ID   GCH1L_STAAM             Reviewed;         366 AA.
AC   P67272; Q99TT7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN   OrderedLocusNames=SAV1559;
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).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT,
RP   AND DOMAIN.
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=17187687; DOI=10.1186/1472-6807-6-27;
RA   Saikatendu K.S., Zhang X., Kinch L., Leybourne M., Grishin N.V., Zhang H.;
RT   "Structure of a conserved hypothetical protein SA1388 from S. aureus
RT   reveals a capped hexameric toroid with two PII domain lids and a dinuclear
RT   metal center.";
RL   BMC Struct. Biol. 6:27-27(2006).
CC   -!- SUBUNIT: Toroid-shaped homohexamer that has a central cavity of about
CC       38 Angstroms diameter. {ECO:0000269|PubMed:17187687}.
CC   -!- DOMAIN: Is organized into three distinct structural domains with
CC       interconnecting topological connectivities. The two NIF3 domains at the
CC       N- and C-terminus of the protein have the same overall fold as
CC       canonical NIF3-like proteins. The middle region of the polypeptide
CC       (residues 126-236) bulges out between the two NIF3 domains and is
CC       structured as a classical PII-like fold. The two entries to the central
CC       hollow space are capped by the two PII-like domain trimers. The
CC       trimeric PII domain may play a ligand induced signaling role and
CC       probably regulates the function of the NIF3-like domains.
CC       {ECO:0000269|PubMed:17187687}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC       {ECO:0000305}.
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DR   EMBL; BA000017; BAB57721.1; -; Genomic_DNA.
DR   RefSeq; WP_000683940.1; NC_002758.2.
DR   PDB; 2NYD; X-ray; 2.00 A; A/B=1-366.
DR   PDB; 3LNL; X-ray; 2.00 A; A/B=1-366.
DR   PDBsum; 2NYD; -.
DR   PDBsum; 3LNL; -.
DR   AlphaFoldDB; P67272; -.
DR   SMR; P67272; -.
DR   World-2DPAGE; 0002:P67272; -.
DR   PaxDb; P67272; -.
DR   EnsemblBacteria; BAB57721; BAB57721; SAV1559.
DR   KEGG; sav:SAV1559; -.
DR   HOGENOM; CLU_037423_1_0_9; -.
DR   OMA; EVAYDIY; -.
DR   PhylomeDB; P67272; -.
DR   BioCyc; SAUR158878:SAV_RS08395-MON; -.
DR   Proteomes; UP000002481; 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   1: Evidence at protein level;
KW   3D-structure; Metal-binding; Zinc.
FT   CHAIN           1..366
FT                   /note="GTP cyclohydrolase 1 type 2 homolog"
FT                   /id="PRO_0000147328"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:17187687"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:17187687"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:17187687"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:17187687"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:17187687"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:17187687"
SQ   SEQUENCE   366 AA;  41075 MW;  CA7D5FADFD78FFF4 CRC64;
     MKIADLMTLL DHHVPFSTAE SWDNVGLLIG DGDVEVTGVL TALDCTLEVV NEAIEKGYNT
     IISHHPLIFK GVTSLKANGY GLIIRKLIQH DINLIAMHTN LDVNPYGVNM MLAKAMGLKN
     ISIINNQQDV YYKVQTYIPK DNVGPFKDKL SENGLAQEGN YEYCFFESEG RGQFKPVGEA
     NPTIGQIDKI EDVDEVKIEF MIDAYQKSRA EQLIKQYHPY ETPVFDFIEI KQTSLYGLGV
     MAEVDNQMTL EDFAADIKSK LNIPSVRFVG ESNQKIKRIA IIGGSGIGYE YQAVQQGADV
     FVTGDIKHHD ALDAKIHGVN LIDINHYSEY VMKEGLKTLL MNWFNIEKIN IDVEASTINT
     DPFQYI