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Conserved domains on  [gi|487220057|gb|EOL37904|]
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thiamin biosynthesis ApbE [Enterococcus faecalis EnGen0362]

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 ...
10-302 6.45e-119

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


:

Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 343.67  E-value: 6.45e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057  10 MGTVIDVFV---DHEEPEKILEEVHQRLITYEQRFSANDSTSELMAVNQQAGQKPVNVHPELYQLIALGKKHSCDPASHL 86
Cdd:COG1477    1 MGTTVSITLygpDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057  87 NITIGPLVQTWRIGFKDARVPSEEEIKACLKKINPEKIHLNPLKQTVFLEEEGMKLDLGALAKGYIADLLIAYLKEVHVT 166
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057 167 SALINLGGNIVTLGPStHQNKKWRIGIRNPQESRETISlLVEVANQSVVTSGIYERSLTEAGRVYHHLLDPTTGYPLETE 246
Cdd:COG1477  161 NALVNLGGDIRALGTK-PDGRPWRVGIEDPRDPGAVLA-VLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEHG 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 487220057 247 MASITIISDASVDGEIWTTRLFGYPIPEALEILNQLDGIEGVIITQDQQILYSSGL 302
Cdd:COG1477  239 LASVTVIAPDAMLADALATALFVLGPEKGLALAERLPGLEALLIDRDGKVFASPGF 294
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
10-302 6.45e-119

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 343.67  E-value: 6.45e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057  10 MGTVIDVFV---DHEEPEKILEEVHQRLITYEQRFSANDSTSELMAVNQQAGQKPVNVHPELYQLIALGKKHSCDPASHL 86
Cdd:COG1477    1 MGTTVSITLygpDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057  87 NITIGPLVQTWRIGFKDARVPSEEEIKACLKKINPEKIHLNPLKQTVFLEEEGMKLDLGALAKGYIADLLIAYLKEVHVT 166
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057 167 SALINLGGNIVTLGPStHQNKKWRIGIRNPQESRETISlLVEVANQSVVTSGIYERSLTEAGRVYHHLLDPTTGYPLETE 246
Cdd:COG1477  161 NALVNLGGDIRALGTK-PDGRPWRVGIEDPRDPGAVLA-VLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEHG 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 487220057 247 MASITIISDASVDGEIWTTRLFGYPIPEALEILNQLDGIEGVIITQDQQILYSSGL 302
Cdd:COG1477  239 LASVTVIAPDAMLADALATALFVLGPEKGLALAERLPGLEALLIDRDGKVFASPGF 294
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
11-286 3.24e-74

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: 227.33  E-value: 3.24e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057   11 GTVIDVFVDHEEP---EKILEEVHQRLITYEQRFSANDSTSELMAVNQqAGQKPVNVHPELYQLIALGKKHSCDPASHLN 87
Cdd:pfam02424   1 GTTVSITVYGPDEaaaEALEAAIDAELDRLEALLSTYRPDSELSRLNR-AGAGPVKVSPELFELLERALEISELSGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057   88 ITIGPLVqtwrigfkdarvpseeeikaclkkinpekihlnplkqtvfleeegmkLDLGALAKGYIADLLIAYLKEVHVTS 167
Cdd:pfam02424  80 ITVGPLV-----------------------------------------------LDLGGIAKGYAVDRAAELLKAKGVTS 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057  168 ALINLGGNIVTLGPSThQNKKWRIGIRNPQEsrETISLLVEVANQSVVTSGIYERSLtEAGRVYHHLLDPTTGYPLETEM 247
Cdd:pfam02424 113 ALVNLGGDIRALGTKP-DGSPWRVGIQDPRD--PDSLAVLELSDKAVATSGDYERYF-EDGKRYHHIIDPRTGYPVANGL 188
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 487220057  248 ASITIISDaSVDGEIWTTRLFGYPIPEALEILNQLDGIE 286
Cdd:pfam02424 189 ASVTVIAD-AMLADALATALFVLGPEKGLALLEKLPGLE 226
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
10-267 2.82e-29

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 114.47  E-value: 2.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057  10 MGTVIDVFV---DHEEPEKILEEVHQRLITYEQRFSANDSTSELMAVNQQAGQKPVNVHPELYQLIALGKKHSCDPASHL 86
Cdd:PRK10461  42 MGTFWRVSIpgiDAKRSAELQEKIQTQLDADDQLLSTYKKDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAM 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057  87 NITIGPLVQTWriGF----KDARVPSEEEIKACLKKINPEKIHLNPLKQTVFLEEE--GMKLDLGALAKGYIADLLIAYL 160
Cdd:PRK10461 122 DITVGPLVNLW--GFgpekQPVQIPSQEQIDAAKAKTGLQHLTVINQSHQQYLQKDlpDLYVDLSTVGEGYAADHLARLM 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057 161 KEVHVTSALINLGGNIVTLGPSThQNKKWRIGIRNPQESRETISLLVEVANQSVVTSGIYERSLTEAGRVYHHLLDPTTG 240
Cdd:PRK10461 200 EQEGISRYLVSVGGALSSRGMNG-EGQPWRVAIQKPTDKENAVQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTG 278
                        250       260
                 ....*....|....*....|....*..
gi 487220057 241 YPLETEMASITIISDASVDGEIWTTRL 267
Cdd:PRK10461 279 RPIEHNLVSVTVIAPTALEADGWDTGL 305
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
10-302 6.45e-119

