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Conserved domains on  [gi|511487052|gb|EPD12065|]
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Thiamine biosynthesis lipoprotein [Lacticaseibacillus paracasei subsp. paracasei Lpp48]

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 ...
12-302 9.13e-84

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


:

Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 253.92  E-value: 9.13e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052  12 LGTNIVLSVFG---EQDNSALVAAELLIRQQESRLTVNQPHSEIMTINQLAGYDNTEISSGTYALIKNAVLASQK-HFGF 87
Cdd:COG1477    1 MGTTVSITLYGpdeAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELsDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052  88 NALIGPLVKLWKIGFNGANVPSDHDIKSRLLLSNPDNIIMDDALHTVKLVKTGMELDLGGIAKGFIADQIRSIWFAYGIR 167
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052 168 AGIINLGGNLLFVGESPrrsDGR-WIVGIQDPNKGRNIgIGTVIKPACAAVTSGIYERFLIKGGKRYHHLLDPQTGYPLQ 246
Cdd:COG1477  161 NALVNLGGDIRALGTKP---DGRpWRVGIEDPRDPGAV-LAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVE 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 511487052 247 TQLAAVTVFTRDSLQGELEAKRLFFAG-KPIPGWEKDPNNLGAVFIYQNGNTQTVKA 302
Cdd:COG1477  237 HGLASVTVIAPDAMLADALATALFVLGpEKGLALAERLPGLEALLIDRDGKVFASPG 293
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
12-302 9.13e-84

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 253.92  E-value: 9.13e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052  12 LGTNIVLSVFG---EQDNSALVAAELLIRQQESRLTVNQPHSEIMTINQLAGYDNTEISSGTYALIKNAVLASQK-HFGF 87
Cdd:COG1477    1 MGTTVSITLYGpdeAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELsDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052  88 NALIGPLVKLWKIGFNGANVPSDHDIKSRLLLSNPDNIIMDDALHTVKLVKTGMELDLGGIAKGFIADQIRSIWFAYGIR 167
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052 168 AGIINLGGNLLFVGESPrrsDGR-WIVGIQDPNKGRNIgIGTVIKPACAAVTSGIYERFLIKGGKRYHHLLDPQTGYPLQ 246
Cdd:COG1477  161 NALVNLGGDIRALGTKP---DGRpWRVGIEDPRDPGAV-LAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVE 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 511487052 247 TQLAAVTVFTRDSLQGELEAKRLFFAG-KPIPGWEKDPNNLGAVFIYQNGNTQTVKA 302
Cdd:COG1477  237 HGLASVTVIAPDAMLADALATALFVLGpEKGLALAERLPGLEALLIDRDGKVFASPG 293
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
13-273 1.09e-52

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: 172.25  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052   13 GTNIVLSVFGEQDNSALVAAEL---LIRQQESRLTVNQPHSEIMTINQlAGYDNTEISSGTYALIKNAVLASQK-HFGFN 88
Cdd:pfam02424   1 GTTVSITVYGPDEAAAEALEAAidaELDRLEALLSTYRPDSELSRLNR-AGAGPVKVSPELFELLERALEISELsGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052   89 ALIGPLVklwkigfnganvpsdhdiksrlllsnpdniimddalhtvklvktgmeLDLGGIAKGFIADQIRSIWFAYGIRA 168
Cdd:pfam02424  80 ITVGPLV-----------------------------------------------LDLGGIAKGYAVDRAAELLKAKGVTS 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052  169 GIINLGGNLLFVGESPrrsDGR-WIVGIQDPNKGRNIGigtVIKPACAAV-TSGIYERFLIKgGKRYHHLLDPQTGYPLQ 246
Cdd:pfam02424 113 ALVNLGGDIRALGTKP---DGSpWRVGIQDPRDPDSLA---VLELSDKAVaTSGDYERYFED-GKRYHHIIDPRTGYPVA 185
                         250       260
                  ....*....|....*....|....*..
gi 511487052  247 TQLAAVTVFTrDSLQGELEAKRLFFAG 273
Cdd:pfam02424 186 NGLASVTVIA-DAMLADALATALFVLG 211
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
50-261 1.10e-13

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 70.55  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052  50 SEIMTINQLAGYDNTEISSGTYALIKNAVLASQKHFG-FNALIGPLVKLWkiGFNGANVPsdhdiksrllLSNPDNIIMD 128
Cdd:PRK10461  83 SALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGaMDITVGPLVNLW--GFGPEKQP----------VQIPSQEQID 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052 129 DA-----LHTVKLVKT-----------GMELDLGGIAKGFIADQIRSIWFAYGIRAGIINLGGNLLFVGESPrrSDGRWI 192
Cdd:PRK10461 151 AAkaktgLQHLTVINQshqqylqkdlpDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNG--EGQPWR 228
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511487052 193 VGIQDPNKGRNIGIGTVIKPACAAVTSGIYERFLIKGGKRYHHLLDPQTGYPLQTQLAAVTVFTRDSLQ 261
Cdd:PRK10461 229 VAIQKPTDKENAVQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALE 297
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
12-302 9.13e-84

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 253.92  E-value: 9.13e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052  12 LGTNIVLSVFG---EQDNSALVAAELLIRQQESRLTVNQPHSEIMTINQLAGYDNTEISSGTYALIKNAVLASQK-HFGF 87
Cdd:COG1477    1 MGTTVSITLYGpdeAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELsDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052  88 NALIGPLVKLWKIGFNGANVPSDHDIKSRLLLSNPDNIIMDDALHTVKLVKTGMELDLGGIAKGFIADQIRSIWFAYGIR 167
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052 168 AGIINLGGNLLFVGESPrrsDGR-WIVGIQDPNKGRNIgIGTVIKPACAAVTSGIYERFLIKGGKRYHHLLDPQTGYPLQ 246
Cdd:COG1477  161 NALVNLGGDIRALGTKP---DGRpWRVGIEDPRDPGAV-LAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVE 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 511487052 247 TQLAAVTVFTRDSLQGELEAKRLFFAG-KPIPGWEKDPNNLGAVFIYQNGNTQTVKA 302
Cdd:COG1477  237 HGLASVTVIAPDAMLADALATALFVLGpEKGLALAERLPGLEALLIDRDGKVFASPG 293
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
13-273 1.09e-52

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: 172.25  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052   13 GTNIVLSVFGEQDNSALVAAEL---LIRQQESRLTVNQPHSEIMTINQlAGYDNTEISSGTYALIKNAVLASQK-HFGFN 88
Cdd:pfam02424   1 GTTVSITVYGPDEAAAEALEAAidaELDRLEALLSTYRPDSELSRLNR-AGAGPVKVSPELFELLERALEISELsGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052   89 ALIGPLVklwkigfnganvpsdhdiksrlllsnpdniimddalhtvklvktgmeLDLGGIAKGFIADQIRSIWFAYGIRA 168
Cdd:pfam02424  80 ITVGPLV-----------------------------------------------LDLGGIAKGYAVDRAAELLKAKGVTS 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052  169 GIINLGGNLLFVGESPrrsDGR-WIVGIQDPNKGRNIGigtVIKPACAAV-TSGIYERFLIKgGKRYHHLLDPQTGYPLQ 246
Cdd:pfam02424 113 ALVNLGGDIRALGTKP---DGSpWRVGIQDPRDPDSLA---VLELSDKAVaTSGDYERYFED-GKRYHHIIDPRTGYPVA 185
                         250       260
                  ....*....|....*....|....*..
gi 511487052  247 TQLAAVTVFTrDSLQGELEAKRLFFAG 273
Cdd:pfam02424 186 NGLASVTVIA-DAMLADALATALFVLG 211
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
50-261 1.10e-13

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 70.55  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052  50 SEIMTINQLAGYDNTEISSGTYALIKNAVLASQKHFG-FNALIGPLVKLWkiGFNGANVPsdhdiksrllLSNPDNIIMD 128
Cdd:PRK10461  83 SALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGaMDITVGPLVNLW--GFGPEKQP----------VQIPSQEQID 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052 129 DA-----LHTVKLVKT-----------GMELDLGGIAKGFIADQIRSIWFAYGIRAGIINLGGNLLFVGESPrrSDGRWI 192
Cdd:PRK10461 151 AAkaktgLQHLTVINQshqqylqkdlpDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNG--EGQPWR 228
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511487052 193 VGIQDPNKGRNIGIGTVIKPACAAVTSGIYERFLIKGGKRYHHLLDPQTGYPLQTQLAAVTVFTRDSLQ 261
Cdd:PRK10461 229 VAIQKPTDKENAVQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPTALE 297
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
48-198 3.78e-03

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 38.99  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052   48 PHSEIMTINQLAGYDNTEISsgtyALIKNAVLASQKHF-----GFNALIGPLVK-LWKIGFNGANVPSD---HDIKSRLL 118
Cdd:PTZ00306  108 PNSEVSRVNRMPVGEKHQMS----AHLKRVMACCQRVYnssggCFDPAAGPLVHeLREAARRQKSVEAEfviEELAGRFT 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511487052  119 LSNPDNIIMDDAlhTVKLVKTGMELDLGGIAKGFIADQIRSIWFAYGIRAGIINLGGNLLFVGESPRRSDgrWIVGIQDP 198
Cdd:PTZ00306  184 LTNSFAIDLEEG--TIARKHEDAMLDLGGVNKGYTVDYVVDRLNAAGFDDVLFEWGGDCRASGVNVQRQP--WAVGIVRP 259
 
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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