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Conserved domains on  [gi|488153423|ref|WP_002224631|]
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FAD:protein FMN transferase [Neisseria meningitidis]

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 ...
41-340 3.74e-130

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


:

Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 373.71  E-value: 3.74e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423  41 MGTTYTVKYLSNNRDKlpsPAEIQKRIDDALKEVNRQMSTYQPDSEISRFNQHTAGKPLRISSDFAHVTAEAVRLNRLTH 120
Cdd:COG1477    1 MGTTVSITLYGPDEAQ---AEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423 121 GALDVTVGPLVNLWGFGPDKsvTREPSPEQIKQAASYTGIDKIILKQGKDyaSLSKTHPKAYLDLSSIAKGFGVDKVAGE 200
Cdd:COG1477   78 GAFDPTVGPLVNLWGFGPDK--ARVPSAAEIAAALALVGYRKVELDEEGG--TVRLARPGMQLDLGGIAKGYAVDRAAEL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423 201 LEKYGIQNYLVEIGGELHGKGKNARGEPWRIGIEQPNivQGGNTQIIVPLNNRSLATSGDYRIFhVDKSGKRLSHIINPN 280
Cdd:COG1477  154 LRAAGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPR--DPGAVLAVLELSDGAVATSGDYERY-FEIDGKRYSHIIDPR 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488153423 281 NKRPISHNLASISVVADSAMTADGLSTGLFVLGETEALKLAEREK-LAVFLIVRDTGGYRT 340
Cdd:COG1477  231 TGYPVEHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLPgLEALLIDRDGKVFAS 291
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
41-340 3.74e-130

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 373.71  E-value: 3.74e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423  41 MGTTYTVKYLSNNRDKlpsPAEIQKRIDDALKEVNRQMSTYQPDSEISRFNQHTAGKPLRISSDFAHVTAEAVRLNRLTH 120
Cdd:COG1477    1 MGTTVSITLYGPDEAQ---AEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423 121 GALDVTVGPLVNLWGFGPDKsvTREPSPEQIKQAASYTGIDKIILKQGKDyaSLSKTHPKAYLDLSSIAKGFGVDKVAGE 200
Cdd:COG1477   78 GAFDPTVGPLVNLWGFGPDK--ARVPSAAEIAAALALVGYRKVELDEEGG--TVRLARPGMQLDLGGIAKGYAVDRAAEL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423 201 LEKYGIQNYLVEIGGELHGKGKNARGEPWRIGIEQPNivQGGNTQIIVPLNNRSLATSGDYRIFhVDKSGKRLSHIINPN 280
Cdd:COG1477  154 LRAAGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPR--DPGAVLAVLELSDGAVATSGDYERY-FEIDGKRYSHIIDPR 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488153423 281 NKRPISHNLASISVVADSAMTADGLSTGLFVLGETEALKLAEREK-LAVFLIVRDTGGYRT 340
Cdd:COG1477  231 TGYPVEHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLPgLEALLIDRDGKVFAS 291
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
8-350 2.12e-108

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 320.55  E-value: 2.12e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423   8 PNFIRVLIFALgFIFLNAC-------SEQTAQTVTLQGETMGTTYTVKYLSNNRDKLPspaEIQKRIDDALKEVNRQMST 80
Cdd:PRK10461   3 ISFTRVALLAA-ALLLVGCdqapqpaKTHATEATVLEGKTMGTFWRVSIPGIDAKRSA---ELQEKIQTQLDADDQLLST 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423  81 YQPDSEISRFNQHTAGKPLRISSDFAHVTAEAVRLNRLTHGALDVTVGPLVNLWGFGPDKSVTREPSPEQIKQAASYTGI 160
Cdd:PRK10461  79 YKKDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEKQPVQIPSQEQIDAAKAKTGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423 161 D--KIILKQGKDYasLSKTHPKAYLDLSSIAKGFGVDKVAGELEKYGIQNYLVEIGGELHGKGKNARGEPWRIGIEQP-- 236
Cdd:PRK10461 159 QhlTVINQSHQQY--LQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPtd 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423 237 --NIVQGgntqiIVPLNNRSLATSGDYRIFHvDKSGKRLSHIINPNNKRPISHNLASISVVADSAMTADGLSTGLFVLGE 314
Cdd:PRK10461 237 keNAVQA-----VVDINGHGISTSGSYRNYY-ELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGP 310
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 488153423 315 TEALKLAEREKLAVFLIVRDTGGYRTAMSSEFEKLL 350
Cdd:PRK10461 311 EKAKEVVRREGLAVYMITKEGDGFKTWMSPQFKSFL 346
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
42-325 1.73e-88

