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P51600

- GCH1_PHYBL

UniProt

P51600 - GCH1_PHYBL

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Protein

GTP cyclohydrolase 1

Gene
N/A
Organism
Phycomyces blakesleeanus
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

GTP cyclohydrolase 1 is the first enzyme in the biosynthetic pathway leading to folic acid.

Catalytic activityi

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

Enzyme regulationi

GTP shows a positive allosteric effect, and tetrahydrobiopterin inhibits the enzyme activity By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi18 – 181Zinc By similarity
Metal bindingi21 – 211Zinc By similarity
Metal bindingi89 – 891Zinc 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. folic acid biosynthetic process Source: UniProtKB-KW
  3. tetrahydrofolate biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Folate 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
OrganismiPhycomyces blakesleeanus
Taxonomic identifieri4837 [NCBI]
Taxonomic lineageiEukaryotaFungiFungi incertae sedisEarly diverging fungal lineagesMucoromycotinaMucoralesPhycomycetaceaePhycomyces

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›94›94GTP cyclohydrolase 1PRO_0000119487Add
BLAST

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP51600.
SMRiP51600. Positions 1-94.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

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]
PROSITEiPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P51600-1 [UniParc]FASTAAdd to Basket

« Hide

EDHDEMVIVK DVDIFSLCEH HKVPSTGKIS IGYIPNRRVV GLSKLARIAE   50
MFSRRLQVQE RLTKQVATAL MEILQPQGVA VVVECSHLCM VMRG 94
Length:94
Mass (Da):10,586
Last modified:October 1, 1996 - v1
Checksum:i4F8C12A0407A65DD
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei94 – 941

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49760 mRNA. Translation: CAA89830.1.
PIRiS54910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49760 mRNA. Translation: CAA89830.1 .
PIRi S54910.

3D structure databases

ProteinModelPortali P51600.
SMRi P51600. Positions 1-94.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00848 ; UER00151 .

Family and domain databases

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 ]
PROSITEi PS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes by reverse-transcription polymerase chain reaction using a general set of degenerate primers."
    Maier J., Witter K., Guetlich M., Ziegler I., Werner T., Ninnemann H.
    Biochem. Biophys. Res. Commun. 212:705-711(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CBS 283.35.

Entry informationi

Entry nameiGCH1_PHYBL
AccessioniPrimary (citable) accession number: P51600
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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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