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Reviewed, UniProtKB/Swiss-Prot P51961 (RISA_PHOPO)

Last modified September 22, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismPhotobacterium phosphoreum
Taxonomic identifier659 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

Protein attributes

Sequence length218 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.

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
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 – 218218Riboflavin synthase alpha chain
PRO_0000068171

Regions

Repeat1 – 9797Lumazine-binding 1
Repeat98 – 19497Lumazine-binding 2

Sequences

Sequence LengthMass (Da)Tools
P51961-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 309B197A71430975

FASTA21823,639
        10         20         30         40         50         60 
MFTGIIEAVG NISAITSKGS DFEVSVNCDT LDLADVKIGD SIATNGICLT VVKLTANSYV 

        70         80         90        100        110        120 
ADLSIETLSR TAFNYYKVGQ AVNLEKAMLP TTRFGGHIVS GHVDAVAEVI ECRTSGRAID 

       130        140        150        160        170        180 
IWIRVPSQIE KYLSEKGSVT VDGVSLTVNA VTGNEFKLTI VPHTVVETTI ADFKVGNKVN 

       190        200        210 
IEVDVLARYI ERLLLVDKPE DKQSKISMDL LERNGFLL 

« Hide

References

[1]"Riboflavin synthesis genes are linked with the lux operon of Photobacterium phosphoreum."
Lee C.Y., O'Kane D.J., Meighen E.A.
J. Bacteriol. 176:2100-2104(1994) [PubMed: 8144477] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 2167 / LMG 4231 / NCIMB 844.

Cross-references

Sequence databases

L11391 Genomic DNA. Translation: AAA25628.1.

3D structure databases

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

Enzyme and pathway databases

BRENDA2.5.1.9. 348.

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_PHOPO
AccessionPrimary (citable) accession number: P51961
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 22, 2009
This is version 46 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

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