ID   GCH4_STAAS              Reviewed;         292 AA.
AC   Q6GBS1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=SAS0524;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG42299.1; -; Genomic_DNA.
DR   RefSeq; WP_000134232.1; NC_002953.3.
DR   AlphaFoldDB; Q6GBS1; -.
DR   SMR; Q6GBS1; -.
DR   KEGG; sas:SAS0524; -.
DR   HOGENOM; CLU_062816_1_1_9; -.
DR   OMA; PCSQGMS; -.
DR   UniPathway; UPA00848; UER00151.
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.
FT   CHAIN           1..292
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000147728"
FT   SITE            176
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   292 AA;  33482 MW;  22E051A090E85536 CRC64;
     MTEFDLSTRE GRWKHFGSVD PIEGTKPTTK NEMTDLQSTH KDFLFEIEEV GIKNLVYPVL
     VDQYQTAGTF SFSTSLTKDE KGINMSRIIE SVEKHYDNGI ELEFNTLYQV LRTLQTNMKQ
     NAAGVDVSGK WFFDRYSPTT NIKAVGNADV TYGLAIDGDK VTRKELTIEA TVTTLCPCSK
     EISEYSAHNQ RGVVTVKTYI NKDQDIVDDY KNKILDAMEA NASSILYPIL KRPDEKRVTE
     RAYENPRFVE DLIRLIAADL VEFDWLDGFD IECRNEESIH QHDAFAKLKY RK