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 343.67  E-value: 6.45e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057  10 MGTVIDVFV---DHEEPEKILEEVHQRLITYEQRFSANDSTSELMAVNQQAGQKPVNVHPELYQLIALGKKHSCDPASHL 86
Cdd:COG1477    1 MGTTVSITLygpDEAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057  87 NITIGPLVQTWRIGFKDARVPSEEEIKACLKKINPEKIHLNPLKQTVFLEEEGMKLDLGALAKGYIADLLIAYLKEVHVT 166
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057 167 SALINLGGNIVTLGPStHQNKKWRIGIRNPQESRETISlLVEVANQSVVTSGIYERSLTEAGRVYHHLLDPTTGYPLETE 246
Cdd:COG1477  161 NALVNLGGDIRALGTK-PDGRPWRVGIEDPRDPGAVLA-VLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEHG 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 487220057 247 MASITIISDASVDGEIWTTRLFGYPIPEALEILNQLDGIEGVIITQDQQILYSSGL 302
Cdd:COG1477  239 LASVTVIAPDAMLADALATALFVLGPEKGLALAERLPGLEALLIDRDGKVFASPGF 294
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
11-286 3.24e-74

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: 227.33  E-value: 3.24e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057   11 GTVIDVFVDHEEP---EKILEEVHQRLITYEQRFSANDSTSELMAVNQqAGQKPVNVHPELYQLIALGKKHSCDPASHLN 87
Cdd:pfam02424   1 GTTVSITVYGPDEaaaEALEAAIDAELDRLEALLSTYRPDSELSRLNR-AGAGPVKVSPELFELLERALEISELSGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057   88 ITIGPLVqtwrigfkdarvpseeeikaclkkinpekihlnplkqtvfleeegmkLDLGALAKGYIADLLIAYLKEVHVTS 167
Cdd:pfam02424  80 ITVGPLV-----------------------------------------------LDLGGIAKGYAVDRAAELLKAKGVTS 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057  168 ALINLGGNIVTLGPSThQNKKWRIGIRNPQEsrETISLLVEVANQSVVTSGIYERSLtEAGRVYHHLLDPTTGYPLETEM 247
Cdd:pfam02424 113 ALVNLGGDIRALGTKP-DGSPWRVGIQDPRD--PDSLAVLELSDKAVATSGDYERYF-EDGKRYHHIIDPRTGYPVANGL 188
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 487220057  248 ASITIISDaSVDGEIWTTRLFGYPIPEALEILNQLDGIE 286
Cdd:pfam02424 189 ASVTVIAD-AMLADALATALFVLGPEKGLALLEKLPGLE 226
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
10-267 2.82e-29

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 114.47  E-value: 2.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057  10 MGTVIDVFV---DHEEPEKILEEVHQRLITYEQRFSANDSTSELMAVNQQAGQKPVNVHPELYQLIALGKKHSCDPASHL 86
Cdd:PRK10461  42 MGTFWRVSIpgiDAKRSAELQEKIQTQLDADDQLLSTYKKDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAM 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057  87 NITIGPLVQTWriGF----KDARVPSEEEIKACLKKINPEKIHLNPLKQTVFLEEE--GMKLDLGALAKGYIADLLIAYL 160
Cdd:PRK10461 122 DITVGPLVNLW--GFgpekQPVQIPSQEQIDAAKAKTGLQHLTVINQSHQQYLQKDlpDLYVDLSTVGEGYAADHLARLM 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057 161 KEVHVTSALINLGGNIVTLGPSThQNKKWRIGIRNPQESRETISLLVEVANQSVVTSGIYERSLTEAGRVYHHLLDPTTG 240
Cdd:PRK10461 200 EQEGISRYLVSVGGALSSRGMNG-EGQPWRVAIQKPTDKENAVQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTG 278
                        250       260
                 ....*....|....*....|....*..
gi 487220057 241 YPLETEMASITIISDASVDGEIWTTRL 267
Cdd:PRK10461 279 RPIEHNLVSVTVIAPTALEADGWDTGL 305
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
24-252 2.81e-08

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 55.17  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057   24 EKILEEVHQRLITYEQRFSANdstSELMAVNQQ-AGQKPVnVHPELYQLIALGKK--HSC----DPAShlnitiGPLVQT 96
Cdd:PTZ00306   89 KEVLRSAFQMVDTHLNSFNPN---SEVSRVNRMpVGEKHQ-MSAHLKRVMACCQRvyNSSggcfDPAA------GPLVHE 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057   97 WRIGFKD-ARVPSEEEIKACLKKIN-PEKIHLNPLKQTVFLEEEGMKLDLGALAKGYIADLLIAYLKEVHVTSALINLGG 174
Cdd:PTZ00306  159 LREAARRqKSVEAEFVIEELAGRFTlTNSFAIDLEEGTIARKHEDAMLDLGGVNKGYTVDYVVDRLNAAGFDDVLFEWGG 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487220057  175 NIVTLGpSTHQNKKWRIGI-----------------RNPQESRETISlLVEVANQSVVTSGIYERSL-TEAGRVYHHLLD 236
Cdd:PTZ00306  239 DCRASG-VNVQRQPWAVGIvrppsvdevraaaksgkSAPPDHKSLLR-VMSLNNEALCTSGDYENVLeGPASKVYSSTFD 316
                         250
                  ....*....|....*....
gi 487220057  237 PTTG---YPLETEMASITI 252
Cdd:PTZ00306  317 WKRRsllEPTESELAQVSV 335
 
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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