Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P51600 (GCH1_PHYBL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP cyclohydrolase 1

EC=3.5.4.16
Alternative name(s):
GTP cyclohydrolase I
Short name=GTP-CH-I
OrganismPhycomyces blakesleeanus
Taxonomic identifier4837 [NCBI]
Taxonomic lineageEukaryotaFungiFungi incertae sedisEarly diverging fungal lineagesMucoromycotinaMucoralesPhycomycetaceaePhycomyces

Protein attributes

Sequence length94 AA.
Sequence statusFragment.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

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

Pathway

Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.

Subunit structure

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

Sequence similarities

Belongs to the GTP cyclohydrolase I family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›94›94GTP cyclohydrolase 1
PRO_0000119487

Sites

Metal binding181Zinc By similarity
Metal binding211Zinc By similarity
Metal binding891Zinc By similarity

Experimental info

Non-terminal residue11
Non-terminal residue941

Sequences

Sequence LengthMass (Da)Tools
P51600 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4F8C12A0407A65DD

FASTA9410,586
        10         20         30         40         50         60 
EDHDEMVIVK DVDIFSLCEH HKVPSTGKIS IGYIPNRRVV GLSKLARIAE MFSRRLQVQE 

        70         80         90 
RLTKQVATAL MEILQPQGVA VVVECSHLCM VMRG 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49760 mRNA. Translation: CAA89830.1.
PIRS54910.

3D structure databases

ProteinModelPortalP51600.
SMRP51600. Positions 1-94.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00848; UER00151.

Family and domain databases

InterProIPR001474. GTP_CycHdrlase_I.
IPR018234. GTP_CycHdrlase_I_CS.
IPR020602. GTP_CycHdrlase_I_dom.
[Graphical view]
PANTHERPTHR11109. PTHR11109. 1 hit.
PfamPF01227. GTP_cyclohydroI. 1 hit.
[Graphical view]
PROSITEPS00859. GTP_CYCLOHYDROL_1_1. 1 hit.
PS00860. GTP_CYCLOHYDROL_1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGCH1_PHYBL
AccessionPrimary (citable) accession number: P51600
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways