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Conserved domains on  [gi|537923854|ref|WP_020991251|]
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FAD:protein FMN transferase [Granulicatella elegans]

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 ...
11-303 4.78e-116

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


:

Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 335.96  E-value: 4.78e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854  11 MGASIHLTIFHED---AQNLLLQSEQLLHLYKNRFSANDADSELMEINLQAGKKAVQVHPELFELIELGKKHSIAANSHL 87
Cdd:COG1477    1 MGTTVSITLYGPDeaqAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854  88 NIAIGPLVQTWRIGFSDAKLPSEEEIQRLLKITDPEEIFLNDSNREVYLSKEGMRIDLGALAKGYIADKLKEFLVEQGVQ 167
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854 168 SGIIDLGGNILTIGENPTfHRPWRIGIQNPaLDRGEHVAVIEVSDGSVVTSGIYERQLVVDGKTYHHIFDRTTGYPMETE 247
Cdd:COG1477  161 NALVNLGGDIRALGTKPD-GRPWRVGIEDP-RDPGAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEHG 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 537923854 248 LASITIVAEKSVDCEIWTTRLFGQNPYDIIEEIEQQPGLEAFVITKNQKMMYTSGI 303
Cdd:COG1477  239 LASVTVIAPDAMLADALATALFVLGPEKGLALAERLPGLEALLIDRDGKVFASPGF 294
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
11-303 4.78e-116

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 335.96  E-value: 4.78e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854  11 MGASIHLTIFHED---AQNLLLQSEQLLHLYKNRFSANDADSELMEINLQAGKKAVQVHPELFELIELGKKHSIAANSHL 87
Cdd:COG1477    1 MGTTVSITLYGPDeaqAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854  88 NIAIGPLVQTWRIGFSDAKLPSEEEIQRLLKITDPEEIFLNDSNREVYLSKEGMRIDLGALAKGYIADKLKEFLVEQGVQ 167
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854 168 SGIIDLGGNILTIGENPTfHRPWRIGIQNPaLDRGEHVAVIEVSDGSVVTSGIYERQLVVDGKTYHHIFDRTTGYPMETE 247
Cdd:COG1477  161 NALVNLGGDIRALGTKPD-GRPWRVGIEDP-RDPGAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEHG 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 537923854 248 LASITIVAEKSVDCEIWTTRLFGQNPYDIIEEIEQQPGLEAFVITKNQKMMYTSGI 303
Cdd:COG1477  239 LASVTVIAPDAMLADALATALFVLGPEKGLALAERLPGLEALLIDRDGKVFASPGF 294
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
12-288 3.40e-75

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: 229.64  E-value: 3.40e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854   12 GASIHLTIFHED---AQNLLLQSEQLLHLYKNRFSANDADSELMEINlQAGKKAVQVHPELFELIELGKKHSIAANSHLN 88
Cdd:pfam02424   1 GTTVSITVYGPDeaaAEALEAAIDAELDRLEALLSTYRPDSELSRLN-RAGAGPVKVSPELFELLERALEISELSGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854   89 IAIGPLVqtwrigfsdaklpseeeiqrllkitdpeeiflndsnrevylskegmrIDLGALAKGYIADKLKEFLVEQGVQS 168
Cdd:pfam02424  80 ITVGPLV-----------------------------------------------LDLGGIAKGYAVDRAAELLKAKGVTS 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854  169 GIIDLGGNILTIGENPTfHRPWRIGIQNPalDRGEHVAVIEVSDGSVVTSGIYERQLvVDGKTYHHIFDRTTGYPMETEL 248
Cdd:pfam02424 113 ALVNLGGDIRALGTKPD-GSPWRVGIQDP--RDPDSLAVLELSDKAVATSGDYERYF-EDGKRYHHIIDPRTGYPVANGL 188
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 537923854  249 ASITIVAeKSVDCEIWTTRLFGQNPYDIIEEIEQQPGLEA 288
Cdd:pfam02424 189 ASVTVIA-DAMLADALATALFVLGPEKGLALLEKLPGLEA 227
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
25-293 1.02e-32

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 123.71  E-value: 1.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854  25 QNLLLQSEQLLHLYKNrfsandaDSELMEINLQAGKKAVQVHPELFELIELGKKHSIAANSHLNIAIGPLVQTWriGF-- 102
Cdd:PRK10461  66 QTQLDADDQLLSTYKK-------DSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLW--GFgp 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854 103 --SDAKLPSEEEIQRLLKITDPEEIFLNDSNREVYLSKE--GMRIDLGALAKGYIADKLKEFLVEQGVQSGIIDLGGNIL 178
Cdd:PRK10461 137 ekQPVQIPSQEQIDAAKAKTGLQHLTVINQSHQQYLQKDlpDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALS 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854 179 TIGENPTfHRPWRIGIQNPAlDRGEHV-AVIEVSDGSVVTSGIYERQLVVDGKTYHHIFDRTTGYPMETELASITIVAEK 257
Cdd:PRK10461 217 SRGMNGE-GQPWRVAIQKPT-DKENAVqAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPT 294
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 537923854 258 SVDCEIWTTRLFGQNPYDIIEEIEQQpGLEAFVITK 293
Cdd:PRK10461 295 ALEADGWDTGLMVLGPEKAKEVVRRE-GLAVYMITK 329
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
11-303 4.78e-116