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: 265.47  E-value: 1.73e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423   42 GTTYTVKYLSNNRDklpSPAEIQKRIDDALKEVNRQMSTYQPDSEISRFNQHtAGKPLRISSDFAHVTAEAVRLNRLTHG 121
Cdd:pfam02424   1 GTTVSITVYGPDEA---AAEALEAAIDAELDRLEALLSTYRPDSELSRLNRA-GAGPVKVSPELFELLERALEISELSGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423  122 ALDVTVGPLVnlwgfgpdksvtrepspeqikqaasytgidkiilkqgkdyaslskthpkayLDLSSIAKGFGVDKVAGEL 201
Cdd:pfam02424  77 AFDITVGPLV---------------------------------------------------LDLGGIAKGYAVDRAAELL 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423  202 EKYGIQNYLVEIGGELHGKGKNARGEPWRIGIEQPNivqGGNTQIIVPLNNRSLATSGDYRIFHVDksGKRLSHIINPNN 281
Cdd:pfam02424 106 KAKGVTSALVNLGGDIRALGTKPDGSPWRVGIQDPR---DPDSLAVLELSDKAVATSGDYERYFED--GKRYHHIIDPRT 180
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 488153423  282 KRPISHNLASISVVADSaMTADGLSTGLFVLGETEALKLAEREK 325
Cdd:pfam02424 181 GYPVANGLASVTVIADA-MLADALATALFVLGPEKGLALLEKLP 223
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
41-340 3.74e-130

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 373.71  E-value: 3.74e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423  41 MGTTYTVKYLSNNRDKlpsPAEIQKRIDDALKEVNRQMSTYQPDSEISRFNQHTAGKPLRISSDFAHVTAEAVRLNRLTH 120
Cdd:COG1477    1 MGTTVSITLYGPDEAQ---AEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423 121 GALDVTVGPLVNLWGFGPDKsvTREPSPEQIKQAASYTGIDKIILKQGKDyaSLSKTHPKAYLDLSSIAKGFGVDKVAGE 200
Cdd:COG1477   78 GAFDPTVGPLVNLWGFGPDK--ARVPSAAEIAAALALVGYRKVELDEEGG--TVRLARPGMQLDLGGIAKGYAVDRAAEL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423 201 LEKYGIQNYLVEIGGELHGKGKNARGEPWRIGIEQPNivQGGNTQIIVPLNNRSLATSGDYRIFhVDKSGKRLSHIINPN 280
Cdd:COG1477  154 LRAAGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPR--DPGAVLAVLELSDGAVATSGDYERY-FEIDGKRYSHIIDPR 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488153423 281 NKRPISHNLASISVVADSAMTADGLSTGLFVLGETEALKLAEREK-LAVFLIVRDTGGYRT 340
Cdd:COG1477  231 TGYPVEHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLPgLEALLIDRDGKVFAS 291
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
8-350 2.12e-108

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 320.55  E-value: 2.12e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423   8 PNFIRVLIFALgFIFLNAC-------SEQTAQTVTLQGETMGTTYTVKYLSNNRDKLPspaEIQKRIDDALKEVNRQMST 80
Cdd:PRK10461   3 ISFTRVALLAA-ALLLVGCdqapqpaKTHATEATVLEGKTMGTFWRVSIPGIDAKRSA---ELQEKIQTQLDADDQLLST 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423  81 YQPDSEISRFNQHTAGKPLRISSDFAHVTAEAVRLNRLTHGALDVTVGPLVNLWGFGPDKSVTREPSPEQIKQAASYTGI 160
Cdd:PRK10461  79 YKKDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEKQPVQIPSQEQIDAAKAKTGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423 161 D--KIILKQGKDYasLSKTHPKAYLDLSSIAKGFGVDKVAGELEKYGIQNYLVEIGGELHGKGKNARGEPWRIGIEQP-- 236
Cdd:PRK10461 159 QhlTVINQSHQQY--LQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPtd 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423 237 --NIVQGgntqiIVPLNNRSLATSGDYRIFHvDKSGKRLSHIINPNNKRPISHNLASISVVADSAMTADGLSTGLFVLGE 314
Cdd:PRK10461 237 keNAVQA-----VVDINGHGISTSGSYRNYY-ELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGP 310
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 488153423 315 TEALKLAEREKLAVFLIVRDTGGYRTAMSSEFEKLL 350
Cdd:PRK10461 311 EKAKEVVRREGLAVYMITKEGDGFKTWMSPQFKSFL 346
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
42-325 1.73e-88

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: 265.47  E-value: 1.73e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423   42 GTTYTVKYLSNNRDklpSPAEIQKRIDDALKEVNRQMSTYQPDSEISRFNQHtAGKPLRISSDFAHVTAEAVRLNRLTHG 121
Cdd:pfam02424   1 GTTVSITVYGPDEA---AAEALEAAIDAELDRLEALLSTYRPDSELSRLNRA-GAGPVKVSPELFELLERALEISELSGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423  122 ALDVTVGPLVnlwgfgpdksvtrepspeqikqaasytgidkiilkqgkdyaslskthpkayLDLSSIAKGFGVDKVAGEL 201
Cdd:pfam02424  77 AFDITVGPLV---------------------------------------------------LDLGGIAKGYAVDRAAELL 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423  202 EKYGIQNYLVEIGGELHGKGKNARGEPWRIGIEQPNivqGGNTQIIVPLNNRSLATSGDYRIFHVDksGKRLSHIINPNN 281
Cdd:pfam02424 106 KAKGVTSALVNLGGDIRALGTKPDGSPWRVGIQDPR---DPDSLAVLELSDKAVATSGDYERYFED--GKRYHHIIDPRT 180
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 488153423  282 KRPISHNLASISVVADSaMTADGLSTGLFVLGETEALKLAEREK 325
Cdd:pfam02424 181 GYPVANGLASVTVIADA-MLADALATALFVLGPEKGLALLEKLP 223
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
26-351 4.21e-30

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 121.42  E-value: 4.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423   26 CSEQTAQTVTLQGETMGTTYTVKYLSNNRDKLPSPAEIQKRI-DDALKEVNRQMSTYQPDSEISRFNQHTAGKPLRISSD 104
Cdd:PTZ00306   50 LHVNQRAQLLYKGLEHTVPYTLKVVVAGPVARQDADAVAKEVlRSAFQMVDTHLNSFNPNSEVSRVNRMPVGEKHQMSAH 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423  105 FAHVTAEAVRLNRLTHGALDVTVGPLVN-LWGFGPDK-SVTREPSPEQIKQAASYTGIDKIILKQGkdyaSLSKTHPKAY 182
Cdd:PTZ00306  130 LKRVMACCQRVYNSSGGCFDPAAGPLVHeLREAARRQkSVEAEFVIEELAGRFTLTNSFAIDLEEG----TIARKHEDAM 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423  183 LDLSSIAKGFGVDKVAGELEKYGIQNYLVEIGGELHGKGKNARGEPWRIGIEQP----NIVQGGNTQI-----------I 247
Cdd:PTZ00306  206 LDLGGVNKGYTVDYVVDRLNAAGFDDVLFEWGGDCRASGVNVQRQPWAVGIVRPpsvdEVRAAAKSGKsappdhksllrV 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488153423  248 VPLNNRSLATSGDYRIFHVDKSGKRLSHIINPNNK---RPISHNLASISVVADSAMTADGLSTGLFVLGETEALklaeRE 324
Cdd:PTZ00306  286 MSLNNEALCTSGDYENVLEGPASKVYSSTFDWKRRsllEPTESELAQVSVKCYSCMYADALATASLVKRDPVKV----RY 361
                         330       340
                  ....*....|....*....|....*..
gi 488153423  325 KLAVFLIVRDTGGYRTAMSSEFEKLLR 351
Cdd:PTZ00306  362 MLENWRYVRNRVTDYTTYTREGERVAH 388
 
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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