GCH1L_CAMJE
ID GCH1L_CAMJE Reviewed; 241 AA.
AC Q9PPK2; Q0PAH4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN OrderedLocusNames=Cj0705;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P0AFP6}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC {ECO:0000305}.
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DR EMBL; AL111168; CAL34842.1; -; Genomic_DNA.
DR PIR; D81341; D81341.
DR RefSeq; WP_002852315.1; NC_002163.1.
DR RefSeq; YP_002344123.1; NC_002163.1.
DR AlphaFoldDB; Q9PPK2; -.
DR SMR; Q9PPK2; -.
DR IntAct; Q9PPK2; 7.
DR STRING; 192222.Cj0705; -.
DR PaxDb; Q9PPK2; -.
DR PRIDE; Q9PPK2; -.
DR EnsemblBacteria; CAL34842; CAL34842; Cj0705.
DR GeneID; 905024; -.
DR KEGG; cje:Cj0705; -.
DR PATRIC; fig|192222.6.peg.697; -.
DR eggNOG; COG0327; Bacteria.
DR HOGENOM; CLU_037423_2_1_7; -.
DR OMA; ISMHTNF; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR002678; DUF34/NIF3.
DR InterPro; IPR036069; DUF34/NIF3_sf.
DR PANTHER; PTHR13799; PTHR13799; 1.
DR Pfam; PF01784; NIF3; 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..241
FT /note="GTP cyclohydrolase 1 type 2 homolog"
FT /id="PRO_0000147300"
FT BINDING 62
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 63
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 101
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 207
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
SQ SEQUENCE 241 AA; 27786 MW; 1574F249905B89EA CRC64;
MKLSEIYNFL DQLSPFNIQE SWDNSGILLG DRDSEISTVY LSLDIDENII KEASENSLII
THHPLIFKGL KDLYDKTYPR AFIKEMIYKN ISLISMHTNY DLSHLNTYFT EEILGFKISF
KDKFLIYVEN SMSFEALCDW VKKKLNLQIL RVSDCGKKDI KRIAICTGSG GDLISKVDAD
CFLSGDFKYH QALEALSNQI SLIDLGHFES ERYFSQCLAK DLKNLPLQVI ITVSKNPFQY
F