NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1858940721|ref|WP_174823087|]
View 

MULTISPECIES: FAD:protein FMN transferase [Pasteurella]

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
PubMed:  23558683
SCOP:  4003899

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
34-338 1.13e-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: 369.86  E-value: 1.13e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721  34 MGTTYSVKYIDDGQIKIKPIEmhGQIEEILKEVNNKMSTYLSTSELSQFNQNTQIDtPVEISADLAFVLKEAIRLHGVTE 113
Cdd:COG1477     1 MGTTVSITLYGPDEAQAEAAL--AAAFAELDRLEALLSTYRPDSELSRLNRAAGGE-PVKVSPELAELLERALEISELSD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 114 GALDVTVGPIVNLWGFGPEKRQPNEtlEEQVEKRRAWVGIEKMKLTEQGDKFYLAKtvPQLYIDLSSIAKGFGVDKVAAH 193
Cdd:COG1477    78 GAFDPTVGPLVNLWGFGPDKARVPS--AAEIAAALALVGYRKVELDEEGGTVRLAR--PGMQLDLGGIAKGYAVDRAAEL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 194 LATKGIANYLVEIGGEINAKGKNIEGKDWQIAIEKPNFDGsrAVSQIIGLKDFSMATSGNYRNYFEENGRHFSHEIDPKT 273
Cdd:COG1477   154 LRAAGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPRDPG--AVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRT 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1858940721 274 GYPIEHRLASITVLADSTMTADGLSTGLYVLGEEKALEVAEKYNLL-VYLISKTEKGFeakMSSAF 338
Cdd:COG1477   232 GYPVEHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLPGLeALLIDRDGKVF---ASPGF 294
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
34-338 1.13e-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: 369.86  E-value: 1.13e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721  34 MGTTYSVKYIDDGQIKIKPIEmhGQIEEILKEVNNKMSTYLSTSELSQFNQNTQIDtPVEISADLAFVLKEAIRLHGVTE 113
Cdd:COG1477     1 MGTTVSITLYGPDEAQAEAAL--AAAFAELDRLEALLSTYRPDSELSRLNRAAGGE-PVKVSPELAELLERALEISELSD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 114 GALDVTVGPIVNLWGFGPEKRQPNEtlEEQVEKRRAWVGIEKMKLTEQGDKFYLAKtvPQLYIDLSSIAKGFGVDKVAAH 193
Cdd:COG1477    78 GAFDPTVGPLVNLWGFGPDKARVPS--AAEIAAALALVGYRKVELDEEGGTVRLAR--PGMQLDLGGIAKGYAVDRAAEL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 194 LATKGIANYLVEIGGEINAKGKNIEGKDWQIAIEKPNFDGsrAVSQIIGLKDFSMATSGNYRNYFEENGRHFSHEIDPKT 273
Cdd:COG1477   154 LRAAGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPRDPG--AVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRT 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1858940721 274 GYPIEHRLASITVLADSTMTADGLSTGLYVLGEEKALEVAEKYNLL-VYLISKTEKGFeakMSSAF 338
Cdd:COG1477   232 GYPVEHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLPGLeALLIDRDGKVF---ASPGF 294
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
23-342 1.40e-111

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 328.64  E-value: 1.40e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721  23 SPEVVTITGKTMGTTYSVKYIDDGQIKIKpiEMHGQIEEILKEVNNKMSTYLSTSELSQFNQNTQIDtPVEISADLAFVL 102
Cdd:PRK10461   31 ATEATVLEGKTMGTFWRVSIPGIDAKRSA--ELQEKIQTQLDADDQLLSTYKKDSALMRFNDSQSLS-PWPVSEAMADIV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 103 KEAIRLHGVTEGALDVTVGPIVNLWGFGPEKrQPNET-LEEQVEKRRAWVGIEKMKLTEQGDKFYLAKTVPQLYIDLSSI 181
Cdd:PRK10461  108 TTSLRIGAKTDGAMDITVGPLVNLWGFGPEK-QPVQIpSQEQIDAAKAKTGLQHLTVINQSHQQYLQKDLPDLYVDLSTV 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 182 AKGFGVDKVAAHLATKGIANYLVEIGGEINAKGKNIEGKDWQIAIEKPNfDGSRAVSQIIGLKDFSMATSGNYRNYFEEN 261
Cdd:PRK10461  187 GEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPT-DKENAVQAVVDINGHGISTSGSYRNYYELD 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 262 GRHFSHEIDPKTGYPIEHRLASITVLADSTMTADGLSTGLYVLGEEKALEVAEKYNLLVYLISKTEKGFEAKMSSAFEKL 341
Cdd:PRK10461  266 GKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRREGLAVYMITKEGDGFKTWMSPQFKSF 345

                  .
gi 1858940721 342 L 342
Cdd:PRK10461  346 L 346
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
35-319 4.64e-90

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: 269.32  E-value: 4.64e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721  35 GTTYSVKYIDDGqiKIKPIEMHGQIEEILKEVNNKMSTYLSTSELSQFNQNTQidTPVEISADLAFVLKEAIRLHGVTEG 114
Cdd:pfam02424   1 GTTVSITVYGPD--EAAAEALEAAIDAELDRLEALLSTYRPDSELSRLNRAGA--GPVKVSPELFELLERALEISELSGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 115 ALDVTVGPIVnlwgfgpekrqpnetleeqvekrrawvgiekmklteqgdkfylaktvpqlyIDLSSIAKGFGVDKVAAHL 194
Cdd:pfam02424  77 AFDITVGPLV---------------------------------------------------LDLGGIAKGYAVDRAAELL 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 195 ATKGIANYLVEIGGEINAKGKNIEGKDWQIAIEKPNFDGSRAVsqiIGLKDFSMATSGNYRNYFEEnGRHFSHEIDPKTG 274
Cdd:pfam02424 106 KAKGVTSALVNLGGDIRALGTKPDGSPWRVGIQDPRDPDSLAV---LELSDKAVATSGDYERYFED-GKRYHHIIDPRTG 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1858940721 275 YPIEHRLASITVLADStMTADGLSTGLYVLGEEKALEVAEKYNLL 319
Cdd:pfam02424 182 YPVANGLASVTVIADA-MLADALATALFVLGPEKGLALLEKLPGL 225
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
34-338 1.13e-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: 369.86  E-value: 1.13e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721  34 MGTTYSVKYIDDGQIKIKPIEmhGQIEEILKEVNNKMSTYLSTSELSQFNQNTQIDtPVEISADLAFVLKEAIRLHGVTE 113
Cdd:COG1477     1 MGTTVSITLYGPDEAQAEAAL--AAAFAELDRLEALLSTYRPDSELSRLNRAAGGE-PVKVSPELAELLERALEISELSD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 114 GALDVTVGPIVNLWGFGPEKRQPNEtlEEQVEKRRAWVGIEKMKLTEQGDKFYLAKtvPQLYIDLSSIAKGFGVDKVAAH 193
Cdd:COG1477    78 GAFDPTVGPLVNLWGFGPDKARVPS--AAEIAAALALVGYRKVELDEEGGTVRLAR--PGMQLDLGGIAKGYAVDRAAEL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 194 LATKGIANYLVEIGGEINAKGKNIEGKDWQIAIEKPNFDGsrAVSQIIGLKDFSMATSGNYRNYFEENGRHFSHEIDPKT 273
Cdd:COG1477   154 LRAAGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPRDPG--AVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRT 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1858940721 274 GYPIEHRLASITVLADSTMTADGLSTGLYVLGEEKALEVAEKYNLL-VYLISKTEKGFeakMSSAF 338
Cdd:COG1477   232 GYPVEHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERLPGLeALLIDRDGKVF---ASPGF 294
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
23-342 1.40e-111

