
 
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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