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Reviewed, UniProtKB/Swiss-Prot Q9PJZ1 (RISA_CHLMU)

Last modified February 9, 2010. Version 56. 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: TC_0685
OrganismChlamydia muridarum [Complete proteome] [HAMAP]
Taxonomic identifier83560 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia

Protein attributes

Sequence length198 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 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; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2.

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 – 198198Riboflavin synthase alpha chain
PRO_0000068163

Regions

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

Sequences

Sequence LengthMass (Da)Tools
Q9PJZ1-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 8C6218EFBD94C318

FASTA19821,761
        10         20         30         40         50         60 
MFSGIIQEVA RVDLIHHYGD SMEIGIFARN LVDGVPGSSI AVDGICLTLV KREFELLFFD 

        70         80         90        100        110        120 
VTEETMACTT IKNYTVGSMV NLERSVRLGD EIGGHFVSGH VCGVGTIIAV EKSYMFFKAP 

       130        140        150        160        170        180 
TNLVPYVLEK GFIAIDGISL TIAQVRGDIF SVSVIPETRA RTSLGYKQVG SHVNMEPDMM 

       190 
TKMQVDTVMR FQAEKIGK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39502.1.
PIRG81675.
RefSeqNP_297059.1.

3D structure databases

SMRQ9PJZ1. Positions 1-185.
ModBaseSearch...

Genome annotation databases

GeneID1246046.
GenomeReviewsGene locus TC_0685 in contig AE002160_GR.
KEGGcmu:TC0685.
TIGRTC_0685.

Phylogenomic databases

HOGENOMHBG289809.
OMADEIGGHS.
PhylomeDBQ9PJZ1.

Enzyme and pathway databases

BioCycCMUR243161:TC_0685-MONOMER.
BRENDA2.5.1.9. 256349.

Family and domain databases

InterProIPR001783. Lumazine_bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERPTHR21098. Lumazine_bd. 1 hit.
PfamPF00677. Lum_binding. 2 hits.
[Graphical view]
PIRSFPIRSF000498. Riboflavin_syn_A. 1 hit.
TIGRFAMsTIGR00187. ribE. 1 hit.
PROSITEPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRISA_CHLMU
AccessionPrimary (citable) accession number: Q9PJZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: February 9, 2010
This is version 56 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