ID   GCH1L_STAAW             Reviewed;         366 AA.
AC   Q8NWB9;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN   OrderedLocusNames=MW1511;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P67272}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC       {ECO:0000305}.
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DR   EMBL; BA000033; BAB95376.1; -; Genomic_DNA.
DR   RefSeq; WP_000683932.1; NC_003923.1.
DR   AlphaFoldDB; Q8NWB9; -.
DR   SMR; Q8NWB9; -.
DR   EnsemblBacteria; BAB95376; BAB95376; BAB95376.
DR   KEGG; sam:MW1511; -.
DR   HOGENOM; CLU_037423_1_0_9; -.
DR   OMA; EVAYDIY; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.120; -; 1.
DR   InterPro; IPR002678; DUF34/NIF3.
DR   InterPro; IPR017221; DUF34/NIF3_bac.
DR   InterPro; IPR036069; DUF34/NIF3_sf.
DR   InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR   PANTHER; PTHR13799; PTHR13799; 1.
DR   Pfam; PF01784; NIF3; 1.
DR   PIRSF; PIRSF037489; UCP037489_NIF3_YqfO; 1.
DR   SUPFAM; SSF102705; SSF102705; 1.
DR   TIGRFAMs; TIGR00486; YbgI_SA1388; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Zinc.
FT   CHAIN           1..366
FT                   /note="GTP cyclohydrolase 1 type 2 homolog"
FT                   /id="PRO_0000147332"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P67272"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P67272"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P67272"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P67272"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P67272"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P67272"
SQ   SEQUENCE   366 AA;  41153 MW;  FA1F28762D878C79 CRC64;
     MKIADLMTLL DHHVPFSTAE SWDNVGLLIG DEDVEVTGVL TALDCTLEVV NEAIEKGYNT
     IISHHPLIFK GVTSLKANGY GLIIRKLIQH DINLIAMHTN LDVNPYGVNM MLAKAMGLKN
     ISIINNQQDV YYKVQTYIPK DNVGPFKDKL SENGLAQEGN YEYCFFESEG RGQFKPVGEA
     NPTIGQIDKI EYVDEVKIEF MIDAYQKSRA EQLIKQYHPY ETPVFDFIEI KQTSLYGLGV
     MAEVDNQMTL EDFAADIKSK LNIPSVRFVG ESNQKIKRIA IIGGSGIGYE YQAVQQGADV
     FVTGDIKHHD ALDAKIHGVN LIDINHYSEY VMKEGLKTLL MNRFNTEKIN IDVEASTINT
     DPFQYI