GCH1L_STAAS
ID GCH1L_STAAS Reviewed; 366 AA.
AC Q6G907;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN OrderedLocusNames=SAS1497;
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 -!- 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; BX571857; CAG43298.1; -; Genomic_DNA.
DR RefSeq; WP_000683932.1; NC_002953.3.
DR AlphaFoldDB; Q6G907; -.
DR SMR; Q6G907; -.
DR KEGG; sas:SAS1497; -.
DR HOGENOM; CLU_037423_1_0_9; -.
DR OMA; EVAYDIY; -.
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_0000147331"
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