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Q4L3P5

- GCH4_STAHJ

UniProt

Q4L3P5 - GCH4_STAHJ

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Protein

GTP cyclohydrolase FolE2

Gene
folE2, SH2423
Organism
Staphylococcus haemolyticus (strain JCSC1435)
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

Converts GTP to 7,8-dihydroneopterin triphosphate By similarity.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 important By similarity

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

BioCyciSHAE279808:GJX7-2481-MONOMER.
UniPathwayiUPA00848; UER00151.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase FolE2 (EC:3.5.4.16)
Gene namesi
Name:folE2
Ordered Locus Names:SH2423
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000543: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292GTP cyclohydrolase FolE2UniRule annotationPRO_0000289525Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi279808.SH2423.

Structurei

3D structure databases

ProteinModelPortaliQ4L3P5.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1469.
HOGENOMiHOG000280679.
KOiK09007.
OMAiDVQSSRD.
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.

Q4L3P5-1 [UniParc]FASTAAdd to Basket

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MTEFDLSTRE GRWKHFGSVD PIEGTKPTTK NEMTDLQSTH KNFLFEIEEV    50
GIKNLIYPVN IDRFQTAGRF SFSTSLNKDE KGINMSRILE SVEKHYNNGL 100
ELNFDTLYQV LRTLQTNMKQ NSSGVDVSGK WFFDRFSPVT NIKAVGNADV 150
TYGLAIEQDQ ITRKEITIEA TVTTLCPCSK EISEYSAHNQ RGVVTVKVYL 200
DKNNQVVDDY KDKILDAMEA NASSILYPIL KRPDEKRVTE RAYENPRFVE 250
DLIRLIAADL VEFDWIDGFD IECRNEESIH QHDAFAKLKY RK 292
Length:292
Mass (Da):33,672
Last modified:August 2, 2005 - v1
Checksum:iF708C438D005469C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006716 Genomic DNA. Translation: BAE05732.1.
RefSeqiWP_011276678.1. NC_007168.1.
YP_254338.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE05732; BAE05732; SH2423.
GeneIDi3482711.
KEGGisha:SH2423.
PATRICi19620921. VBIStaHae67511_2380.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006716 Genomic DNA. Translation: BAE05732.1 .
RefSeqi WP_011276678.1. NC_007168.1.
YP_254338.1. NC_007168.1.

3D structure databases

ProteinModelPortali Q4L3P5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 279808.SH2423.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAE05732 ; BAE05732 ; SH2423 .
GeneIDi 3482711.
KEGGi sha:SH2423.
PATRICi 19620921. VBIStaHae67511_2380.

Phylogenomic databases

eggNOGi COG1469.
HOGENOMi HOG000280679.
KOi K09007.
OMAi DVQSSRD.
OrthoDBi EOG6X6RBH.

Enzyme and pathway databases

UniPathwayi UPA00848 ; UER00151 .
BioCyci SHAE279808:GJX7-2481-MONOMER.

Family and domain databases

HAMAPi MF_01527_B. GTP_cyclohydrol_B.
InterProi IPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view ]
Pfami PF02649. GCHY-1. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00294. TIGR00294. 1 hit.
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCSC1435.

Entry informationi

Entry nameiGCH4_STAHJ
AccessioniPrimary (citable) accession number: Q4L3P5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: August 2, 2005
Last modified: September 3, 2014
This is version 58 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

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