GCH4_PSEPG
ID GCH4_PSEPG Reviewed; 301 AA.
AC B0KR89;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=GTP cyclohydrolase FolE2 {ECO:0000255|HAMAP-Rule:MF_01527};
DE EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_01527};
GN Name=folE2 {ECO:0000255|HAMAP-Rule:MF_01527};
GN OrderedLocusNames=PputGB1_5412;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate.
CC {ECO:0000255|HAMAP-Rule:MF_01527}.
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_01527};
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_01527}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family.
CC {ECO:0000255|HAMAP-Rule:MF_01527}.
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DR EMBL; CP000926; ABZ01294.1; -; Genomic_DNA.
DR RefSeq; WP_012274891.1; NC_010322.1.
DR AlphaFoldDB; B0KR89; -.
DR SMR; B0KR89; -.
DR STRING; 76869.PputGB1_5412; -.
DR EnsemblBacteria; ABZ01294; ABZ01294; PputGB1_5412.
DR KEGG; ppg:PputGB1_5412; -.
DR eggNOG; COG1469; Bacteria.
DR HOGENOM; CLU_062816_0_0_6; -.
DR OMA; AKGIHMS; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000002157; Chromosome.
DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1.
DR InterPro; IPR022838; GTP_cyclohydrolase_FolE2.
DR InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR PANTHER; PTHR36445; PTHR36445; 1.
DR Pfam; PF02649; GCHY-1; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..301
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_1000087581"
FT SITE 149
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 301 AA; 33077 MW; F896514A60269099 CRC64;
MTQLKLPDIA AQTQAYAVPL NWVGMCGIAL PVQFEGRTAA AKVDAGVSLV DGSSRGIHMS
RLYLALGSLE HQPLTPLAIR QLLEDFLSSH ASLSSAAYLR FSFEHLLNRP ALISPLAGWK
SYAVTVDTRI ENEVFHVELS VSVPYSSTCP CSAALARQLI QQQFQTHFSE QKIEKAAVLQ
WLGSAEGIVA TPHSQRSTAQ VQVRLNSNQQ VLPITELIDR IEASLGTAVQ TAVKRADEQA
FALANGQNLM FCEDAARRLH QALRQIEWSK AFKLRVEHAE SLHAHDAVAT SQWQWDVSCA
V