GCH1_CAEEL
ID GCH1_CAEEL Reviewed; 223 AA.
AC Q19980;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=GTP cyclohydrolase 1;
DE EC=3.5.4.16;
DE AltName: Full=GTP cyclohydrolase I;
DE Short=GTP-CH-I;
GN Name=cat-4; ORFNames=F32G8.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Involved in serotonin and dopamine biosynthesis that affects
CC movement, mating behavior, foraging behavior, and cell migration.
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 -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC -!- SUBUNIT: Toroid-shaped homodecamer, composed of two pentamers of five
CC dimers. {ECO:0000250}.
CC -!- INTERACTION:
CC Q19980; W6RTA4: cla-1; NbExp=2; IntAct=EBI-311852, EBI-2916517;
CC Q19980; Q22306: T07D4.2; NbExp=2; IntAct=EBI-311852, EBI-311847;
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
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DR EMBL; Z72509; CAA96650.1; -; Genomic_DNA.
DR PIR; T21669; T21669.
DR RefSeq; NP_505710.1; NM_073309.5.
DR AlphaFoldDB; Q19980; -.
DR SMR; Q19980; -.
DR BioGRID; 44501; 10.
DR DIP; DIP-24416N; -.
DR IntAct; Q19980; 10.
DR STRING; 6239.F32G8.6; -.
DR EPD; Q19980; -.
DR PaxDb; Q19980; -.
DR PeptideAtlas; Q19980; -.
DR EnsemblMetazoa; F32G8.6.1; F32G8.6.1; WBGene00000298.
DR GeneID; 179472; -.
DR KEGG; cel:CELE_F32G8.6; -.
DR UCSC; F32G8.6; c. elegans.
DR CTD; 179472; -.
DR WormBase; F32G8.6; CE05795; WBGene00000298; cat-4.
DR eggNOG; KOG2698; Eukaryota.
DR GeneTree; ENSGT00390000013481; -.
DR HOGENOM; CLU_049768_2_0_1; -.
DR InParanoid; Q19980; -.
DR OMA; WMTRDIA; -.
DR OrthoDB; 793457at2759; -.
DR PhylomeDB; Q19980; -.
DR Reactome; R-CEL-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR UniPathway; UPA00848; UER00151.
DR PRO; PR:Q19980; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000298; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IMP:WormBase.
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:0006585; P:dopamine biosynthetic process from tyrosine; IMP:WormBase.
DR GO; GO:0042438; P:melanin biosynthetic process; IMP:WormBase.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IMP:WormBase.
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 1: Evidence at protein level;
KW Allosteric enzyme; GTP-binding; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Tetrahydrobiopterin biosynthesis;
KW Zinc.
FT CHAIN 1..223
FT /note="GTP cyclohydrolase 1"
FT /id="PRO_0000119480"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 223 AA; 25132 MW; B6584D6CBA6FA003 CRC64;
MSRIENESGF LSSDAASVGS EDDKVEMKKR NGTIPKEDHL KSMCNAYQSI IQHVGEDINR
QGLLKTPERA AKAMMAFTKG YDDQLDELLN EAVFDEDHDE MVIVKDIEMF SLCEHHLVPF
MGKVHIGYIP NKKVLGLSKL ARIVEMFSRR LQVQERLTKQ IATAMVQAVQ PSGVAVVIEA
SHMCMVMRGV QKINASTTTS CMLGVFRDDP KTREEFLNLI NKR
