Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot Q4L7B1 (RIBBA_STAHJ)

Last modified June 16, 2009. Version 31. 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
Synonyms: ribA
Ordered Locus Names: SH1155
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [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; 3,4-dihydroxy-2-butanone 4-phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP MF_01283

Cofactor biosynthesis; riboflavin biosynthesis; 6,7-dimethyl-8-(1-D-ribityl)lumazine 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_0000151741

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
Q4L7B1-1 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 1E941738D1618462

FASTA39343,703
        10         20         30         40         50         60 
MEFDEIKDAL NALKRGESII VVDDEDRENE GDLVAITQWM NDNTINFMAK EGRGLICAPI 

        70         80         90        100        110        120 
SKDLALKFNL MPMVEHNTDG FGTNFTVSID HATTSTGISA FDRMATARAL INPESTPEDF 

       130        140        150        160        170        180 
HKPGHLFPLI AKENGVLERT GHTEAAVDLA KLTKAAPAGV ICEIMNEDGT MAKGEQLEAF 

       190        200        210        220        230        240 
KHQHGLKMIT IESLVNYQKD KDTSVELKAK VNMPTDHGAF EMYGFESSLT KEEIVVLAKG 

       250        260        270        280        290        300 
EPRVTENVRI HSACLTGDIF HSQRCDCGAQ LESAMKYINE HGGMIIYLPQ EGRGIGLINK 

       310        320        330        340        350        360 
LRAYELIEQG HDTVTANLAL GFDEDLRDYH IAAQILNYFN VQQVNLLSNN PKKFEGLSEY 

       370        380        390 
GIKVADRTPI IVAENEHNHD YMNTKKIKMG HLI 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed: 16237012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP006716 Genomic DNA. Translation: BAE04464.1.
RefSeqYP_253070.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3481881.
GenomeReviewsGene locus SH1155 in contig AP006716_GR.
KEGGsha:SH1155.
NMPDRfig|279808.3.peg.2221.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ4L7B1.
OMAQ4L7B1. HTEASLE.

Enzyme and pathway databases

BioCycSHAE279808:SH1155-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_STAHJ
AccessionPrimary (citable) accession number: Q4L7B1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: August 2, 2005
Last modified: June 16, 2009
This is version 31 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