GCH1L_STAAC
ID GCH1L_STAAC Reviewed; 366 AA.
AC Q5HFK1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN OrderedLocusNames=SACOL1616;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P67272}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000046; AAW38232.1; -; Genomic_DNA.
DR RefSeq; WP_000683931.1; NC_002951.2.
DR AlphaFoldDB; Q5HFK1; -.
DR SMR; Q5HFK1; -.
DR EnsemblBacteria; AAW38232; AAW38232; SACOL1616.
DR KEGG; sac:SACOL1616; -.
DR HOGENOM; CLU_037423_1_0_9; -.
DR OMA; EVAYDIY; -.
DR Proteomes; UP000000530; 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_0000147327"
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; 7CFA287639D6C97B 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 VMKEGLKALL MNWFNTEKIN LDVEASTINT
DPFQYI