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Q975M5 (RISB_SULTO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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
Ordered Locus Names:STK_03940
OrganismSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) [Complete proteome] [HAMAP]
Taxonomic identifier273063 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

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: 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 – 1551556,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178
PRO_0000134854

Sequences

Sequence LengthMass (Da)Tools
Q975M5 [UniParc].

Last modified December 14, 2011. Version 2.
Checksum: 9B005BE2D94973C7

FASTA15517,242
        10         20         30         40         50         60 
MPDQSINLAI VVAEFNYDIT YLMLQRAIAH AKFLGANVKV VFKVPGSYDM AIAVKELLKR 

        70         80         90        100        110        120 
DDIDAVVTLG AVIKGETKHD EIVATQTARK ILDLSVEYGK PVTLGIIGHG VTHEQAVERI 

       130        140        150 
EEYSTRAVEA AIKLAKRLRE LRKIQTLNEE MVVIE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000023 Genomic DNA. Translation: BAK54262.1.

3D structure databases

ProteinModelPortalQ975M5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GenomeReviewsGene locus ST0394 in contig BA000023_GR.
KEGGsto:ST0394.
NMPDRfig|273063.1.peg.434.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG311126.
OMAIQGATKH.
PhylomeDBQ975M5.
ProtClustDBPRK00061.

Enzyme and pathway databases

BioCycSTOK273063:ST0394-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_SULTO
AccessionPrimary (citable) accession number: Q975M5
Secondary accession number(s): F9VMW5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: December 14, 2011
Last modified: January 25, 2012
This is version 53 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