ID   GCH4_STAAM              Reviewed;         292 AA.
AC   Q99W43;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=SAV0566;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB56728.1; -; Genomic_DNA.
DR   RefSeq; WP_000134236.1; NC_002758.2.
DR   AlphaFoldDB; Q99W43; -.
DR   SMR; Q99W43; -.
DR   World-2DPAGE; 0002:Q99W43; -.
DR   PaxDb; Q99W43; -.
DR   EnsemblBacteria; BAB56728; BAB56728; SAV0566.
DR   KEGG; sav:SAV0566; -.
DR   HOGENOM; CLU_062816_1_1_9; -.
DR   OMA; PCSQGMS; -.
DR   PhylomeDB; Q99W43; -.
DR   BioCyc; SAUR158878:SAV_RS03155-MON; -.
DR   UniPathway; UPA00848; UER00151.
DR   Proteomes; UP000002481; 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.
FT   CHAIN           1..292
FT                   /note="GTP cyclohydrolase FolE2"
FT                   /id="PRO_0000147725"
FT   SITE            176
FT                   /note="May be catalytically important"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ   SEQUENCE   292 AA;  33481 MW;  78EAF10A9A42553B CRC64;
     MTEFDLSTRE GRWKHFGSVD PIEGTKPTTK NEMTDLQSTH KDFLFEIEEV GIKNLVYPVL
     VDQYQTAGTF SFSTSLTKDE KGINMSRIIE SVEKHYDNGI ELEFNTLYQV LRTLQTNMKQ
     NAAGVDVSGK WFFDRYSPTT NIKAVGNADV TYGLAIDGDK VTRKELTIEA TVTTLCPCSK
     EISEYSAHNQ RGVVTVKTYI NKDQNIVDDY KNKILDAMEA NASSILYPIL KRPDEKRVTE
     RAYENPRFVE DLIRLIAADL VEFDWLDGFD IECRNEESIH QHDAFAKLKY RK