ID GCH12_PSEAE Reviewed; 181 AA. AC Q9I351; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=GTP cyclohydrolase 1 2; DE EC=3.5.4.16; DE AltName: Full=GTP cyclohydrolase I 2; DE Short=GTP-CH-I 2; GN Name=folE2; OrderedLocusNames=PA1674; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). 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: Homomer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE004091; AAG05063.1; -; Genomic_DNA. DR PIR; C83435; C83435. DR RefSeq; NP_250365.1; NC_002516.2. DR RefSeq; WP_003087639.1; NZ_QZGE01000003.1. DR AlphaFoldDB; Q9I351; -. DR SMR; Q9I351; -. DR STRING; 208964.PA1674; -. DR PaxDb; 208964-PA1674; -. DR GeneID; 879308; -. DR KEGG; pae:PA1674; -. DR PATRIC; fig|208964.12.peg.1735; -. DR PseudoCAP; PA1674; -. DR HOGENOM; CLU_049768_3_4_6; -. DR InParanoid; Q9I351; -. DR OrthoDB; 9801207at2; -. DR PhylomeDB; Q9I351; -. DR BioCyc; PAER208964:G1FZ6-1705-MONOMER; -. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000002438; Chromosome. 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; 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:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IBA:GO_Central. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00642; GTP_cyclohydro1; 1. 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_0000119429" SQ SEQUENCE 181 AA; 20236 MW; AE63943491AA7BC3 CRC64; MSLEQHYSSI LTQLGEDVNR EGLLDTPKRA AKAMKYLCRG YQQSLEEVVN GALFSSDNSE MVLVKDIELY SLCEHHLLPF IGKAHVAYIP NGKVLGLSKV ARIVDMYARR LQIQENMSRQ IAEAVQQVTG ALGVAVVIQA QHMCMMMRGV EKQNSSMVTS VMLGEFRDNA ATRSEFLSLI R //