GCH1L_STAES
ID GCH1L_STAES Reviewed; 366 AA.
AC Q8CSD9;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN OrderedLocusNames=SE_1246;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04845.1; -; Genomic_DNA.
DR RefSeq; NP_764801.1; NC_004461.1.
DR RefSeq; WP_002485076.1; NZ_WBME01000008.1.
DR AlphaFoldDB; Q8CSD9; -.
DR SMR; Q8CSD9; -.
DR STRING; 176280.SE_1246; -.
DR EnsemblBacteria; AAO04845; AAO04845; SE_1246.
DR KEGG; sep:SE_1246; -.
DR PATRIC; fig|176280.10.peg.1214; -.
DR eggNOG; COG0327; Bacteria.
DR HOGENOM; CLU_037423_1_0_9; -.
DR OMA; EVAYDIY; -.
DR Proteomes; UP000001411; 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.
FT CHAIN 1..366
FT /note="GTP cyclohydrolase 1 type 2 homolog"
FT /id="PRO_0000147333"
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; 41639 MW; BF73A88EE77462A1 CRC64;
MKISELMEVL NNHVPFHQAE SWDNVGLLIG NDKLDITGIL TTLDCTDDVV NQAIELNTNT
IIAHHPLIFK GVKRIVEDGY GSIIRKLIQN NINLIALHTN LDVNPKGVNR MLADQIGLEN
ISMINTNSSY YYKVQTFIPK NYIEDFKDSL NELGLAKEGN YEYCFFESEG KGQFKPVGDA
SPYIGKLDSI EYVDEIKLEF MIKGNELEIT KRAILDNHPY ETPVFDFIKM NKESEYGLGI
IGQLNQTMTL DEFSEYAKKQ LNIPSVRYTG QHDSPIKKVA IIGGSGIGFE YKASQLGADV
FVTGDIKHHD ALDAKIQNVN LLDINHYSEY VMKEGLKELL EKWLFKYENQ FPIYASEINT
DPFKYK
