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Protein

GTP cyclohydrolase FolE2

Gene

folE2

Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Converts GTP to 7,8-dihydroneopterin triphosphate.UniRule annotation

Catalytic activityi

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei176 – 1761May be catalytically importantUniRule annotation

GO - Molecular functioni

  1. GTP cyclohydrolase I activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciSAUR273036:GJVS-535-MONOMER.
UniPathwayiUPA00848; UER00151.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase FolE2UniRule annotation (EC:3.5.4.16UniRule annotation)
Gene namesi
Name:folE2UniRule annotation
Ordered Locus Names:SAB0516c
OrganismiStaphylococcus aureus (strain bovine RF122 / ET3-1)
Taxonomic identifieri273036 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000001927 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292GTP cyclohydrolase FolE2PRO_0000289522Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi273036.SAB0516c.

Structurei

3D structure databases

ProteinModelPortaliQ2YS98.
SMRiQ2YS98. Positions 47-290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GTP cyclohydrolase IV family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1469.
HOGENOMiHOG000280679.
KOiK09007.
OMAiGAHNQRG.
OrthoDBiEOG6X6RBH.

Family and domain databases

HAMAPiMF_01527_B. GTP_cyclohydrol_B.
InterProiIPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view]
PfamiPF02649. GCHY-1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00294. TIGR00294. 1 hit.

Sequencei

Sequence statusi: Complete.

Q2YS98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEFDLSTRE GRWKHFGSVD PIEGTKPTTK NEMTDLQSTH KDFLFEIEEV
60 70 80 90 100
GIKNLVYPVL VDQYQTAGTF SFSTSLTKDE KGINMSRIIE SVEKHYDNGI
110 120 130 140 150
ELEFNTLYQV LRTLQTNMKQ NAAGVDVSGK WFFDRYSPTT NIKAVGNADV
160 170 180 190 200
TYGLAIDGDK VTRKELTIEA TVTTLCPCSK EISEYSAHNQ RGVVTVKTYI
210 220 230 240 250
NKDQDIVDDY KNKILDAMEA NASSILYPIL KRPDEKRVTE RAYENPRFVE
260 270 280 290
DLIRLIAADL VEFDWLDGFD IECRNEESIH QHDAFAKLKY RK
Length:292
Mass (Da):33,482
Last modified:December 20, 2005 - v1
Checksum:i22E051A090E85536
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ938182 Genomic DNA. Translation: CAI80204.1.
RefSeqiYP_416012.1. NC_007622.1.

Genome annotation databases

EnsemblBacteriaiCAI80204; CAI80204; SAB0516c.
GeneIDi3794721.
KEGGisab:SAB0516c.
PATRICi19521819. VBIStaAur92441_0561.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ938182 Genomic DNA. Translation: CAI80204.1.
RefSeqiYP_416012.1. NC_007622.1.

3D structure databases

ProteinModelPortaliQ2YS98.
SMRiQ2YS98. Positions 47-290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273036.SAB0516c.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAI80204; CAI80204; SAB0516c.
GeneIDi3794721.
KEGGisab:SAB0516c.
PATRICi19521819. VBIStaAur92441_0561.

Phylogenomic databases

eggNOGiCOG1469.
HOGENOMiHOG000280679.
KOiK09007.
OMAiGAHNQRG.
OrthoDBiEOG6X6RBH.

Enzyme and pathway databases

UniPathwayiUPA00848; UER00151.
BioCyciSAUR273036:GJVS-535-MONOMER.

Family and domain databases

HAMAPiMF_01527_B. GTP_cyclohydrol_B.
InterProiIPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view]
PfamiPF02649. GCHY-1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00294. TIGR00294. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular correlates of host specialization in Staphylococcus aureus."
    Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.
    PLoS ONE 2:E1120-E1120(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: bovine RF122 / ET3-1.

Entry informationi

Entry nameiGCH4_STAAB
AccessioniPrimary (citable) accession number: Q2YS98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: December 20, 2005
Last modified: January 7, 2015
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.