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A3D367 (RIBA_SHEB5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:Sbal_1668
OrganismShewanella baltica (strain OS155 / ATCC BAA-1091) [Complete proteome] [HAMAP]
Taxonomic identifier325240 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length204 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

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 – 204204GTP cyclohydrolase-2 HAMAP-Rule MF_00179
PRO_1000040579

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
A3D367 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 81F61281BD8FAA24

FASTA20422,997
        10         20         30         40         50         60 
MSIKYVATSK LPTPWGVFAM HGFEDTESGK EHVALTFGTL SADEPVLGRI HSECLTGDAL 

        70         80         90        100        110        120 
FSLRCDCGFQ LQAAMQNIAE TGSGFILYLR QEGRGIGLLN KIRAYELQDK GANTVEANEQ 

       130        140        150        160        170        180 
LGFEADMRKY DMIKPILEQI GVKHVRLMTN NPRKVKAMKE FGIEVVERVP LQVGKNRYNE 

       190        200 
AYLKTKSTEL GHMMSEYHFM DENK 

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS155."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I., Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS155 / ATCC BAA-1091.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000563 Genomic DNA. Translation: ABN61180.1.
RefSeqYP_001050049.1. NC_009052.1.

3D structure databases

ProteinModelPortalA3D367.
SMRA3D367. Positions 1-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING325240.Sbal_1668.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN61180; ABN61180; Sbal_1668.
GeneID4844764.
KEGGsbl:Sbal_1668.
PATRIC37182199. VBISheBal55297_1948.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0807.
HOGENOMHOG000115442.
KOK01497.
OMAQGFILYL.
OrthoDBEOG679TK8.

Enzyme and pathway databases

BioCycSBAL325240:GCTA-1697-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_SHEB5
AccessionPrimary (citable) accession number: A3D367
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 44 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