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O28152 (RISB_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 69. 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:AF_2128
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length143 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 – 1431436,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178
PRO_0000134840

Sequences

Sequence LengthMass (Da)Tools
O28152 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: BBA3141206905410

FASTA14315,645
        10         20         30         40         50         60 
MEKVKLGMVV AEFNRDITYM MEILGKEHAE FLGAEVSEVI RVPGTFDIPI AVKKMLEKGR 

        70         80         90        100        110        120 
VDAVVAIGCV IEGETEHDEI VAQHAARKIM DLSLEYGKPV TLGISGPGMG RIAATERVDY 

       130        140 
AKRAVEAAVK LVKRLKEYDA EGS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000782 Genomic DNA. Translation: AAB89124.1.
PIRH69515.
RefSeqNP_070953.1. NC_000917.1.

3D structure databases

ProteinModelPortalO28152.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1485357.
GenomeReviewsGene locus AF_2128 in contig AE000782_GR.
KEGGafu:AF2128.
NMPDRfig|224325.1.peg.2114.
TIGRAF_2128.

Phylogenomic databases

HOGENOMHBG311126.
OMAIQGATKH.
PhylomeDBO28152.
ProtClustDBPRK00061.

Enzyme and pathway databases

BioCycAFUL224325:AF_2128-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_ARCFU
AccessionPrimary (citable) accession number: O28152
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: December 14, 2011
This is version 69 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