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Q9REF4 (RISB_BARHE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:ribE
Ordered Locus Names:BH07580
OrganismBartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea henselae) [Complete proteome] [HAMAP]
Taxonomic identifier283166 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length155 AA.
Sequence statusComplete.
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. HAMAP MF_00178

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; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2. 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: UniProtKB-KW

   Cellular componentriboflavin synthase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionriboflavin synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1551556,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178
PRO_0000134717

Experimental info

Sequence conflict951L → S in CAB63092. Ref.1
Sequence conflict1261D → A in CAB63092. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9REF4 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: 26590561428BC2AE

FASTA15516,953
        10         20         30         40         50         60 
MTIEICKKLH VLIVEARFYD GISDALLTGA VSTLQKAEAT YDIVTVPGAL EIPGAIAFAE 

        70         80         90        100        110        120 
KNSKIYYDGY VALGCVIRGE TYHFEIVAND SCRALMDLTI HKHLAIGNGI LTVENEKQAW 

       130        140        150 
ARAKQDEKNK GGFAAQAALC MIALKKRFGE IIKYG 

« Hide

References

« Hide 'large scale' references
[1]"Molecular analysis of riboflavin synthesis genes in Bartonella henselae and use of the ribC gene for differentiation of Bartonella species by PCR."
Bereswill S., Hinkelmann S., Kist M., Sander A.
J. Clin. Microbiol. 37:3159-3166(1999) [PubMed: 10488170] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 49882 / Houston 1.
[2]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49882 / Houston 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ132928 Genomic DNA. Translation: CAB63092.1.
BX897699 Genomic DNA. Translation: CAF27559.1.
RefSeqYP_033570.1. NC_005956.1.

3D structure databases

ProteinModelPortalQ9REF4.
SMRQ9REF4. Positions 10-149.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2864803.
GenomeReviewsGene locus BH07580 in contig BX897699_GR.
KEGGbhe:BH07580.
NMPDRfig|283166.1.peg.698.
PATRIC20545332. VBIBarHen29080_0811.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG311126.
OMASSRALMD.
PhylomeDBQ9REF4.
ProtClustDBPRK00061.

Enzyme and pathway databases

BioCycBHEN283166:BH07580-MONOMER.

Family and domain databases

HAMAPMF_00178. Lumazine_synth.
[Tree]
InterProIPR002180. DMRL_synthase.
[Graphical view]
Gene3DG3DSA:3.40.50.960. DMRL_synthase. 1 hit.
KOK00794.
PANTHERPTHR21058. DMRL_synthase. 1 hit.
PfamPF00885. DMRL_synthase. 1 hit.
[Graphical view]
SUPFAMSSF52121. DMRL_synthase. 1 hit.
TIGRFAMsTIGR00114. Lumazine-synth. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRISB_BARHE
AccessionPrimary (citable) accession number: Q9REF4
Secondary accession number(s): Q6G3K9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: August 31, 2004
Last modified: January 25, 2012
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families