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Conserved domains on  [gi|507083037|ref|WP_016153786|]
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MULTISPECIES: FAD:protein FMN transferase ApbE [Citrobacter]

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

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List of domain hits

Name Accession Description Interval E-value
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
1-349 0e+00

thiamine biosynthesis lipoprotein ApbE; Provisional


:

Pssm-ID: 182478  Cd Length: 350  Bit Score: 741.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037   1 MEVNFYRAALLAVTIFFVGCDEAPKPAQTTQP-ATVLEGKTMGTFWRVSAVGVDAKRAGELQAKIQAQLDADDQLLSTYK 79
Cdd:PRK10461   1 MEISFTRVALLAAALLLVGCDQAPQPAKTHATeATVLEGKTMGTFWRVSIPGIDAKRSAELQEKIQTQLDADDQLLSTYK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037  80 NDSALMRFNLSKSLSPWPVNDAMADIVTSALRIGAKTGGAMDITVGPLVNLWGFGPDQQPVHIPTQAQIDAAKAQTGLSH 159
Cdd:PRK10461  81 KDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEKQPVQIPSQEQIDAAKAKTGLQH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037 160 LKVVNEAHRNYLQKDLPELYVDLSTVGEGYAADHLARLMEQEGIARYLVSVGGALNSRGMNADGLSWRVAIQKPTDRENA 239
Cdd:PRK10461 161 LTVINQSHQQYLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPTDKENA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037 240 VQAIVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRRE 319
Cdd:PRK10461 241 VQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRRE 320
                        330       340       350
                 ....*....|....*....|....*....|
gi 507083037 320 GLAVYMIIKEGEGFKTWMSPQFKSFLLSEK 349
Cdd:PRK10461 321 GLAVYMITKEGDGFKTWMSPQFKSFLVSEK 350
 
Name Accession Description Interval E-value
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
1-349 0e+00

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 741.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037   1 MEVNFYRAALLAVTIFFVGCDEAPKPAQTTQP-ATVLEGKTMGTFWRVSAVGVDAKRAGELQAKIQAQLDADDQLLSTYK 79
Cdd:PRK10461   1 MEISFTRVALLAAALLLVGCDQAPQPAKTHATeATVLEGKTMGTFWRVSIPGIDAKRSAELQEKIQTQLDADDQLLSTYK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037  80 NDSALMRFNLSKSLSPWPVNDAMADIVTSALRIGAKTGGAMDITVGPLVNLWGFGPDQQPVHIPTQAQIDAAKAQTGLSH 159
Cdd:PRK10461  81 KDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEKQPVQIPSQEQIDAAKAKTGLQH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037 160 LKVVNEAHRNYLQKDLPELYVDLSTVGEGYAADHLARLMEQEGIARYLVSVGGALNSRGMNADGLSWRVAIQKPTDRENA 239
Cdd:PRK10461 161 LTVINQSHQQYLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPTDKENA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037 240 VQAIVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRRE 319
Cdd:PRK10461 241 VQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRRE 320
                        330       340       350
                 ....*....|....*....|....*....|
gi 507083037 320 GLAVYMIIKEGEGFKTWMSPQFKSFLLSEK 349
Cdd:PRK10461 321 GLAVYMITKEGDGFKTWMSPQFKSFLVSEK 350
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
41-341 2.71e-126

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 364.08  E-value: 2.71e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037  41 MGTFWRVSAVGVDAKRAGELQAKIQAQLDADDQLLSTYKNDSALMRFNLSKSLSPWPVNDAMADIVTSALRIGAKTGGAM 120
Cdd:COG1477    1 MGTTVSITLYGPDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037 121 DITVGPLVNLWGFGPDQQpvHIPTQAQIDAAKAQTGLSHLKVvnEAHRNYLQKDLPELYVDLSTVGEGYAADHLARLMEQ 200
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKA--RVPSAAEIAAALALVGYRKVEL--DEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037 201 EGIARYLVSVGGALNSRGMNADGLSWRVAIQKPTDReNAVQAIVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPI 280
Cdd:COG1477  157 AGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPRDP-GAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPV 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507083037 281 EHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRRE-GLAVYMIIKEGEGFktwMSPQF 341
Cdd:COG1477  236 EHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLpGLEALLIDRDGKVF---ASPGF 294
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
42-320 8.25e-78

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: 238.12  E-value: 8.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037   42 GTFWRVSAVGVDAKRAGELQAKIQAQLDADDQLLSTYKNDSALMRFNLSKSlSPWPVNDAMADIVTSALRIGAKTGGAMD 121
Cdd:pfam02424   1 GTTVSITVYGPDEAAAEALEAAIDAELDRLEALLSTYRPDSELSRLNRAGA-GPVKVSPELFELLERALEISELSGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037  122 ITVGPLVnlwgfgpdqqpvhiptqaqidaakaqtglshlkvvneahrnylqkdlpelyVDLSTVGEGYAADHLARLMEQE 201
Cdd:pfam02424  80 ITVGPLV---------------------------------------------------LDLGGIAKGYAVDRAAELLKAK 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037  202 GIARYLVSVGGALNSRGMNADGLSWRVAIQKPtdRENAVQAIVDINGHGISTSGSYRNYYElDGKRLSHVIDPQTGRPIE 281
Cdd:pfam02424 109 GVTSALVNLGGDIRALGTKPDGSPWRVGIQDP--RDPDSLAVLELSDKAVATSGDYERYFE-DGKRYHHIIDPRTGYPVA 185
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 507083037  282 HNLVSVTVIAPtALEADGWDTGLMVLGPEKAKEVVRREG 320
Cdd:pfam02424 186 NGLASVTVIAD-AMLADALATALFVLGPEKGLALLEKLP 223
 
Name Accession Description Interval E-value
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
1-349 0e+00

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 741.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037   1 MEVNFYRAALLAVTIFFVGCDEAPKPAQTTQP-ATVLEGKTMGTFWRVSAVGVDAKRAGELQAKIQAQLDADDQLLSTYK 79
Cdd:PRK10461   1 MEISFTRVALLAAALLLVGCDQAPQPAKTHATeATVLEGKTMGTFWRVSIPGIDAKRSAELQEKIQTQLDADDQLLSTYK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037  80 NDSALMRFNLSKSLSPWPVNDAMADIVTSALRIGAKTGGAMDITVGPLVNLWGFGPDQQPVHIPTQAQIDAAKAQTGLSH 159
Cdd:PRK10461  81 KDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEKQPVQIPSQEQIDAAKAKTGLQH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037 160 LKVVNEAHRNYLQKDLPELYVDLSTVGEGYAADHLARLMEQEGIARYLVSVGGALNSRGMNADGLSWRVAIQKPTDRENA 239
Cdd:PRK10461 161 LTVINQSHQQYLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPTDKENA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037 240 VQAIVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRRE 319
Cdd:PRK10461 241 VQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRRE 320
                        330       340       350
                 ....*....|....*....|....*....|
gi 507083037 320 GLAVYMIIKEGEGFKTWMSPQFKSFLLSEK 349
Cdd:PRK10461 321 GLAVYMITKEGDGFKTWMSPQFKSFLVSEK 350
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
41-341 2.71e-126

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 364.08  E-value: 2.71e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037  41 MGTFWRVSAVGVDAKRAGELQAKIQAQLDADDQLLSTYKNDSALMRFNLSKSLSPWPVNDAMADIVTSALRIGAKTGGAM 120
Cdd:COG1477    1 MGTTVSITLYGPDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037 121 DITVGPLVNLWGFGPDQQpvHIPTQAQIDAAKAQTGLSHLKVvnEAHRNYLQKDLPELYVDLSTVGEGYAADHLARLMEQ 200
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKA--RVPSAAEIAAALALVGYRKVEL--DEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037 201 EGIARYLVSVGGALNSRGMNADGLSWRVAIQKPTDReNAVQAIVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPI 280
Cdd:COG1477  157 AGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPRDP-GAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPV 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507083037 281 EHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRRE-GLAVYMIIKEGEGFktwMSPQF 341
Cdd:COG1477  236 EHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLpGLEALLIDRDGKVF---ASPGF 294
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
42-320 8.25e-78

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: 238.12  E-value: 8.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037   42 GTFWRVSAVGVDAKRAGELQAKIQAQLDADDQLLSTYKNDSALMRFNLSKSlSPWPVNDAMADIVTSALRIGAKTGGAMD 121
Cdd:pfam02424   1 GTTVSITVYGPDEAAAEALEAAIDAELDRLEALLSTYRPDSELSRLNRAGA-GPVKVSPELFELLERALEISELSGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037  122 ITVGPLVnlwgfgpdqqpvhiptqaqidaakaqtglshlkvvneahrnylqkdlpelyVDLSTVGEGYAADHLARLMEQE 201
Cdd:pfam02424  80 ITVGPLV---------------------------------------------------LDLGGIAKGYAVDRAAELLKAK 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037  202 GIARYLVSVGGALNSRGMNADGLSWRVAIQKPtdRENAVQAIVDINGHGISTSGSYRNYYElDGKRLSHVIDPQTGRPIE 281
Cdd:pfam02424 109 GVTSALVNLGGDIRALGTKPDGSPWRVGIQDP--RDPDSLAVLELSDKAVATSGDYERYFE-DGKRYHHIIDPRTGYPVA 185
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 507083037  282 HNLVSVTVIAPtALEADGWDTGLMVLGPEKAKEVVRREG 320
Cdd:pfam02424 186 NGLASVTVIAD-AMLADALATALFVLGPEKGLALLEKLP 223
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
72-306 1.09e-06

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 50.55  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037   72 DQLLSTYKNDSALMRFNLSKSLSPWPVNDAMADIVTSALRIGAKTGGAMDITVGPLVN-LWGFGPDQQPVhiPTQAQIDA 150
Cdd:PTZ00306  100 DTHLNSFNPNSEVSRVNRMPVGEKHQMSAHLKRVMACCQRVYNSSGGCFDPAAGPLVHeLREAARRQKSV--EAEFVIEE 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037  151 AKAQTGLSHLKVVNeAHRNYLQKDLPELYVDLSTVGEGYAADHLARLMEQEGIARYLVSVGGALNSRGMNADGLSWRVAI 230
Cdd:PTZ00306  178 LAGRFTLTNSFAID-LEEGTIARKHEDAMLDLGGVNKGYTVDYVVDRLNAAGFDDVLFEWGGDCRASGVNVQRQPWAVGI 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083037  231 QKPTDRENAVQA----------------IVDINGHGISTSGSYRNY-YELDGKRLSHVIDPQTG---RPIEHNLVSVTVI 290
Cdd:PTZ00306  257 VRPPSVDEVRAAaksgksappdhksllrVMSLNNEALCTSGDYENVlEGPASKVYSSTFDWKRRsllEPTESELAQVSVK 336
                         250
                  ....*....|....*.
gi 507083037  291 APTALEADGWDTGLMV 306
Cdd:PTZ00306  337 CYSCMYADALATASLV 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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