GCH4_PSEPF
ID GCH4_PSEPF Reviewed; 298 AA.
AC Q3K4B0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
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}; OrderedLocusNames=Pfl01_5658;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA77394.1; -; Genomic_DNA.
DR RefSeq; WP_011336651.1; NC_007492.2.
DR AlphaFoldDB; Q3K4B0; -.
DR SMR; Q3K4B0; -.
DR STRING; 205922.Pfl01_5658; -.
DR PRIDE; Q3K4B0; -.
DR EnsemblBacteria; ABA77394; ABA77394; Pfl01_5658.
DR KEGG; pfo:Pfl01_5658; -.
DR eggNOG; COG1469; Bacteria.
DR HOGENOM; CLU_062816_0_0_6; -.
DR OMA; AKGIHMS; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000002704; 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..298
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_0000289510"
FT SITE 149
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 298 AA; 32630 MW; 6BB9A08D174BE18C CRC64;
MNALTLPDVA AQAARQALPL EWVGMCGIAL PVFIEGQRLA AKADAGVSLD DGDARGIHMS
RLYLGLEAME QQNLSPALLR QVLQRFLDSH EDLSEAAYLN IHIDLLLRRP ALVSPLAGWK
NYPVTVSAQL KNKVFHVELK IDVAYSSTCP CSAALARQLI QQQFVDDFAN KPLQHADVLA
WLGSTQGIVA TPHSQRSTAQ LHLHLDEFVD ELPLTSIIND AEAALGTAVQ TAVKRADEQA
FALANGQNLM FCEDAARRLN LALRGSPGIS QFHVRVIHAE SLHAHDAVAE SHWRREQP