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Q7A511 (RIBBA_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Riboflavin biosynthesis protein ribBA

Including the following 2 domains:

  1. 3,4-dihydroxy-2-butanone 4-phosphate synthase
    Short name=DHBP synthase
    EC=4.1.99.12
  2. GTP cyclohydrolase-2
    EC=3.5.4.25
    Alternative name(s):
    GTP cyclohydrolase II
Gene names
Name:ribBA
Synonyms:ribA
Ordered Locus Names:SA1587
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate By similarity. HAMAP MF_01283

Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate By similarity. HAMAP MF_01283

Catalytic activity

D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. HAMAP MF_01283

GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. HAMAP MF_01283

Cofactor

Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity.

Binds 1 zinc ion per subunit By similarity. HAMAP MF_01283

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP MF_01283

Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4. HAMAP MF_01283

Sequence similarities

In the N-terminal section; belongs to the DHBP synthase family.

In the C-terminal section; belongs to the GTP cyclohydrolase II family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Riboflavin biosynthesis protein ribBA HAMAP MF_01283
PRO_0000151735

Regions

Nucleotide binding249 – 2535GTP By similarity
Nucleotide binding291 – 2933GTP By similarity
Region1 – 200200DHBP synthase HAMAP MF_01283
Region27 – 282D-ribulose 5-phosphate binding By similarity
Region139 – 1435D-ribulose 5-phosphate binding By similarity
Region201 – 393193GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site3251Proton acceptor; for GTP cyclohydrolase activity Potential
Active site3271Nucleophile; for GTP cyclohydrolase activity By similarity
Metal binding281Magnesium or manganese 1 By similarity
Metal binding281Magnesium or manganese 2 By similarity
Metal binding1421Magnesium or manganese 2 By similarity
Metal binding2541Zinc; catalytic By similarity
Metal binding2651Zinc; catalytic By similarity
Metal binding2671Zinc; catalytic By similarity
Binding site321D-ribulose 5-phosphate By similarity
Binding site1631D-ribulose 5-phosphate By similarity
Binding site2701GTP By similarity
Binding site3131GTP By similarity
Binding site3481GTP By similarity
Binding site3531GTP By similarity
Site1251Essential for DHBP synthase activity By similarity
Site1631Essential for DHBP synthase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7A511 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 764A49DFDD46792C

FASTA39344,148
        10         20         30         40         50         60 
MQFDNIDSAL MALKNGETII VVDDENRENE GDLVAVTEWM NDNTINFMAK EARGLICAPV 

        70         80         90        100        110        120 
SKDIAQRLDL VQMVDDNSDI FGTQFTVSID HVDTTTGISA YERTLTAKKL IDPSSEAKDF 

       130        140        150        160        170        180 
NRPGHLFPLV AQDKGVLARN GHTEAAVDLA KLTGAKPAGV ICEIMNDDGT MAKGQDLQNF 

       190        200        210        220        230        240 
KEKHQLKMIT IDDLIEYRKK LEPEIEFKAK VKMPTDFGTF DMYGFKATYT DEEIVVLTKG 

       250        260        270        280        290        300 
AIRQHENVRL HSACLTGDIF HSQRCDCGAQ LESSMKYINE HGGMIIYLPQ EGRGIGLLNK 

       310        320        330        340        350        360 
LRAYELIEQG YDTVTANLAL GFDEDLRDYH IAAQILKYFN IEHINLLSNN PSKFEGLKQY 

       370        380        390 
GIDIAERIEV IVPETVHNHD YMVTKKIKMG HLI

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000018 Genomic DNA. Translation: BAB42855.1.
PIRB89962.
RefSeqNP_374876.1. NC_002745.2.

3D structure databases

ProteinModelPortalQ7A511.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7A511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000000735; EBSTAP00000000735; EBSTAG00000000735.
GeneID1124433.
GenomeReviewsGene locus SA1587 in contig BA000018_GR.
KEGGsau:SA1587.
PATRIC19575480. VBIStaAur116463_1710.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0108.
GeneTreeEBGT00050000025480.
HOGENOMHBG735778.
OMARCDCRMQ.
PhylomeDBQ7A511.
ProtClustDBCLSK885544.

Enzyme and pathway databases

BioCycSAUR158879:SA1587-MONOMER.

Family and domain databases

HAMAPMF_01283. RibBA.
[Tree]
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR000926. GTP_CycHdrlaseII_RibA.
IPR016299. Riboflavin_synth_RibBA.
[Graphical view]
Gene3DG3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
KOK14652.
PfamPF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
PIRSFPIRSF001259. RibA. 1 hit.
SUPFAMSSF55821. DHBP_synth_RibB-like_a/b_dom. 1 hit.
TIGRFAMsTIGR00505. RibA. 1 hit.
TIGR00506. RibB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBBA_STAAN
AccessionPrimary (citable) accession number: Q7A511
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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