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A9R1B1

- GCH1_YERPG

UniProt

A9R1B1 - GCH1_YERPG

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Protein

GTP cyclohydrolase 1

Gene

folE

Organism
Yersinia pestis bv. Antiqua (strain Angola)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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
Metal bindingi109 – 1091ZincUniRule annotation
Metal bindingi112 – 1121ZincUniRule annotation
Metal bindingi180 – 1801ZincUniRule annotation

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. GTP cyclohydrolase I activity Source: UniProtKB-HAMAP
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
  2. one-carbon metabolic process Source: UniProtKB-HAMAP
  3. tetrahydrofolate biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

GTP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciYPES349746:GHPB-3020-MONOMER.
UniPathwayiUPA00848; UER00151.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase 1UniRule annotation (EC:3.5.4.16UniRule annotation)
Alternative name(s):
GTP cyclohydrolase IUniRule annotation
Short name:
GTP-CH-IUniRule annotation
Gene namesi
Name:folEUniRule annotation
Ordered Locus Names:YpAngola_A3014
OrganismiYersinia pestis bv. Antiqua (strain Angola)
Taxonomic identifieri349746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001204: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 220220GTP cyclohydrolase 1PRO_1000100213Add
BLAST

Proteomic databases

PRIDEiA9R1B1.

Interactioni

Subunit structurei

Homopolymer.UniRule annotation

Protein-protein interaction databases

STRINGi349746.YpAngola_A3014.

Structurei

3D structure databases

ProteinModelPortaliA9R1B1.
SMRiA9R1B1. Positions 3-219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GTP cyclohydrolase I family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0302.
HOGENOMiHOG000221222.
KOiK01495.
OMAiVQFFSSR.
OrthoDBiEOG6XHC8G.

Family and domain databases

HAMAPiMF_00223. FolE.
InterProiIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view]
PANTHERiPTHR11109. PTHR11109. 1 hit.
PfamiPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00063. folE. 1 hit.
PROSITEiPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9R1B1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSLSKEAEL VHQALLARGL ETPLRKPELD AETRKTRIQA HMTEVMHLLN
60 70 80 90 100
LDLTDDSLAD TPRRIAKMYV DEIFSGLDYE NFPKITLIQN KMKVDEMVTV
110 120 130 140 150
RDITLTSTCE HHFVTIDGKA TVAYIPKDSV IGLSKINRIV QFFAQRPQVQ
160 170 180 190 200
ERLTQQILLA LQTLLGTNNV AVSIDAVHYC VKARGIRDAT SATTTTSLGG
210 220
LFKSSQNTRQ EFLRAVRHHG
Length:220
Mass (Da):24,714
Last modified:February 5, 2008 - v1
Checksum:i5B497C8B4FA301F8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000901 Genomic DNA. Translation: ABX87571.1.
RefSeqiYP_001607382.1. NC_010159.1.

Genome annotation databases

EnsemblBacteriaiABX87571; ABX87571; YpAngola_A3014.
GeneIDi5801486.
KEGGiypg:YpAngola_A3014.
PATRICi18575567. VBIYerPes97331_3547.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000901 Genomic DNA. Translation: ABX87571.1 .
RefSeqi YP_001607382.1. NC_010159.1.

3D structure databases

ProteinModelPortali A9R1B1.
SMRi A9R1B1. Positions 3-219.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349746.YpAngola_A3014.

Proteomic databases

PRIDEi A9R1B1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX87571 ; ABX87571 ; YpAngola_A3014 .
GeneIDi 5801486.
KEGGi ypg:YpAngola_A3014.
PATRICi 18575567. VBIYerPes97331_3547.

Phylogenomic databases

eggNOGi COG0302.
HOGENOMi HOG000221222.
KOi K01495.
OMAi VQFFSSR.
OrthoDBi EOG6XHC8G.

Enzyme and pathway databases

UniPathwayi UPA00848 ; UER00151 .
BioCyci YPES349746:GHPB-3020-MONOMER.

Family and domain databases

HAMAPi MF_00223. FolE.
InterProi IPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view ]
PANTHERi PTHR11109. PTHR11109. 1 hit.
Pfami PF01227. GTP_cyclohydroI. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00063. folE. 1 hit.
PROSITEi PS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
    Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
    J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Angola.

Entry informationi

Entry nameiGCH1_YERPG
AccessioniPrimary (citable) accession number: A9R1B1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: October 1, 2014
This is version 49 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