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 335.96  E-value: 4.78e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854  11 MGASIHLTIFHED---AQNLLLQSEQLLHLYKNRFSANDADSELMEINLQAGKKAVQVHPELFELIELGKKHSIAANSHL 87
Cdd:COG1477    1 MGTTVSITLYGPDeaqAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854  88 NIAIGPLVQTWRIGFSDAKLPSEEEIQRLLKITDPEEIFLNDSNREVYLSKEGMRIDLGALAKGYIADKLKEFLVEQGVQ 167
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854 168 SGIIDLGGNILTIGENPTfHRPWRIGIQNPaLDRGEHVAVIEVSDGSVVTSGIYERQLVVDGKTYHHIFDRTTGYPMETE 247
Cdd:COG1477  161 NALVNLGGDIRALGTKPD-GRPWRVGIEDP-RDPGAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEHG 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 537923854 248 LASITIVAEKSVDCEIWTTRLFGQNPYDIIEEIEQQPGLEAFVITKNQKMMYTSGI 303
Cdd:COG1477  239 LASVTVIAPDAMLADALATALFVLGPEKGLALAERLPGLEALLIDRDGKVFASPGF 294
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
12-288 3.40e-75

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: 229.64  E-value: 3.40e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854   12 GASIHLTIFHED---AQNLLLQSEQLLHLYKNRFSANDADSELMEINlQAGKKAVQVHPELFELIELGKKHSIAANSHLN 88
Cdd:pfam02424   1 GTTVSITVYGPDeaaAEALEAAIDAELDRLEALLSTYRPDSELSRLN-RAGAGPVKVSPELFELLERALEISELSGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854   89 IAIGPLVqtwrigfsdaklpseeeiqrllkitdpeeiflndsnrevylskegmrIDLGALAKGYIADKLKEFLVEQGVQS 168
Cdd:pfam02424  80 ITVGPLV-----------------------------------------------LDLGGIAKGYAVDRAAELLKAKGVTS 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854  169 GIIDLGGNILTIGENPTfHRPWRIGIQNPalDRGEHVAVIEVSDGSVVTSGIYERQLvVDGKTYHHIFDRTTGYPMETEL 248
Cdd:pfam02424 113 ALVNLGGDIRALGTKPD-GSPWRVGIQDP--RDPDSLAVLELSDKAVATSGDYERYF-EDGKRYHHIIDPRTGYPVANGL 188
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 537923854  249 ASITIVAeKSVDCEIWTTRLFGQNPYDIIEEIEQQPGLEA 288
Cdd:pfam02424 189 ASVTVIA-DAMLADALATALFVLGPEKGLALLEKLPGLEA 227
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
25-293 1.02e-32

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 123.71  E-value: 1.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854  25 QNLLLQSEQLLHLYKNrfsandaDSELMEINLQAGKKAVQVHPELFELIELGKKHSIAANSHLNIAIGPLVQTWriGF-- 102
Cdd:PRK10461  66 QTQLDADDQLLSTYKK-------DSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNLW--GFgp 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854 103 --SDAKLPSEEEIQRLLKITDPEEIFLNDSNREVYLSKE--GMRIDLGALAKGYIADKLKEFLVEQGVQSGIIDLGGNIL 178
Cdd:PRK10461 137 ekQPVQIPSQEQIDAAKAKTGLQHLTVINQSHQQYLQKDlpDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALS 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854 179 TIGENPTfHRPWRIGIQNPAlDRGEHV-AVIEVSDGSVVTSGIYERQLVVDGKTYHHIFDRTTGYPMETELASITIVAEK 257
Cdd:PRK10461 217 SRGMNGE-GQPWRVAIQKPT-DKENAVqAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVTVIAPT 294
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 537923854 258 SVDCEIWTTRLFGQNPYDIIEEIEQQpGLEAFVITK 293
Cdd:PRK10461 295 ALEADGWDTGLMVLGPEKAKEVVRRE-GLAVYMITK 329
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
20-253 9.24e-13

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 68.65  E-value: 9.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854   20 FHEDAQNLLLQSEQLLHLYKNRFSANdadSELMEIN-LQAGKKAvQVHPELFELIELGKKHSIAANSHLNIAIGPLVQTW 98
Cdd:PTZ00306   84 ADAVAKEVLRSAFQMVDTHLNSFNPN---SEVSRVNrMPVGEKH-QMSAHLKRVMACCQRVYNSSGGCFDPAAGPLVHEL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854   99 RIGFSDAK-LPSEEEIQRLLKITDPEEIFLNDSNREVYLSK-EGMRIDLGALAKGYIADKLKEFLVEQGVQSGIIDLGGN 176
Cdd:PTZ00306  160 REAARRQKsVEAEFVIEELAGRFTLTNSFAIDLEEGTIARKhEDAMLDLGGVNKGYTVDYVVDRLNAAGFDDVLFEWGGD 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 537923854  177 ILTIGENPTfHRPWRIGI-QNPALDRGEHVA---------------VIEVSDGSVVTSGIYERQLVV-DGKTYHHIFD-- 237
Cdd:PTZ00306  240 CRASGVNVQ-RQPWAVGIvRPPSVDEVRAAAksgksappdhksllrVMSLNNEALCTSGDYENVLEGpASKVYSSTFDwk 318
                         250
                  ....*....|....*..
gi 537923854  238 -RTTGYPMETELASITI 253
Cdd:PTZ00306  319 rRSLLEPTESELAQVSV 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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