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Q5HNE3 (RIBBA_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. 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
Ordered Locus Names:SERP1326
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [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_0000151740

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
Q5HNE3 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: C12B8589078DF592

FASTA39344,290
        10         20         30         40         50         60 
MQFDTIELAI EALRNGESII VVDDEDRENE GDLVAVTEWM DDNTINFMAR EGRGLICAPI 

        70         80         90        100        110        120 
DKSIAERLKL QSMEQNNTDI YGTHFTVSID HYKTTTGISA HERTQTARAL IDENTNPEDF 

       130        140        150        160        170        180 
HRPGHLFPLI AKENGVLTRN GHTEAAVDLA RLTGAQPAGV ICEIMNDDGT MAKGEDLQSF 

       190        200        210        220        230        240 
KERHHLKMIT IKSLVAFRKA VELNVNLKAK VKMPTDFGHF DMYGFTTNYS DEEIVAIVKG 

       250        260        270        280        290        300 
DLKSNPNVRM HSACLTGDIF HSQRCDCGAQ LEASMKYIDE HGGMIIYLPQ EGRGIGLINK 

       310        320        330        340        350        360 
LRAYELIEKG YDTVTANLAL GFDEDLRDYH VAAEILKYFD ISEINLLSNN PKKFEGLEDY 

       370        380        390 
GIEIVDRIEL IVPETQYNHS YMETKKNKMG HLI

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000029 Genomic DNA. Translation: AAW54662.1.
RefSeqYP_188898.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HNE3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HNE3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000041837; EBSTAP00000040380; EBSTAG00000041835.
GeneID3241713.
GenomeReviewsGene locus SERP1326 in contig CP000029_GR.
KEGGser:SERP1326.
NMPDRfig|176279.3.peg.1153.
PATRIC19613501. VBIStaEpi130894_1293.
TIGRSERP1326.

Phylogenomic databases

eggNOGCOG0108.
GeneTreeEBGT00050000025480.
HOGENOMHBG735778.
OMARCDCRMQ.
PhylomeDBQ5HNE3.
ProtClustDBCLSK885544.

Enzyme and pathway databases

BioCycSEPI176279:SERP1326-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_STAEQ
AccessionPrimary (citable) accession number: Q5HNE3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: February 15, 2005
Last modified: January 25, 2012
This is version 56 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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