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Reviewed, UniProtKB/Swiss-Prot Q8CNU2 (RIBBA_STAES)

Last modified November 3, 2009. Version 47. 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 biosynthesis protein ribBA
Including the following 2 domains:
    1- Recommended name:
            3,4-dihydroxy-2-butanone 4-phosphate synthase
                Short name=DHBP synthase
              EC=4.1.99.12
    2- Recommended name:
            GTP cyclohydrolase-2
              EC=3.5.4.25
        Alternative name(s):
            GTP cyclohydrolase II
Gene names
Name: ribBA
Ordered Locus Names: SE_1439
OrganismStaphylococcus epidermidis (strain ATCC 12228) [Complete proteome] [HAMAP]
Taxonomic identifier176280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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

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-phosphoribosylamino)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.

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_0000151739

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
Q8CNU2-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 2D87843A194F6F37

FASTA39344,263
        10         20         30         40         50         60 
MQFDTIELAI EALRNGESII VVDDEDRENE GDLVAVTEWM DDNTINFMAK 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 DMYGFTTDYS 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]"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)."
Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.
Mol. Microbiol. 49:1577-1593(2003) [PubMed: 12950922] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE015929 Genomic DNA. Translation: AAO05038.1.
RefSeqNP_764994.1.

3D structure databases

HSSPHSSP built from PDB template 1G58 based on UniProtKB P24199.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8CNU2.

Genome annotation databases

GeneID1056615.
GenomeReviewsGene locus SE_1439 in contig AE015929_GR.
KEGGsep:SE1439.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8CNU2.
OMALRCDCRM.

Enzyme and pathway databases

BioCycSEPI176280:SE_1439-MON.

Family and domain databases

HAMAPMF_01283.
[Tree]
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR000926. GTP_CycHdrlase_II.
IPR016299. Riboflavin_synth_RibA.
[Graphical view]
Gene3DG3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
PfamPF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
PIRSFPIRSF001259. RibA. 1 hit.
ProDomPD003034. DHBP_synthase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00505. ribA. 1 hit.
TIGR00506. ribB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBBA_STAES
AccessionPrimary (citable) accession number: Q8CNU2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: March 1, 2003
Last modified: November 3, 2009
This is version 47 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