ID GCH12_PSESM Reviewed; 181 AA.
AC Q884Q3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=GTP cyclohydrolase 1 2 {ECO:0000255|HAMAP-Rule:MF_00223};
DE EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_00223};
DE AltName: Full=GTP cyclohydrolase I 2 {ECO:0000255|HAMAP-Rule:MF_00223};
DE Short=GTP-CH-I 2 {ECO:0000255|HAMAP-Rule:MF_00223};
GN Name=folE2 {ECO:0000255|HAMAP-Rule:MF_00223}; OrderedLocusNames=PSPTO_2035;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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:0000255|HAMAP-Rule:MF_00223};
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00223}.
CC -!- SUBUNIT: Homomer. {ECO:0000255|HAMAP-Rule:MF_00223}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family.
CC {ECO:0000255|HAMAP-Rule:MF_00223}.
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DR EMBL; AE016853; AAO55553.1; -; Genomic_DNA.
DR RefSeq; NP_791858.1; NC_004578.1.
DR RefSeq; WP_005616969.1; NC_004578.1.
DR AlphaFoldDB; Q884Q3; -.
DR SMR; Q884Q3; -.
DR STRING; 223283.PSPTO_2035; -.
DR GeneID; 61788648; -.
DR KEGG; pst:PSPTO_2035; -.
DR PATRIC; fig|223283.9.peg.2065; -.
DR eggNOG; COG0302; Bacteria.
DR HOGENOM; CLU_049768_3_4_6; -.
DR OrthoDB; 9801207at2; -.
DR PhylomeDB; Q884Q3; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
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 NCBIfam; TIGR00063; folE; 1.
DR PANTHER; PTHR11109:SF7; GTP CYCLOHYDROLASE 1; 1.
DR PANTHER; PTHR11109; GTP CYCLOHYDROLASE I; 1.
DR Pfam; PF01227; GTP_cyclohydroI; 1.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
DR PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1.
DR PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1.
PE 3: Inferred from homology;
KW GTP-binding; Hydrolase; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..181
FT /note="GTP cyclohydrolase 1 2"
FT /id="PRO_0000119433"
SQ SEQUENCE 181 AA; 20084 MW; 4D07BABCC9C16743 CRC64;
MTLEQNYTAI LGQLGEDVSR EGLLDTPKRA AKAMQYLCRG YAQTLEEVTN GALFSSDASE
MVMVKDIELY SLCEHHLLPF IGKAHVAYIP NGKVLGLSKV ARIVDMYARR LQIQENLSRQ
IAEAIQQVTG AQGVAVVIEA KHMCMMMRGV EKQNSAMITS VMLGEFRENA ATRSEFLSLI
K
//
