GCH1_SOLLC
ID GCH1_SOLLC Reviewed; 456 AA.
AC Q8VYU3;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=GTP cyclohydrolase 1 {ECO:0000305};
DE EC=3.5.4.16 {ECO:0000269|PubMed:12221287};
DE AltName: Full=GTP cyclohydrolase I {ECO:0000303|PubMed:12221287};
GN Name=GCH1; Synonyms=GCHI {ECO:0000303|PubMed:12221287};
GN OrderedLocusNames=Solyc06g083230; ORFNames=LOC543831;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP TISSUE SPECIFICITY.
RX PubMed=12221287; DOI=10.1073/pnas.192278499;
RA Basset G., Quinlivan E.P., Ziemak M.J., Diaz De La Garza R., Fischer M.,
RA Schiffmann S., Bacher A., Gregory J.F., Hanson A.D.;
RT "Folate synthesis in plants: the first step of the pterin branch is
RT mediated by a unique bimodular GTP cyclohydrolase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12489-12494(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
CC -!- FUNCTION: GTP cyclohydrolase 1 is the first enzyme in the biosynthetic
CC pathway leading to folic acid. {ECO:0000269|PubMed:12221287}.
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:0000269|PubMed:12221287};
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12221287}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and unripe fruits.
CC {ECO:0000269|PubMed:12221287}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
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DR EMBL; AY069920; AAL49957.1; -; mRNA.
DR RefSeq; NP_001234141.1; NM_001247212.3.
DR AlphaFoldDB; Q8VYU3; -.
DR SMR; Q8VYU3; -.
DR STRING; 4081.Solyc06g083230.2.1; -.
DR PaxDb; Q8VYU3; -.
DR PRIDE; Q8VYU3; -.
DR EnsemblPlants; Solyc06g083230.3.1; Solyc06g083230.3.1; Solyc06g083230.3.
DR GeneID; 543831; -.
DR Gramene; Solyc06g083230.3.1; Solyc06g083230.3.1; Solyc06g083230.3.
DR KEGG; sly:543831; -.
DR eggNOG; KOG2698; Eukaryota.
DR HOGENOM; CLU_039473_0_0_1; -.
DR InParanoid; Q8VYU3; -.
DR OMA; IHSELHL; -.
DR OrthoDB; 793457at2759; -.
DR PhylomeDB; Q8VYU3; -.
DR BRENDA; 3.5.4.16; 3101.
DR SABIO-RK; Q8VYU3; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000004994; Chromosome 6.
DR ExpressionAtlas; Q8VYU3; baseline and differential.
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; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IBA:GO_Central.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.286.10; -; 2.
DR Gene3D; 3.30.1130.10; -; 2.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR InterPro; IPR043134; GTP-CH-I_N.
DR InterPro; IPR001474; GTP_CycHdrlase_I.
DR InterPro; IPR020602; GTP_CycHdrlase_I_dom.
DR PANTHER; PTHR11109; PTHR11109; 1.
DR Pfam; PF01227; GTP_cyclohydroI; 2.
PE 1: Evidence at protein level;
KW GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Tetrahydrobiopterin biosynthesis; Zinc.
FT CHAIN 1..456
FT /note="GTP cyclohydrolase 1"
FT /id="PRO_0000430620"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30793"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30793"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30793"
SQ SEQUENCE 456 AA; 49951 MW; 619867385D32BA43 CRC64;
MGALDEGHYH AEIDNEVSFE LGFETQPETL VIQDAVRVLL QGLGEDINRE GIKKTPFRVA
KALRQGTRGY KQKVNDIVHG ALFPEAGLEG GSGQAGGVGG LVIVRDLDLF SYCESCLLPF
QVKCHVGYVP SGKRVVGLSK LSRVADIFAK RLQSPQRLAD EVCTALQHGI KPTGVAVVLQ
CMHIHFPNFE SAFLDSTSQG WVKITATSGS GVFEDGNADV WTDFWSLLKF RGISIDNAHR
RSSGQSWCPS QSCGMPGQAN SAMTNAVNSI LKSLGEDPLR EELVETPSRF VKWFMNFRNS
NLEMKLNGFV RSRIDTRSPQ GGNFNDGICS ELNLSFWSQC EHHLLPFQGV VHIGYHSSDG
VNPVGRPLVQ SVVHFYGFKL QVQERVTRQI AETVSSFLGE DIIVVVEANH TCMISRGIEK
FGSNTATFAV LGRFSTDPVA RAKFLQSLPD SGSAGR
