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A5DB51 (RISA_PICGU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 37. 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 attributes

Sequence length239 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil By similarity.

Catalytic activity

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

Pathway

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

Induction

Repressed by iron. Ref.1

Sequence similarities

Contains 2 lumazine-binding repeats.

Sequence caution

The sequence EDK36408.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionoxidoreductase activity

Inferred from electronic annotation. Source: InterPro

riboflavin synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 239239Riboflavin synthase
PRO_0000295039

Regions

Repeat1 – 105105Lumazine-binding 1
Repeat106 – 205100Lumazine-binding 2
Region89 – 935Lumazine binding Probable
Region189 – 1935Lumazine binding Probable

Sequences

Sequence LengthMass (Da)Tools
A5DB51 [UniParc].

Last modified February 10, 2009. Version 3.
Checksum: 64DA06FEFB2D59B2

FASTA23926,044
        10         20         30         40         50         60 
MFTGLVEHIG TVLQVTEKDT TASGGDGVSM VIGDCSKILE DVQLGDSICT NGVCLTVTEF 

        70         80         90        100        110        120 
DMARSQFKVG ISPETLRRSD LGELKPGSKV NLERAVKADV RMGGHVVQGH VDTIATIVNR 

       130        140        150        160        170        180 
RGDGNAINFT FKLRDSQYGK YIVEKGFIAI DGTSLTVTDV DHEQSEFSIS MVSYTQEKVI 

       190        200        210        220        230 
MPLKNSGDSV NIEVDLTGKL IEKQIELSLL SYIKDETSPL STLIGKLVEK KVDDVLKRN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF459790 Genomic DNA. Translation: AAL66353.2.
AY138984 Genomic DNA. Translation: AAN08875.2.
CH408155 Genomic DNA. Translation: EDK36408.2. Different initiation.
RefSeqXP_001487129.1. XM_001487079.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4929.A5DB51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5129626.
KEGGpgu:PGUG_00506.

Phylogenomic databases

eggNOGCOG0307.
KOK00793.
OrthoDBEOG793BMH.

Enzyme and pathway databases

UniPathwayUPA00275; UER00405.

Family and domain databases

Gene3D2.40.30.20. 2 hits.
InterProIPR023366. ATPase_asu-like.
IPR001783. Lumazine-bd.
IPR026017. Lumazine-bd_dom.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERPTHR21098. PTHR21098. 1 hit.
PfamPF00677. Lum_binding. 2 hits.
[Graphical view]
PIRSFPIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMSSF63380. SSF63380. 2 hits.
TIGRFAMsTIGR00187. ribE. 1 hit.
PROSITEPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRISA_PICGU
AccessionPrimary (citable) accession number: A5DB51
Secondary accession number(s): Q8X181
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: February 10, 2009
Last modified: November 13, 2013
This is version 37 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways