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Reviewed, UniProtKB/Swiss-Prot P57212 (RISA_BUCAI)

Last modified November 3, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Riboflavin synthase alpha chain
    EC=2.5.1.9
Gene names
Name: ribE
Ordered Locus Names: BU112
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]
Taxonomic identifier118099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 alpha subunit catalyzes the dismutation of 6,7-dimethyl-8-lumazine to riboflavin and 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione 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; 5-amino-6-(D-ribitylamino)uracil and riboflavin from 6,7-dimethyl-8-(1-D-ribityl)lumazine: step 1/1.

Subunit structure

Oligomer that consist of 3 alpha subunits and 60 beta subunits By similarity.

Sequence similarities

Contains 2 lumazine-binding repeats.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 208208Riboflavin synthase alpha chain
PRO_0000068160

Regions

Repeat1 – 9797Lumazine-binding 1
Repeat98 – 19598Lumazine-binding 2

Sequences

Sequence LengthMass (Da)Tools
P57212-1 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 7CCE3272CF54BA5B

FASTA20823,505
        10         20         30         40         50         60 
MFTGIINGTA TIVYIEKKKK KYRYTVELPS NLSKNLKLGD SISHNGCCLT VKLINNSFII 

        70         80         90        100        110        120 
CDVIQETLKS TNLGILNIGD SINIERSIKY GDEIGGHIIS GHVMNTAEIS KMSKSDNNCV 

       130        140        150        160        170        180 
IWLKMNNMSL MKYIFYKGFI CVDGISLTVN DIIKNEFCVN IIPYTFLFTT IKDKKNGSLV 

       190        200 
NIEIDFYTQT IVDTTERLIN NNLKSLYD 

« Hide

References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed: 10993077] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tokyo 1998.

Cross-references

Sequence databases

BA000003 Genomic DNA. Translation: BAB12830.1.
RefSeqNP_239944.1.

3D structure databases

HSSPHSSP built from PDB template 1I8D based on UniProtKB P29015.
ModBaseSearch...

Genome annotation databases

GeneID1109556.
GenomeReviewsGene locus BU112 in contig BA000003_GR.
KEGGbuc:BU112.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP57212.
OMACLTVTKI.

Enzyme and pathway databases

BioCycBSP107806:BU112-MON.

Family and domain databases

InterProIPR001783. Lumazine_bd.
[Graphical view]
PANTHERPTHR21098. Lumazine_bd. 1 hit.
PfamPF00677. Lum_binding. 2 hits.
[Graphical view]
PIRSFPIRSF000498. Riboflavin_syn_A. 1 hit.
ProDomPD004110. Lum_binding. 2 hits.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00187. ribE. 1 hit.
PROSITEPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRISA_BUCAI
AccessionPrimary (citable) accession number: P57212
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents