GCH1_ARATH
ID GCH1_ARATH Reviewed; 466 AA.
AC Q9SFV7; Q8S3C2;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=At3g07270 {ECO:0000312|Araport:AT3G07270};
GN ORFNames=T1B9.6 {ECO:0000312|EMBL:AAF20219.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
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. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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:0000250|UniProtKB:Q8VYU3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SFV7-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}.
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DR EMBL; AF489530; AAM03126.1; -; mRNA.
DR EMBL; AC012395; AAF20219.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74520.1; -; Genomic_DNA.
DR EMBL; AY099882; AAM20733.1; -; mRNA.
DR EMBL; BT006600; AAP31944.1; -; mRNA.
DR RefSeq; NP_187383.1; NM_111607.3. [Q9SFV7-1]
DR AlphaFoldDB; Q9SFV7; -.
DR SMR; Q9SFV7; -.
DR BioGRID; 5250; 4.
DR IntAct; Q9SFV7; 3.
DR STRING; 3702.AT3G07270.1; -.
DR PaxDb; Q9SFV7; -.
DR PRIDE; Q9SFV7; -.
DR EnsemblPlants; AT3G07270.1; AT3G07270.1; AT3G07270. [Q9SFV7-1]
DR GeneID; 819915; -.
DR Gramene; AT3G07270.1; AT3G07270.1; AT3G07270. [Q9SFV7-1]
DR KEGG; ath:AT3G07270; -.
DR Araport; AT3G07270; -.
DR TAIR; locus:2098525; AT3G07270.
DR eggNOG; KOG2698; Eukaryota.
DR HOGENOM; CLU_039473_0_0_1; -.
DR PhylomeDB; Q9SFV7; -.
DR BioCyc; ARA:AT3G07270-MON; -.
DR BRENDA; 3.5.4.16; 399.
DR UniPathway; UPA00848; UER00151.
DR PRO; PR:Q9SFV7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SFV7; baseline and differential.
DR Genevisible; Q9SFV7; AT.
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: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 Alternative splicing; GTP-binding; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Tetrahydrobiopterin biosynthesis;
KW Zinc.
FT CHAIN 1..466
FT /note="GTP cyclohydrolase 1"
FT /id="PRO_0000430619"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30793"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30793"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P30793"
FT CONFLICT 18
FT /note="K -> R (in Ref. 1; AAM03126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 51380 MW; D424D8E383E4440F CRC64;
MGALDEGCLN LELDIGMKNG CIELAFEHQP ETLAIQDAVK LLLQGLHEDV NREGIKKTPF
RVAKALREGT RGYKQKVKDY VQSALFPEAG LDEGVGQAGG VGGLVVVRDL DHYSYCESCL
LPFHVKCHIG YVPSGQRVLG LSKFSRVTDV FAKRLQDPQR LADDICSALQ HWVKPAGVAV
VLECSHIHFP SLDLDSLNLS SHRGFVKLLV SSGSGVFEDE SSNLWGEFQS FLMFKGVKTQ
ALCRNGSSVK EWCPSVKSSS KLSPEVDPEM VSAVVSILKS LGEDPLRKEL IATPTRFLKW
MLNFQRTNLE MKLNSFNPAK VNGEVKEKRL HCELNMPFWS MCEHHLLPFY GVVHIGYFCA
EGSNPNPVGS SLMKAIVHFY GFKLQVQERM TRQIAETLSP LVGGDVIVVA EAGHTCMISR
GIEKFGSSTA TIAVLGRFSS DNSARAMFLD KIHTTNALKT ESSSPF
