GCH1L_STAEQ
ID GCH1L_STAEQ Reviewed; 366 AA.
AC Q5HNY9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN OrderedLocusNames=SERP1125;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
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}.
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DR EMBL; CP000029; AAW54538.1; -; Genomic_DNA.
DR RefSeq; WP_001831093.1; NC_002976.3.
DR AlphaFoldDB; Q5HNY9; -.
DR SMR; Q5HNY9; -.
DR STRING; 176279.SERP1125; -.
DR EnsemblBacteria; AAW54538; AAW54538; SERP1125.
DR GeneID; 50018638; -.
DR KEGG; ser:SERP1125; -.
DR eggNOG; COG0327; Bacteria.
DR HOGENOM; CLU_037423_1_0_9; -.
DR OMA; EVAYDIY; -.
DR OrthoDB; 502462at2; -.
DR Proteomes; UP000000531; 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; Reference proteome.
FT CHAIN 1..366
FT /note="GTP cyclohydrolase 1 type 2 homolog"
FT /id="PRO_0000147334"
FT BINDING 64
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67272"
FT BINDING 65
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67272"
FT BINDING 102
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67272"
FT BINDING 326
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67272"
FT BINDING 329
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67272"
FT BINDING 329
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67272"
SQ SEQUENCE 366 AA; 41697 MW; BC8066BF05664D71 CRC64;
MKISELMEVL NNHVPFHQAE SWDNVGLLIG NDKLDITGIL TTLDCTDDVV NQAIELNTNT
IIAHHPLIFK GVKRIVEDGY GSIIRKLIQN NINLIALHTN LDVNPKGVNR MLADQIGLEN
ISMINTNSSY YYKVQTFIPK NYIEDFKDSL NELGLAKEGN YEYCFFESEG KGQFKPVGDA
SPYIGKLDSI EYVDEIKLEF MIKDNELEIT KRAILDNHPY ETPVFDFIKM NKESEYGLGI
IGQLNQTMTL DEFSEYAKKQ LNIPSVRYTG QHDSPIKKVA IIGGSGIGFE YKASQLGADV
FVTGDIKHHD ALDAKIQNVN LLDINHYSEY VMKEGLKELL EKWLFKYENQ FPIYASEINT
DPFKYK
