Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O84410 (RISA_CHLTR)

Last modified November 3, 2009. Version 54. 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
Synonyms: ribC
Ordered Locus Names: CT_405
OrganismChlamydia trachomatis [Complete proteome] [HAMAP]
Taxonomic identifier813 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia

Protein attributes

Sequence length199 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 – 199199Riboflavin synthase alpha chain
PRO_0000068165

Regions

Repeat1 – 9595Lumazine-binding 1
Repeat96 – 18893Lumazine-binding 2

Sequences

Sequence LengthMass (Da)Tools
O84410-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: C815DE0AC8534E16

FASTA19922,222
        10         20         30         40         50         60 
MFSGIIQEVA RVDLIHHLRD SMEIGVFARK LIDVVPGSSF SVDGICLTLV KRQYELLFFD 

        70         80         90        100        110        120 
VTEETMAWTT IKDYTVGTMV NLERSVRLGD EIGGHFVSGH VCGIGTIIAI EKSYMFFKAP 

       130        140        150        160        170        180 
ANLVPYILEK GFIAIDGISL TIARVKGDIF SVSLIPETRA RTSLGYKQVG AHVNMEPDMM 

       190 
TKMQVDTIMR FHAEKEISK 

« Hide

References

[1]"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis."
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.
Science 282:754-759(1998) [PubMed: 9784136] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D/UW-3/Cx.

Cross-references

Sequence databases

AE001273 Genomic DNA. Translation: AAC68002.1.
PIRH71519.
RefSeqNP_219915.1.

3D structure databases

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

Genome annotation databases

GeneID884709.
GenomeReviewsGene locus CT_405 in contig AE001273_GR.
KEGGctr:CT405.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO84410.
OMACLTVTKI.

Enzyme and pathway databases

BioCycCTRA315277:CT405-MON.
BRENDA2.5.1.9. 108.

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_CHLTR
AccessionPrimary (citable) accession number: O84410
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: November 3, 2009
This is version 54 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