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Conserved domains on  [gi|1423924313|ref|WP_112307889|]
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MULTISPECIES: FAD:protein FMN transferase [unclassified Providencia]

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 ...
35-335 2.31e-139

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


:

Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 396.82  E-value: 2.31e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313  35 MGTYYSVKYVtDSSESKPEAIQAEIDKRLEEVNDQMSTYRPDSELSRFNQfKEVNTPFPVSAATATVVKKAIEINKLTNG 114
Cdd:COG1477     1 MGTTVSITLY-GPDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNR-AAGGEPVKVSPELAELLERALEISELSDG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 115 SLDVTVGPLVNLWGFGPEGRvtKAPSDEELAKRRAWTGIEKLSVQDNN--LIKTIPELYVDLSSIAKGYGVDVVAEYLES 192
Cdd:COG1477    79 AFDPTVGPLVNLWGFGPDKA--RVPSAAEIAAALALVGYRKVELDEEGgtVRLARPGMQLDLGGIAKGYAVDRAAELLRA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 193 LDINNYMVDIGGEVRTKGTNGKEVPWRIAIEKPVADGvsqTAQEIIEPGDRSIATSGDYRNYFEQDGVRFSHTIDPKTGK 272
Cdd:COG1477   157 AGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPRDPG---AVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGY 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423924313 273 PITHNLVSITVIAENCMSADGLSTGLNVLGPEVGFDLAEK-MNIPVFMIVKTDKGFeerYTKAF 335
Cdd:COG1477   234 PVEHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERlPGLEALLIDRDGKVF---ASPGF 294
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
35-335 2.31e-139

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 396.82  E-value: 2.31e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313  35 MGTYYSVKYVtDSSESKPEAIQAEIDKRLEEVNDQMSTYRPDSELSRFNQfKEVNTPFPVSAATATVVKKAIEINKLTNG 114
Cdd:COG1477     1 MGTTVSITLY-GPDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNR-AAGGEPVKVSPELAELLERALEISELSDG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 115 SLDVTVGPLVNLWGFGPEGRvtKAPSDEELAKRRAWTGIEKLSVQDNN--LIKTIPELYVDLSSIAKGYGVDVVAEYLES 192
Cdd:COG1477    79 AFDPTVGPLVNLWGFGPDKA--RVPSAAEIAAALALVGYRKVELDEEGgtVRLARPGMQLDLGGIAKGYAVDRAAELLRA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 193 LDINNYMVDIGGEVRTKGTNGKEVPWRIAIEKPVADGvsqTAQEIIEPGDRSIATSGDYRNYFEQDGVRFSHTIDPKTGK 272
Cdd:COG1477   157 AGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPRDPG---AVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGY 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423924313 273 PITHNLVSITVIAENCMSADGLSTGLNVLGPEVGFDLAEK-MNIPVFMIVKTDKGFeerYTKAF 335
Cdd:COG1477   234 PVEHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERlPGLEALLIDRDGKVF---ASPGF 294
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
11-343 3.75e-123

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 357.91  E-value: 3.75e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313  11 LLFVAALFLTAC---------GGPEQQNLQGQTMGTYYSVKYVTDSSESKPEaIQAEIDKRLEEVNDQMSTYRPDSELSR 81
Cdd:PRK10461    9 ALLAAALLLVGCdqapqpaktHATEATVLEGKTMGTFWRVSIPGIDAKRSAE-LQEKIQTQLDADDQLLSTYKKDSALMR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313  82 FNQFKEVNtPFPVSAATATVVKKAIEINKLTNGSLDVTVGPLVNLWGFGPEGRVTKAPSDEELAKRRAWTGIEKLSVQDN 161
Cdd:PRK10461   88 FNDSQSLS-PWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEKQPVQIPSQEQIDAAKAKTGLQHLTVINQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 162 N----LIKTIPELYVDLSSIAKGYGVDVVAEYLESLDINNYMVDIGGEVRTKGTNGKEVPWRIAIEKPVADgvSQTAQEI 237
Cdd:PRK10461  167 ShqqyLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPTDK--ENAVQAV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 238 IEPGDRSIATSGDYRNYFEQDGVRFSHTIDPKTGKPITHNLVSITVIAENCMSADGLSTGLNVLGPEVGFDLAEKMNIPV 317
Cdd:PRK10461  245 VDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRREGLAV 324
                         330       340
                  ....*....|....*....|....*.
gi 1423924313 318 FMIVKTDKGFEERYTKAFEPFLTKKQ 343
Cdd:PRK10461  325 YMITKEGDGFKTWMSPQFKSFLVSEK 350
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
36-314 1.03e-95

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: 283.57  E-value: 1.03e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313  36 GTYYSVKYVTDSSESKpEAIQAEIDKRLEEVNDQMSTYRPDSELSRFNQFKEvnTPFPVSAATATVVKKAIEINKLTNGS 115
Cdd:pfam02424   1 GTTVSITVYGPDEAAA-EALEAAIDAELDRLEALLSTYRPDSELSRLNRAGA--GPVKVSPELFELLERALEISELSGGA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 116 LDVTVGPLVnlwgfgpegrvtkapsdeelakrrawtgieklsvqdnnliktipelyVDLSSIAKGYGVDVVAEYLESLDI 195
Cdd:pfam02424  78 FDITVGPLV-----------------------------------------------LDLGGIAKGYAVDRAAELLKAKGV 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 196 NNYMVDIGGEVRTKGTNGKEVPWRIAIEKPVADGvsqtAQEIIEPGDRSIATSGDYRNYFEqDGVRFSHTIDPKTGKPIT 275
Cdd:pfam02424 111 TSALVNLGGDIRALGTKPDGSPWRVGIQDPRDPD----SLAVLELSDKAVATSGDYERYFE-DGKRYHHIIDPRTGYPVA 185
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1423924313 276 HNLVSITVIAeNCMSADGLSTGLNVLGPEVGFDLAEKMN 314
Cdd:pfam02424 186 NGLASVTVIA-DAMLADALATALFVLGPEKGLALLEKLP 223
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
35-335 2.31e-139

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 396.82  E-value: 2.31e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313  35 MGTYYSVKYVtDSSESKPEAIQAEIDKRLEEVNDQMSTYRPDSELSRFNQfKEVNTPFPVSAATATVVKKAIEINKLTNG 114
Cdd:COG1477     1 MGTTVSITLY-GPDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNR-AAGGEPVKVSPELAELLERALEISELSDG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 115 SLDVTVGPLVNLWGFGPEGRvtKAPSDEELAKRRAWTGIEKLSVQDNN--LIKTIPELYVDLSSIAKGYGVDVVAEYLES 192
Cdd:COG1477    79 AFDPTVGPLVNLWGFGPDKA--RVPSAAEIAAALALVGYRKVELDEEGgtVRLARPGMQLDLGGIAKGYAVDRAAELLRA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 193 LDINNYMVDIGGEVRTKGTNGKEVPWRIAIEKPVADGvsqTAQEIIEPGDRSIATSGDYRNYFEQDGVRFSHTIDPKTGK 272
Cdd:COG1477   157 AGVTNALVNLGGDIRALGTKPDGRPWRVGIEDPRDPG---AVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGY 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423924313 273 PITHNLVSITVIAENCMSADGLSTGLNVLGPEVGFDLAEK-MNIPVFMIVKTDKGFeerYTKAF 335
Cdd:COG1477   234 PVEHGLASVTVIAPDAMLADALATALFVLGPEKGLALAERlPGLEALLIDRDGKVF---ASPGF 294
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
11-343 3.75e-123

