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Q9A9S4 (RISB1_CAUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6,7-dimethyl-8-ribityllumazine synthase 1

Short name=DMRL synthase 1
Short name=Lumazine synthase 1
EC=2.5.1.9
Alternative name(s):
Riboflavin synthase 1 beta chain
Gene names
Name:ribH1
Ordered Locus Names:CC_0888
OrganismCaulobacter crescentus (Caulobacter vibrioides)
Taxonomic identifier155892 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length153 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
Reference 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 – 1531536,7-dimethyl-8-ribityllumazine synthase 1 HAMAP MF_00178
PRO_0000134735

Sequences

Sequence LengthMass (Da)Tools
Q9A9S4 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: A627F438886735CB

FASTA15315,959
        10         20         30         40         50         60 
MTDPVPPRIA IVVSQFNPEV TDGLLKGALD HLAAQGAPVA APDIIAAPGA YELPLIAQTL 

        70         80         90        100        110        120 
ARTGRYAGVV CLGCVIKGET AHFEFISLGA SLGLMAAGLQ TETPVSFGVL TTYTDEQAVA 

       130        140        150 
RSRDDAENKG REAANACLST VQTLRRIREN ALA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005673 Genomic DNA. Translation: AAK22873.1.
PIRE87359.
RefSeqNP_419705.1. NC_002696.2.

3D structure databases

ProteinModelPortalQ9A9S4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID941137.
GenomeReviewsGene locus CC_0888 in contig AE005673_GR.
KEGGccr:CC_0888.
NMPDRfig|190650.1.peg.885.
PATRIC21298734. VBICauCre124313_0901.
TIGRCC_0888.

Phylogenomic databases

HOGENOMHBG311126.
OMAAGECSSG.
ProtClustDBCLSK890126.

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 nameRISB1_CAUCR
AccessionPrimary (citable) accession number: Q9A9S4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 63 of the entry and version 1 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