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Q31ZX1 (RIBA_SHIBS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP cyclohydrolase-2

EC=3.5.4.25
Alternative name(s):
GTP cyclohydrolase II
Gene names
Name:ribA
Ordered Locus Names:SBO_1787
OrganismShigella boydii serotype 4 (strain Sb227) [Complete proteome] [HAMAP]
Taxonomic identifier300268 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate By similarity. HAMAP-Rule MF_00179

Catalytic activity

GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. HAMAP-Rule MF_00179

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00179

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4. HAMAP-Rule MF_00179

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00179

Sequence similarities

Belongs to the GTP cyclohydrolase II family.

Ontologies

Keywords
   Biological processRiboflavin biosynthesis
   LigandGTP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processriboflavin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTP cyclohydrolase II activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196GTP cyclohydrolase-2 HAMAP-Rule MF_00179
PRO_1000040589

Regions

Nucleotide binding49 – 535GTP By similarity
Nucleotide binding92 – 943GTP By similarity

Sites

Active site1261Proton acceptor Potential
Active site1281Nucleophile By similarity
Metal binding541Zinc; catalytic By similarity
Metal binding651Zinc; catalytic By similarity
Metal binding671Zinc; catalytic By similarity
Binding site701GTP By similarity
Binding site1141GTP By similarity
Binding site1491GTP By similarity
Binding site1541GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q31ZX1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: C22FED98F48098DF

FASTA19621,836
        10         20         30         40         50         60 
MQLKRVAEAK LPTPWGDFLM VGFEELATGH DHVALVYGDI SGHTPVLARV HSECLTGDAL 

        70         80         90        100        110        120 
FSLRCDCGFQ LEAALTQIAE EGRGILLYHR QEGRNIGLLN KIRAYALQDQ GYDTVEANHQ 

       130        140        150        160        170        180 
LGFAADERDF TLCADMFKLL GVNEVRLLTN NPKKVEILTE AGINIVERVP LIVGRNPNNE 

       190 
HYLDTKAEKM GHLLNK 

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sb227.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000036 Genomic DNA. Translation: ABB66387.1.
RefSeqYP_408215.1. NC_007613.1.

3D structure databases

ProteinModelPortalQ31ZX1.
SMRQ31ZX1. Positions 1-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300268.SBO_1787.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB66387; ABB66387; SBO_1787.
GeneID3780770.
KEGGsbo:SBO_1787.
PATRIC18682716. VBIShiBoy33460_2286.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0807.
HOGENOMHOG000115442.
KOK01497.
OMAQGFILYL.
OrthoDBEOG679TK8.
ProtClustDBPRK00393.

Enzyme and pathway databases

BioCycSBOY300268:GJFL-1784-MONOMER.
UniPathwayUPA00275; UER00400.

Family and domain databases

HAMAPMF_00179. RibA.
InterProIPR000926. GTP_CycHdrlaseII_RibA.
[Graphical view]
PfamPF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00505. ribA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBA_SHIBS
AccessionPrimary (citable) accession number: Q31ZX1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: February 19, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways