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Conserved domains on  [gi|810807116|emb|CNA22427|]
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thiamine biosynthesis lipoprotein [Streptococcus pneumoniae]

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 ...
11-304 4.05e-114

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


:

Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 331.34  E-value: 4.05e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116  11 MGTTITISLVD---EQADIFLQKSFDLLKELEYRFNANSQESELMEINYQAGVSPVTVHPDLFELISLGLEHSLALSSHL 87
Cdd:COG1477    1 MGTTVSITLYGpdeAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116  88 NISIGPLIQTWRIGFSDAKVAQPQEIESVLPLINPHGIELDSSTSTVFLKQKGMKIDLGCLAKGYSADKVAQFLRKEGVT 167
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116 168 SALINLGGNILTIGKNQarGDNPWQIGIQDPaNPRGNHLMTIPVVNKSVVTSGIYERHLTVDGQDYHHIFDSQTGYPVET 247
Cdd:COG1477  161 NALVNLGGDIRALGTKP--DGRPWRVGIEDP-RDPGAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEH 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 810807116 248 ELASLTIISDKSVDGEIWTTRLFGERPASILWQVESLEGIEVILIDKEGHLSCSSGI 304
Cdd:COG1477  238 GLASVTVIAPDAMLADALATALFVLGPEKGLALAERLPGLEALLIDRDGKVFASPGF 294
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
11-304 4.05e-114

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 331.34  E-value: 4.05e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116  11 MGTTITISLVD---EQADIFLQKSFDLLKELEYRFNANSQESELMEINYQAGVSPVTVHPDLFELISLGLEHSLALSSHL 87
Cdd:COG1477    1 MGTTVSITLYGpdeAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116  88 NISIGPLIQTWRIGFSDAKVAQPQEIESVLPLINPHGIELDSSTSTVFLKQKGMKIDLGCLAKGYSADKVAQFLRKEGVT 167
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116 168 SALINLGGNILTIGKNQarGDNPWQIGIQDPaNPRGNHLMTIPVVNKSVVTSGIYERHLTVDGQDYHHIFDSQTGYPVET 247
Cdd:COG1477  161 NALVNLGGDIRALGTKP--DGRPWRVGIEDP-RDPGAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEH 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 810807116 248 ELASLTIISDKSVDGEIWTTRLFGERPASILWQVESLEGIEVILIDKEGHLSCSSGI 304
Cdd:COG1477  238 GLASVTVIAPDAMLADALATALFVLGPEKGLALAERLPGLEALLIDRDGKVFASPGF 294
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
12-289 7.47e-73

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: 223.86  E-value: 7.47e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116   12 GTTITISLVDE---QADIFLQKSFDLLKELEYRFNANSQESELMEINyQAGVSPVTVHPDLFELISLGLEHSLALSSHLN 88
Cdd:pfam02424   1 GTTVSITVYGPdeaAAEALEAAIDAELDRLEALLSTYRPDSELSRLN-RAGAGPVKVSPELFELLERALEISELSGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116   89 ISIGPLIqtwrigfsdakvaqpqeiesvlplinphgieldsststvflkqkgmkIDLGCLAKGYSADKVAQFLRKEGVTS 168
Cdd:pfam02424  80 ITVGPLV-----------------------------------------------LDLGGIAKGYAVDRAAELLKAKGVTS 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116  169 ALINLGGNILTIGKNQarGDNPWQIGIQDPANPRGnhLMTIPVVNKSVVTSGIYERHLTvDGQDYHHIFDSQTGYPVETE 248
Cdd:pfam02424 113 ALVNLGGDIRALGTKP--DGSPWRVGIQDPRDPDS--LAVLELSDKAVATSGDYERYFE-DGKRYHHIIDPRTGYPVANG 187
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 810807116  249 LASLTIISDkSVDGEIWTTRLFGERPASILWQVESLEGIEV 289
Cdd:pfam02424 188 LASVTVIAD-AMLADALATALFVLGPEKGLALLEKLPGLEA 227
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
11-297 7.56e-33

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 124.10  E-value: 7.56e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116  11 MGTTITISLVDEQAdiflQKSFDLLKELEYRFNANSQE-------SELMEINYQAGVSPVTVHPDLFELISLGLEHSLAL 83
Cdd:PRK10461  42 MGTFWRVSIPGIDA----KRSAELQEKIQTQLDADDQLlstykkdSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKT 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116  84 SSHLNISIGPLIQTWriGFSDAKvaQP------QEIESVLPLINPHGIELDSSTSTVFLkQK---GMKIDLGCLAKGYSA 154
Cdd:PRK10461 118 DGAMDITVGPLVNLW--GFGPEK--QPvqipsqEQIDAAKAKTGLQHLTVINQSHQQYL-QKdlpDLYVDLSTVGEGYAA 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116 155 DKVAQFLRKEGVTSALINLGGNILTIGKNqARGdNPWQIGIQDPANpRGNHLMTIPVVN-KSVVTSGIYERHLTVDGQDY 233
Cdd:PRK10461 193 DHLARLMEQEGISRYLVSVGGALSSRGMN-GEG-QPWRVAIQKPTD-KENAVQAVVDINgHGISTSGSYRNYYELDGKRL 269
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 810807116 234 HHIFDSQTGYPVETELASLTIISDKSVDGEIWTTRL--FGERPASilwQVESLEGIEVILIDKEGH 297
Cdd:PRK10461 270 SHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLmvLGPEKAK---EVVRREGLAVYMITKEGD 332
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
11-304 4.05e-114

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


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 331.34  E-value: 4.05e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116  11 MGTTITISLVD---EQADIFLQKSFDLLKELEYRFNANSQESELMEINYQAGVSPVTVHPDLFELISLGLEHSLALSSHL 87
Cdd:COG1477    1 MGTTVSITLYGpdeAQAEAALAAAFAELDRLEALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116  88 NISIGPLIQTWRIGFSDAKVAQPQEIESVLPLINPHGIELDSSTSTVFLKQKGMKIDLGCLAKGYSADKVAQFLRKEGVT 167
Cdd:COG1477   81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116 168 SALINLGGNILTIGKNQarGDNPWQIGIQDPaNPRGNHLMTIPVVNKSVVTSGIYERHLTVDGQDYHHIFDSQTGYPVET 247
Cdd:COG1477  161 NALVNLGGDIRALGTKP--DGRPWRVGIEDP-RDPGAVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEH 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 810807116 248 ELASLTIISDKSVDGEIWTTRLFGERPASILWQVESLEGIEVILIDKEGHLSCSSGI 304
Cdd:COG1477  238 GLASVTVIAPDAMLADALATALFVLGPEKGLALAERLPGLEALLIDRDGKVFASPGF 294
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
12-289 7.47e-73

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: 223.86  E-value: 7.47e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116   12 GTTITISLVDE---QADIFLQKSFDLLKELEYRFNANSQESELMEINyQAGVSPVTVHPDLFELISLGLEHSLALSSHLN 88
Cdd:pfam02424   1 GTTVSITVYGPdeaAAEALEAAIDAELDRLEALLSTYRPDSELSRLN-RAGAGPVKVSPELFELLERALEISELSGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116   89 ISIGPLIqtwrigfsdakvaqpqeiesvlplinphgieldsststvflkqkgmkIDLGCLAKGYSADKVAQFLRKEGVTS 168
Cdd:pfam02424  80 ITVGPLV-----------------------------------------------LDLGGIAKGYAVDRAAELLKAKGVTS 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116  169 ALINLGGNILTIGKNQarGDNPWQIGIQDPANPRGnhLMTIPVVNKSVVTSGIYERHLTvDGQDYHHIFDSQTGYPVETE 248
Cdd:pfam02424 113 ALVNLGGDIRALGTKP--DGSPWRVGIQDPRDPDS--LAVLELSDKAVATSGDYERYFE-DGKRYHHIIDPRTGYPVANG 187
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 810807116  249 LASLTIISDkSVDGEIWTTRLFGERPASILWQVESLEGIEV 289
Cdd:pfam02424 188 LASVTVIAD-AMLADALATALFVLGPEKGLALLEKLPGLEA 227
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
11-297 7.56e-33

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 124.10  E-value: 7.56e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116  11 MGTTITISLVDEQAdiflQKSFDLLKELEYRFNANSQE-------SELMEINYQAGVSPVTVHPDLFELISLGLEHSLAL 83
Cdd:PRK10461  42 MGTFWRVSIPGIDA----KRSAELQEKIQTQLDADDQLlstykkdSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKT 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116  84 SSHLNISIGPLIQTWriGFSDAKvaQP------QEIESVLPLINPHGIELDSSTSTVFLkQK---GMKIDLGCLAKGYSA 154
Cdd:PRK10461 118 DGAMDITVGPLVNLW--GFGPEK--QPvqipsqEQIDAAKAKTGLQHLTVINQSHQQYL-QKdlpDLYVDLSTVGEGYAA 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116 155 DKVAQFLRKEGVTSALINLGGNILTIGKNqARGdNPWQIGIQDPANpRGNHLMTIPVVN-KSVVTSGIYERHLTVDGQDY 233
Cdd:PRK10461 193 DHLARLMEQEGISRYLVSVGGALSSRGMN-GEG-QPWRVAIQKPTD-KENAVQAVVDINgHGISTSGSYRNYYELDGKRL 269
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 810807116 234 HHIFDSQTGYPVETELASLTIISDKSVDGEIWTTRL--FGERPASilwQVESLEGIEVILIDKEGH 297
Cdd:PRK10461 270 SHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLmvLGPEKAK---EVVRREGLAVYMITKEGD 332
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
21-254 2.88e-11

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 64.03  E-value: 2.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116   21 DEQADIFLQKSFDLLKELEYRFNANSQESelmeinyQAGVSPV----TVHPDLFELISLGLEHSLALSSHLNISIGPLIQ 96
Cdd:PTZ00306   85 DAVAKEVLRSAFQMVDTHLNSFNPNSEVS-------RVNRMPVgekhQMSAHLKRVMACCQRVYNSSGGCFDPAAGPLVH 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116   97 TWRIGFSDAK-VAQPQEIESVLPLIN-PHGIELDSSTSTVFLKQKGMKIDLGCLAKGYSADKVAQFLRKEGVTSALINLG 174
Cdd:PTZ00306  158 ELREAARRQKsVEAEFVIEELAGRFTlTNSFAIDLEEGTIARKHEDAMLDLGGVNKGYTVDYVVDRLNAAGFDDVLFEWG 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 810807116  175 GNILTIGKNQARgdNPWQIGIQDP--------------ANPRG--NHLMTIPVVNKSVVTSGIYERHL-TVDGQDYHHIF 237
Cdd:PTZ00306  238 GDCRASGVNVQR--QPWAVGIVRPpsvdevraaaksgkSAPPDhkSLLRVMSLNNEALCTSGDYENVLeGPASKVYSSTF 315
                         250       260
                  ....*....|....*....|
gi 810807116  238 DSQTG---YPVETELASLTI 254
Cdd:PTZ00306  316 DWKRRsllEPTESELAQVSV 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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