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Reviewed, UniProtKB/Swiss-Prot Q81MB5 (RISB_BACAN)

Last modified November 3, 2009. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    6,7-dimethyl-8-ribityllumazine synthase
      Short name=DMRL synthase
      Short name=Lumazine synthase
    EC=2.5.1.9
Alternative name(s):
    Riboflavin synthase beta chain
Gene names
Name: ribH
Ordered Locus Names: BA_4334, GBAA_4334, BAS4021
OrganismBacillus anthracis [Complete proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Riboflavin synthase is a bifunctional enzyme complex catalyzing the formation of riboflavin from 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydrohy-2-butanone-4-phosphate via 6,7-dimethyl-8-lumazine. The beta subunit catalyzes the condensation of 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4-phosphate yielding 6,7-dimethyl-8-lumazine By similarity.

Catalytic activity

2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine. HAMAP MF_00178

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil and riboflavin from 6,7-dimethyl-8-(1-D-ribityl)lumazine: step 1/1. HAMAP MF_00178

Sequence similarities

Belongs to the DMRL synthase family.

Ontologies

Keywords
   Biological processRiboflavin biosynthesis
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processriboflavin biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentriboflavin synthase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionriboflavin synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1531536,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178
PRO_0000134710

Sequences

Sequence LengthMass (Da)Tools
Q81MB5-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: AA5391784EA66839

FASTA15316,255
        10         20         30         40         50         60 
MVFEGHLVGT GLKVGVVVGR FNEFITSKLL GGALDGLKRH GVEENDIDVA WVPGAFEIPL 

        70         80         90        100        110        120 
IAKKMANSGK YDAVITLGTV IRGATTHYDY VCNEVAKGVA SLSLQTDIPV IFGVLTTETI 

       130        140        150 
EQAIERAGTK AGNKGYESAV AAIEMAHLSK HWA 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

AE016879 Genomic DNA. Translation: AAP28053.1.
AE017334 Genomic DNA. Translation: AAT33455.1.
AE017225 Genomic DNA. Translation: AAT56322.1.
RefSeqNP_846567.1.
YP_020980.1.
YP_030271.1.

3D structure databases

HSSPHSSP built from PDB template 1RVV based on UniProtKB P11998.
SMRQ81MB5. Positions 2-152.
ModBaseSearch...

Genome annotation databases

GeneID1087551.
2815209.
2850962.
GenomeReviewsGene locus BA_4334 in contig AE016879_GR.
Gene locus BAS4021 in contig AE017225_GR.
Gene locus GBAA_4334 in contig AE017334_GR.
KEGGban:BA4334.
bar:GBAA4334.
bat:BAS4021.
TIGRBA_4334.
GBAA_4334.

Phylogenomic databases

HOGENOMQ81MB5.
OMALTTDTMQ.

Enzyme and pathway databases

BioCycBANT260799:BAS4021-MON.
BANT261594:GBAA4334-MON.
BRENDA2.5.1.9. 267517.

Family and domain databases

HAMAPMF_00178.
[Tree]
InterProIPR002180. DMRL_synthase.
[Graphical view]
Gene3DG3DSA:3.40.50.960. DMRL_synthase. 1 hit.
PANTHERPTHR21058. DMRL_synthase. 1 hit.
PfamPF00885. DMRL_synthase. 1 hit.
[Graphical view]
ProDomPD003664. DMRL_synthase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00114. lumazine-synth. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRISB_BACAN
AccessionPrimary (citable) accession number: Q81MB5
Secondary accession number(s): Q6HTR7, Q6KN05
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents