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Conserved domains on  [gi|1711178106|gb|TVS28876|]
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FAD:protein FMN transferase [Lactobacillus crispatus]

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 ...
17-304 4.07e-98

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


:

Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 290.51  E-value: 4.07e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106  17 LGTSITLQIFG---TQNRDLLQKSFDLIDHYEDIFTVNRDESEVMDINHAAGEHPVQVSSAVYGLVKLAVEKSRE-NFGF 92
Cdd:COG1477     1 MGTTVSITLYGpdeAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELsDGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106  93 NALIGPVVKLWHIGFKGAHVPKDEEIKDRMLLTDPFKVVLNDSDQSVFLKMKGMELDLGGIAKGWIADRIRDLWRAYGVE 172
Cdd:COG1477    81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106 173 AGIINLGGNILLVGDSPKRisGQWSIGVQDPKQPrGDNITSVMVPECSAVTSGTYERYLVVNGKKYHHLIDPRTGYPVKT 252
Cdd:COG1477   161 NALVNLGGDIRALGTKPDG--RPWRVGIEDPRDP-GAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEH 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1711178106 253 DLAGVTTFTKTSVEAEIECKRLFFAGKPlKG--WHDNPDRIGAIFVYNDEHIEY 304
Cdd:COG1477   238 GLASVTVIAPDAMLADALATALFVLGPE-KGlaLAERLPGLEALLIDRDGKVFA 290
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
17-304 4.07e-98

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 290.51  E-value: 4.07e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106  17 LGTSITLQIFG---TQNRDLLQKSFDLIDHYEDIFTVNRDESEVMDINHAAGEHPVQVSSAVYGLVKLAVEKSRE-NFGF 92
Cdd:COG1477     1 MGTTVSITLYGpdeAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELsDGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106  93 NALIGPVVKLWHIGFKGAHVPKDEEIKDRMLLTDPFKVVLNDSDQSVFLKMKGMELDLGGIAKGWIADRIRDLWRAYGVE 172
Cdd:COG1477    81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106 173 AGIINLGGNILLVGDSPKRisGQWSIGVQDPKQPrGDNITSVMVPECSAVTSGTYERYLVVNGKKYHHLIDPRTGYPVKT 252
Cdd:COG1477   161 NALVNLGGDIRALGTKPDG--RPWRVGIEDPRDP-GAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEH 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1711178106 253 DLAGVTTFTKTSVEAEIECKRLFFAGKPlKG--WHDNPDRIGAIFVYNDEHIEY 304
Cdd:COG1477   238 GLASVTVIAPDAMLADALATALFVLGPE-KGlaLAERLPGLEALLIDRDGKVFA 290
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
18-278 1.26e-62

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: 197.67  E-value: 1.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106  18 GTSITLQIFG---TQNRDLLQKSFDLIDHYEDIFTVNRDESEVMDINhAAGEHPVQVSSAVYGLVKLAVEKSRE-NFGFN 93
Cdd:pfam02424   1 GTTVSITVYGpdeAAAEALEAAIDAELDRLEALLSTYRPDSELSRLN-RAGAGPVKVSPELFELLERALEISELsGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106  94 ALIGPVVklwhigfkgahvpkdeeikdrmlltdpfkvvlndsdqsvflkmkgmeLDLGGIAKGWIADRIRDLWRAYGVEA 173
Cdd:pfam02424  80 ITVGPLV-----------------------------------------------LDLGGIAKGYAVDRAAELLKAKGVTS 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106 174 GIINLGGNILLVGDSPKRisGQWSIGVQDPKQPrgDNITSVMVPECSAVTSGTYERYLVVnGKKYHHLIDPRTGYPVKTD 253
Cdd:pfam02424 113 ALVNLGGDIRALGTKPDG--SPWRVGIQDPRDP--DSLAVLELSDKAVATSGDYERYFED-GKRYHHIIDPRTGYPVANG 187
                         250       260
                  ....*....|....*....|....*
gi 1711178106 254 LAGVTTFTkTSVEAEIECKRLFFAG 278
Cdd:pfam02424 188 LASVTVIA-DAMLADALATALFVLG 211
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
8-268 3.83e-20

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 89.04  E-value: 3.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106   8 EQVVGDHHALGTSITLQIFG--TQNRDLLQKSFD-LIDHYEDIFTVNRDESEVMDINHAAGEHPVQVSSAVYGLVKLAVE 84
Cdd:PRK10461   33 EATVLEGKTMGTFWRVSIPGidAKRSAELQEKIQtQLDADDQLLSTYKKDSALMRFNDSQSLSPWPVSEAMADIVTTSLR 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106  85 KSRENFG-FNALIGPVVKLWhiGF----KGAHVPKDEEIKDRMLLTDPFKV-VLNDSDQSVFLK-MKGMELDLGGIAKGW 157
Cdd:PRK10461  113 IGAKTDGaMDITVGPLVNLW--GFgpekQPVQIPSQEQIDAAKAKTGLQHLtVINQSHQQYLQKdLPDLYVDLSTVGEGY 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106 158 IADRIRDLWRAYGVEAGIINLGGNILLVGDSPkriSGQ-WSIGVQDPKQPRGDNITSVMVPECSAVTSGTYERYLVVNGK 236
Cdd:PRK10461  191 AADHLARLMEQEGISRYLVSVGGALSSRGMNG---EGQpWRVAIQKPTDKENAVQAVVDINGHGISTSGSYRNYYELDGK 267
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1711178106 237 KYHHLIDPRTGYPVKTDLAGVTTFTKTSVEAE 268
Cdd:PRK10461  268 RLSHVIDPQTGRPIEHNLVSVTVIAPTALEAD 299
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
17-304 4.07e-98

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 290.51  E-value: 4.07e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106  17 LGTSITLQIFG---TQNRDLLQKSFDLIDHYEDIFTVNRDESEVMDINHAAGEHPVQVSSAVYGLVKLAVEKSRE-NFGF 92
Cdd:COG1477     1 MGTTVSITLYGpdeAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELsDGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106  93 NALIGPVVKLWHIGFKGAHVPKDEEIKDRMLLTDPFKVVLNDSDQSVFLKMKGMELDLGGIAKGWIADRIRDLWRAYGVE 172
Cdd:COG1477    81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106 173 AGIINLGGNILLVGDSPKRisGQWSIGVQDPKQPrGDNITSVMVPECSAVTSGTYERYLVVNGKKYHHLIDPRTGYPVKT 252
Cdd:COG1477   161 NALVNLGGDIRALGTKPDG--RPWRVGIEDPRDP-GAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEH 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1711178106 253 DLAGVTTFTKTSVEAEIECKRLFFAGKPlKG--WHDNPDRIGAIFVYNDEHIEY 304
Cdd:COG1477   238 GLASVTVIAPDAMLADALATALFVLGPE-KGlaLAERLPGLEALLIDRDGKVFA 290
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
18-278 1.26e-62

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: 197.67  E-value: 1.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106  18 GTSITLQIFG---TQNRDLLQKSFDLIDHYEDIFTVNRDESEVMDINhAAGEHPVQVSSAVYGLVKLAVEKSRE-NFGFN 93
Cdd:pfam02424   1 GTTVSITVYGpdeAAAEALEAAIDAELDRLEALLSTYRPDSELSRLN-RAGAGPVKVSPELFELLERALEISELsGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106  94 ALIGPVVklwhigfkgahvpkdeeikdrmlltdpfkvvlndsdqsvflkmkgmeLDLGGIAKGWIADRIRDLWRAYGVEA 173
Cdd:pfam02424  80 ITVGPLV-----------------------------------------------LDLGGIAKGYAVDRAAELLKAKGVTS 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106 174 GIINLGGNILLVGDSPKRisGQWSIGVQDPKQPrgDNITSVMVPECSAVTSGTYERYLVVnGKKYHHLIDPRTGYPVKTD 253
Cdd:pfam02424 113 ALVNLGGDIRALGTKPDG--SPWRVGIQDPRDP--DSLAVLELSDKAVATSGDYERYFED-GKRYHHIIDPRTGYPVANG 187
                         250       260
                  ....*....|....*....|....*
gi 1711178106 254 LAGVTTFTkTSVEAEIECKRLFFAG 278
Cdd:pfam02424 188 LASVTVIA-DAMLADALATALFVLG 211
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
8-268 3.83e-20

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 89.04  E-value: 3.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106   8 EQVVGDHHALGTSITLQIFG--TQNRDLLQKSFD-LIDHYEDIFTVNRDESEVMDINHAAGEHPVQVSSAVYGLVKLAVE 84
Cdd:PRK10461   33 EATVLEGKTMGTFWRVSIPGidAKRSAELQEKIQtQLDADDQLLSTYKKDSALMRFNDSQSLSPWPVSEAMADIVTTSLR 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106  85 KSRENFG-FNALIGPVVKLWhiGF----KGAHVPKDEEIKDRMLLTDPFKV-VLNDSDQSVFLK-MKGMELDLGGIAKGW 157
Cdd:PRK10461  113 IGAKTDGaMDITVGPLVNLW--GFgpekQPVQIPSQEQIDAAKAKTGLQHLtVINQSHQQYLQKdLPDLYVDLSTVGEGY 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106 158 IADRIRDLWRAYGVEAGIINLGGNILLVGDSPkriSGQ-WSIGVQDPKQPRGDNITSVMVPECSAVTSGTYERYLVVNGK 236
Cdd:PRK10461  191 AADHLARLMEQEGISRYLVSVGGALSSRGMNG---EGQpWRVAIQKPTDKENAVQAVVDINGHGISTSGSYRNYYELDGK 267
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1711178106 237 KYHHLIDPRTGYPVKTDLAGVTTFTKTSVEAE 268
Cdd:PRK10461  268 RLSHVIDPQTGRPIEHNLVSVTVIAPTALEAD 299
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
33-237 1.21e-07

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 53.24  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106   33 LLQKSFDLIDHYEDIFTVNrdeSEVMDINH--AAGEHpvQVSSAVYGLVKLAVE-KSRENFGFNALIGPVVK-LWHIGFK 108
Cdd:PTZ00306    91 VLRSAFQMVDTHLNSFNPN---SEVSRVNRmpVGEKH--QMSAHLKRVMACCQRvYNSSGGCFDPAAGPLVHeLREAARR 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711178106  109 GAHVPKD---EEIKDRMLLTDPFKVVLNDSdqSVFLKMKGMELDLGGIAKGWIADRIRDLWRAYGVEAGIINLGGNILLV 185
Cdd:PTZ00306   166 QKSVEAEfviEELAGRFTLTNSFAIDLEEG--TIARKHEDAMLDLGGVNKGYTVDYVVDRLNAAGFDDVLFEWGGDCRAS 243
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1711178106  186 GDSPKRisGQWSIGVQDP---------------KQPRGDNITSVMVPECSAV-TSGTYERYLVVNGKK 237
Cdd:PTZ00306   244 GVNVQR--QPWAVGIVRPpsvdevraaaksgksAPPDHKSLLRVMSLNNEALcTSGDYENVLEGPASK 309
 
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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