GCH4_STAEQ
ID GCH4_STAEQ Reviewed; 292 AA.
AC Q5HRI1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=SERP0212;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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}.
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; CP000029; AAW53584.1; -; Genomic_DNA.
DR RefSeq; WP_002445753.1; NC_002976.3.
DR AlphaFoldDB; Q5HRI1; -.
DR SMR; Q5HRI1; -.
DR STRING; 176279.SERP0212; -.
DR EnsemblBacteria; AAW53584; AAW53584; SERP0212.
DR KEGG; ser:SERP0212; -.
DR eggNOG; COG1469; Bacteria.
DR HOGENOM; CLU_062816_1_1_9; -.
DR OMA; PCSQGMS; -.
DR OrthoDB; 757842at2; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000000531; 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.
DR TIGRFAMs; TIGR00294; TIGR00294; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..292
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_0000147731"
FT SITE 176
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 292 AA; 33656 MW; 04DE264081C8E6C8 CRC64;
MTEFDLSTRE GRWKHFGSVD PVKGTKPTTK NEMTDLQSTH KNFLFEIEEV GIKNLTYPVL
IDQYQTAGLF SFSTSLNKNE KGINMSRILE SVEKHYDNGI ELEFNTLHQL LRTLQDKMNQ
NAAGVDVSGK WFFDRYSPVT HIKAVGHADV TYGLAIENHT VTRKELTIQA KVTTLCPCSK
EISEYSAHNQ RGIVTVKAYL DKNNDVIDDY KNKILDAMEA NASSILYPIL KRPDEKRVTE
RAYENPRFVE DLIRLIAADL VEFDWIEGFD IECRNEESIH QHDAFARLKY RK