GCH1_CHICK
ID GCH1_CHICK Reviewed; 236 AA.
AC P50141;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=GTP cyclohydrolase 1;
DE EC=3.5.4.16 {ECO:0000250|UniProtKB:P30793};
DE AltName: Full=GTP cyclohydrolase I;
DE Short=GTP-CH-I;
GN Name=GCH1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7542887; DOI=10.1006/bbrc.1995.2026;
RA Maier J., Witter K., Guetlich M., Ziegler I., Werner T., Ninnemann H.;
RT "Homology cloning of GTP-cyclohydrolase I from various unrelated eukaryotes
RT by reverse-transcription polymerase chain reaction using a general set of
RT degenerate primers.";
RL Biochem. Biophys. Res. Commun. 212:705-711(1995).
CC -!- FUNCTION: May positively regulate nitric oxide synthesis in endothelial
CC cells. May be involved in dopamine synthesis. May modify pain
CC sensitivity and persistence. {ECO:0000250|UniProtKB:P30793}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate +
CC H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16;
CC Evidence={ECO:0000250|UniProtKB:P30793};
CC -!- ACTIVITY REGULATION: GTP shows a positive allosteric effect, and
CC tetrahydrobiopterin inhibits the enzyme activity. Zinc is required for
CC catalytic activity. Inhibited by Mg(2+).
CC {ECO:0000250|UniProtKB:P30793}.
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC {ECO:0000250|UniProtKB:P30793}.
CC -!- SUBUNIT: Toroid-shaped homodecamer, composed of two pentamers of five
CC dimers. {ECO:0000250|UniProtKB:P30793}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30793}. Nucleus
CC {ECO:0000250|UniProtKB:P30793}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
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DR EMBL; Z49267; CAA89261.1; -; mRNA.
DR PIR; I50646; I50646.
DR RefSeq; NP_990554.1; NM_205223.1.
DR AlphaFoldDB; P50141; -.
DR SMR; P50141; -.
DR STRING; 9031.ENSGALP00000019895; -.
DR PaxDb; P50141; -.
DR GeneID; 396146; -.
DR KEGG; gga:396146; -.
DR CTD; 2643; -.
DR VEuPathDB; HostDB:geneid_396146; -.
DR eggNOG; KOG2698; Eukaryota.
DR InParanoid; P50141; -.
DR OrthoDB; 793457at2759; -.
DR PhylomeDB; P50141; -.
DR UniPathway; UPA00848; UER00151.
DR PRO; PR:P50141; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003933; F:GTP cyclohydrolase activity; IDA:AgBase.
DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:AgBase.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IDA:AgBase.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.286.10; -; 1.
DR Gene3D; 3.30.1130.10; -; 1.
DR HAMAP; MF_00223; FolE; 1.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR043134; GTP-CH-I_N.
DR InterPro; IPR001474; GTP_CycHdrlase_I.
DR InterPro; IPR018234; GTP_CycHdrlase_I_CS.
DR InterPro; IPR020602; GTP_CycHdrlase_I_dom.
DR PANTHER; PTHR11109; PTHR11109; 1.
DR Pfam; PF01227; GTP_cyclohydroI; 1.
DR TIGRFAMs; TIGR00063; folE; 1.
DR PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
DR PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; Cytoplasm; GTP-binding; Hydrolase; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Tetrahydrobiopterin biosynthesis; Zinc.
FT CHAIN 1..236
FT /note="GTP cyclohydrolase 1"
FT /id="PRO_0000119477"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30793"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30793"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30793"
SQ SEQUENCE 236 AA; 26115 MW; F235D56B991D8C24 CRC64;
MAAARSCNGY ARREGPPSPK LGTEKPRVSA GSGGSGDGWR GERPRSEEDN ELSLPSLAAA
YTTILRALGE DPERQGLLKT PWRAATAMQF FTKGYQETIA DVLNDAIFDE DHDEMVIVKN
IDMFSLCEHH LVPFVGKVHI GYLPNKQVLG LSKLARIVEI YSRRLQVQER LTKQIAIAIT
EALQPAGVGV VIEATHMCMV MRGVQKMNSK TATSTMLGVF REDPKTREEF LTLIRS