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 357.91  E-value: 3.75e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313  11 LLFVAALFLTAC---------GGPEQQNLQGQTMGTYYSVKYVTDSSESKPEaIQAEIDKRLEEVNDQMSTYRPDSELSR 81
Cdd:PRK10461    9 ALLAAALLLVGCdqapqpaktHATEATVLEGKTMGTFWRVSIPGIDAKRSAE-LQEKIQTQLDADDQLLSTYKKDSALMR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313  82 FNQFKEVNtPFPVSAATATVVKKAIEINKLTNGSLDVTVGPLVNLWGFGPEGRVTKAPSDEELAKRRAWTGIEKLSVQDN 161
Cdd:PRK10461   88 FNDSQSLS-PWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLWGFGPEKQPVQIPSQEQIDAAKAKTGLQHLTVINQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 162 N----LIKTIPELYVDLSSIAKGYGVDVVAEYLESLDINNYMVDIGGEVRTKGTNGKEVPWRIAIEKPVADgvSQTAQEI 237
Cdd:PRK10461  167 ShqqyLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPTDK--ENAVQAV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 238 IEPGDRSIATSGDYRNYFEQDGVRFSHTIDPKTGKPITHNLVSITVIAENCMSADGLSTGLNVLGPEVGFDLAEKMNIPV 317
Cdd:PRK10461  245 VDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGPEKAKEVVRREGLAV 324
                         330       340
                  ....*....|....*....|....*.
gi 1423924313 318 FMIVKTDKGFEERYTKAFEPFLTKKQ 343
Cdd:PRK10461  325 YMITKEGDGFKTWMSPQFKSFLVSEK 350
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
36-314 1.03e-95

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: 283.57  E-value: 1.03e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313  36 GTYYSVKYVTDSSESKpEAIQAEIDKRLEEVNDQMSTYRPDSELSRFNQFKEvnTPFPVSAATATVVKKAIEINKLTNGS 115
Cdd:pfam02424   1 GTTVSITVYGPDEAAA-EALEAAIDAELDRLEALLSTYRPDSELSRLNRAGA--GPVKVSPELFELLERALEISELSGGA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 116 LDVTVGPLVnlwgfgpegrvtkapsdeelakrrawtgieklsvqdnnliktipelyVDLSSIAKGYGVDVVAEYLESLDI 195
Cdd:pfam02424  78 FDITVGPLV-----------------------------------------------LDLGGIAKGYAVDRAAELLKAKGV 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313 196 NNYMVDIGGEVRTKGTNGKEVPWRIAIEKPVADGvsqtAQEIIEPGDRSIATSGDYRNYFEqDGVRFSHTIDPKTGKPIT 275
Cdd:pfam02424 111 TSALVNLGGDIRALGTKPDGSPWRVGIQDPRDPD----SLAVLELSDKAVATSGDYERYFE-DGKRYHHIIDPRTGYPVA 185
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1423924313 276 HNLVSITVIAeNCMSADGLSTGLNVLGPEVGFDLAEKMN 314
Cdd:pfam02424 186 NGLASVTVIA-DAMLADALATALFVLGPEKGLALLEKLP 223
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
23-296 1.21e-23

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 102.16  E-value: 1.21e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313   23 GGPEQQNLQGQTMGTYYSVKY-----VTDSSE-SKPEAIQAEIDKRLEEVNDQ-MSTYRPDSELSRFNQFKeVNTPFPVS 95
Cdd:PTZ00306    49 ELHVNQRAQLLYKGLEHTVPYtlkvvVAGPVArQDADAVAKEVLRSAFQMVDThLNSFNPNSEVSRVNRMP-VGEKHQMS 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313   96 AATATVVKKAIEINKLTNGSLDVTVGPLVN-LWGFGPEGRVTKAPS-DEELAKRRAWTGIEKLSVQDNNLIKTIPELYVD 173
Cdd:PTZ00306   128 AHLKRVMACCQRVYNSSGGCFDPAAGPLVHeLREAARRQKSVEAEFvIEELAGRFTLTNSFAIDLEEGTIARKHEDAMLD 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423924313  174 LSSIAKGYGVDVVAEYLESLDINNYMVDIGGEVRTKGTNGKEVPWRIAIEKPVA-DGVSQTAQE-------------IIE 239
Cdd:PTZ00306   208 LGGVNKGYTVDYVVDRLNAAGFDDVLFEWGGDCRASGVNVQRQPWAVGIVRPPSvDEVRAAAKSgksappdhksllrVMS 287
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423924313  240 PGDRSIATSGDYRNYFEQDGVR-FSHTIDPKTG---KPITHNLVSITVIAENCMSADGLST 296
Cdd:PTZ00306   288 LNNEALCTSGDYENVLEGPASKvYSSTFDWKRRsllEPTESELAQVSVKCYSCMYADALAT 348
 
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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