ID G6PI_CAMJE Reviewed; 406 AA.
AC Q9PMD4; Q0P890;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473}; OrderedLocusNames=Cj1535c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Campylobacterota; 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 -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00473};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473, ECO:0000305}.
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DR EMBL; AL111168; CAL35635.1; -; Genomic_DNA.
DR PIR; E81300; E81300.
DR RefSeq; WP_002855462.1; NZ_SZUC01000003.1.
DR RefSeq; YP_002344907.1; NC_002163.1.
DR AlphaFoldDB; Q9PMD4; -.
DR SMR; Q9PMD4; -.
DR IntAct; Q9PMD4; 47.
DR STRING; 192222.Cj1535c; -.
DR PaxDb; 192222-Cj1535c; -.
DR EnsemblBacteria; CAL35635; CAL35635; Cj1535c.
DR GeneID; 905817; -.
DR KEGG; cje:Cj1535c; -.
DR PATRIC; fig|192222.6.peg.1512; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_037303_1_0_7; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035476; SIS_PGI_1.
DR InterPro; IPR035482; SIS_PGI_2.
DR PANTHER; PTHR11469; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..406
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180616"
FT ACT_SITE 259
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 284
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 397
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 406 AA; 46013 MW; F5BD432A86E482CE CRC64;
MLNNTLFFKQ SEIHTISSYA NRINDEVKSG DIGYYHLIDT SLNLIDESLQ FIQDKEYVKN
IVLVGMGGSS CGVKALRDML FNEKSNQREL FILDNTSSHS FNKTLEKIKL EESLFLIISK
TGSTIEVVSL FKLLIEHFKL DMQELKKYFV FITDKDSKLH QEGENLGIKC FFIPANVGGR
FSILSAVGIV PLCFCGYNAK ALLEGAKACF EDFFTHKKDE ILQKAYHYCT HKNANINVLF
SYSDAFKGFN EWYIQLIAES LGKKQGYKRI GLTPIALIGA RDQHSFLQLI MDGPKNKTVT
FLKIKDAQKA PIIPDIHFKF LDSLSNKVNL HELLNAQCDA TMHALIAENL SVDVIELEKL
DAWHAGYLMY YYELFTSTCG VMLGINTYDQ PGVEVGKLIL KNILNS
//