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 328.64  E-value: 1.40e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721  23 SPEVVTITGKTMGTTYSVKYIDDGQIKIKpiEMHGQIEEILKEVNNKMSTYLSTSELSQFNQNTQIDtPVEISADLAFVL 102
Cdd:PRK10461   31 ATEATVLEGKTMGTFWRVSIPGIDAKRSA--ELQEKIQTQLDADDQLLSTYKKDSALMRFNDSQSLS-PWPVSEAMADIV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 103 KEAIRLHGVTEGALDVTVGPIVNLWGFGPEKrQPNET-LEEQVEKRRAWVGIEKMKLTEQGDKFYLAKTVPQLYIDLSSI 181
Cdd:PRK10461  108 TTSLRIGAKTDGAMDITVGPLVNLWGFGPEK-QPVQIpSQEQIDAAKAKTGLQHLTVINQSHQQYLQKDLPDLYVDLSTV 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 182 AKGFGVDKVAAHLATKGIANYLVEIGGEINAKGKNIEGKDWQIAIEKPNfDGSRAVSQIIGLKDFSMATSGNYRNYFEEN 261
Cdd:PRK10461  187 GEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPT-DKENAVQAVVDINGHGISTSGSYRNYYELD 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 262 GRHFSHEIDPKTGYPIEHRLASITVLADSTMTADGLSTGLYVLGEEKALEVAEKYNLLVYLISKTEKGFEAKMSSAFEKL 341
Cdd:PRK10461  266 GKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRREGLAVYMITKEGDGFKTWMSPQFKSF 345

                  .
gi 1858940721 342 L 342
Cdd:PRK10461  346 L 346
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
35-319 4.64e-90

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: 269.32  E-value: 4.64e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721  35 GTTYSVKYIDDGqiKIKPIEMHGQIEEILKEVNNKMSTYLSTSELSQFNQNTQidTPVEISADLAFVLKEAIRLHGVTEG 114
Cdd:pfam02424   1 GTTVSITVYGPD--EAAAEALEAAIDAELDRLEALLSTYRPDSELSRLNRAGA--GPVKVSPELFELLERALEISELSGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 115 ALDVTVGPIVnlwgfgpekrqpnetleeqvekrrawvgiekmklteqgdkfylaktvpqlyIDLSSIAKGFGVDKVAAHL 194
Cdd:pfam02424  77 AFDITVGPLV---------------------------------------------------LDLGGIAKGYAVDRAAELL 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721 195 ATKGIANYLVEIGGEINAKGKNIEGKDWQIAIEKPNFDGSRAVsqiIGLKDFSMATSGNYRNYFEEnGRHFSHEIDPKTG 274
Cdd:pfam02424 106 KAKGVTSALVNLGGDIRALGTKPDGSPWRVGIQDPRDPDSLAV---LELSDKAVATSGDYERYFED-GKRYHHIIDPRTG 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1858940721 275 YPIEHRLASITVLADStMTADGLSTGLYVLGEEKALEVAEKYNLL 319
Cdd:pfam02424 182 YPVANGLASVTVIADA-MLADALATALFVLGPEKGLALLEKLPGL 225
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
60-303 6.53e-18

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 85.22  E-value: 6.53e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721   60 EEILKE----VNNKMSTYLSTSELSQFNQntqidTPV----EISADLAFVLKEAIRLHGVTEGALDVTVGPIVN-LWGFG 130
Cdd:PTZ00306    89 KEVLRSafqmVDTHLNSFNPNSEVSRVNR-----MPVgekhQMSAHLKRVMACCQRVYNSSGGCFDPAAGPLVHeLREAA 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721  131 PEKRQ-PNETLEEQVekrrawvgIEKMKLTEQGDKFYLAKTVPQLY----IDLSSIAKGFGVDKVAAHLATKGIANYLVE 205
Cdd:PTZ00306   164 RRQKSvEAEFVIEEL--------AGRFTLTNSFAIDLEEGTIARKHedamLDLGGVNKGYTVDYVVDRLNAAGFDDVLFE 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858940721  206 IGGEINAKGKNIEGKDWQIAIEKP---------------NFDGSRAVSQIIGLKDFSMATSGNYRNYFEENG-RHFSHEI 269
Cdd:PTZ00306   236 WGGDCRASGVNVQRQPWAVGIVRPpsvdevraaaksgksAPPDHKSLLRVMSLNNEALCTSGDYENVLEGPAsKVYSSTF 315
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1858940721  270 DPKTG---YPIEHRLASITVLADSTMTADGLSTGLYV 303
Cdd:PTZ00306   316 DWKRRsllEPTESELAQVSVKCYSCMYADALATASLV 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH