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O61573

- GCH1_OSTOS

UniProt

O61573 - GCH1_OSTOS

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Protein
GTP cyclohydrolase 1
Gene
gch
Organism
Ostertagia ostertagi (Brown stomach worm)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

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 bindingi104 – 1041Zinc By similarity
Metal bindingi107 – 1071Zinc By similarity
Metal bindingi175 – 1751Zinc By similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. GTP cyclohydrolase I activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
  2. tetrahydrobiopterin biosynthetic process Source: UniProtKB-KW
  3. tetrahydrofolate biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Tetrahydrobiopterin biosynthesis

Keywords - Ligandi

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

Enzyme and pathway databases

UniPathwayiUPA00848; UER00151.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase 1 (EC:3.5.4.16)
Alternative name(s):
GTP cyclohydrolase I
Short name:
GTP-CH-I
Gene namesi
Name:gch
OrganismiOstertagia ostertagi (Brown stomach worm)
Taxonomic identifieri6317 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaStrongylidaTrichostrongyloideaTrichostrongylidaeTrichostrongylinaeOstertagia

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213GTP cyclohydrolase 1UniRule annotation
PRO_0000119483Add
BLAST

Interactioni

Subunit structurei

Toroid-shaped homodecamer, composed of two pentamers of five dimers By similarity.

Structurei

3D structure databases

ProteinModelPortaliO61573.
SMRiO61573. Positions 30-211.

Family & Domainsi

Sequence similaritiesi

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.

O61573-1 [UniParc]FASTAAdd to Basket

« Hide

MASESGFLSS DSSSEDCDQK IIAFSKKTSN LDKMTAAYSS IISHVGEDVN    50
RQGLLKTPDR AAKAMLYFTK GYEQQLDDIL NDAVFDENHD EMVIVRDIEM 100
FSLCEHHLVP FNGKVHIGYI PNKKVLGLSK LARIVEMFSR RLQVQERLTK 150
QIATAMVQAV QPAGVAVVIE ASHMCMVMRG VQKINATTST SCMLGVFRDD 200
PKTREEFLNL IHK 213
Length:213
Mass (Da):23,843
Last modified:August 1, 1998 - v1
Checksum:i2B5170D1902C32E9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF052048 mRNA. Translation: AAC06296.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF052048 mRNA. Translation: AAC06296.1 .

3D structure databases

ProteinModelPortali O61573.
SMRi O61573. Positions 30-211.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00848 ; UER00151 .

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. "Identification of abundant mRNAs from the third stage larvae of the parasitic nematode, Ostertagia ostertagi."
    Moore J., Tetley L., Devaney E.
    Biochem. J. 347:763-770(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiGCH1_OSTOS
AccessioniPrimary (citable) accession number: O61573
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: February 19, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme

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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