ID   G6PI_METJA              Reviewed;         401 AA.
AC   Q59000;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=MJ1605;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   FUNCTION AS A GLUCOSE-6-PHOSPHATE ISOMERASE, BIOPHYSICOCHEMICAL PROPERTIES,
RP   ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=14655001; DOI=10.1007/s00203-003-0626-4;
RA   Rudolph B., Hansen T., Schonheit P.;
RT   "Glucose-6-phosphate isomerase from the hyperthermophilic archaeon
RT   Methanococcus jannaschii: characterization of the first archaeal member of
RT   the phosphoglucose isomerase superfamily.";
RL   Arch. Microbiol. 181:82-87(2004).
RN   [3]
RP   FUNCTION AS A GLUCOSE-6-PHOSPHATE ISOMERASE.
RX   PubMed=17014089; DOI=10.1021/bi061018a;
RA   White R.H., Xu H.;
RT   "Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5-
RT   ketofructose-1-phosphate: a precursor for aromatic amino acid biosynthesis
RT   in Methanocaldococcus jannaschii.";
RL   Biochemistry 45:12366-12379(2006).
CC   -!- FUNCTION: Catalyzes the isomerization of glucose-6-P to fructose-6-P.
CC       {ECO:0000269|PubMed:14655001, ECO:0000269|PubMed:17014089}.
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   -!- ACTIVITY REGULATION: Competively inhibited by 6-phosphogluconate and
CC       erythrose 4-phosphate. {ECO:0000269|PubMed:14655001}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.04 mM for F6P (at pH 6.3 and 50 degrees Celsius)
CC         {ECO:0000269|PubMed:14655001};
CC         KM=1 mM for G6P (at pH 6.3 and 50 degrees Celsius)
CC         {ECO:0000269|PubMed:14655001};
CC         Vmax=9 umol/min/mg enzyme for G6P (at pH 6.3 and 50 degrees Celsius)
CC         {ECO:0000269|PubMed:14655001};
CC         Vmax=21 umol/min/mg enzyme for F6P (at pH 6.3 and 50 degrees Celsius)
CC         {ECO:0000269|PubMed:14655001};
CC       pH dependence:
CC         Optimum pH is 6.3. 50% remaining activity is observed at pH 5.3 and
CC         pH 7. {ECO:0000269|PubMed:14655001};
CC       Temperature dependence:
CC         Optimum temperature is 89 degrees Celsius. It does not lose activity
CC         upon incubation at 80 degrees Celsius for about 120 min and still has
CC         a half-life at 95 degrees Celsius of 40 min. At 100 degrees Celsius,
CC         an almost complete loss of activity is observed after 30 min.
CC         {ECO:0000269|PubMed:14655001};
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   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14655001}.
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; L77117; AAB99624.1; -; Genomic_DNA.
DR   PIR; D64500; D64500.
DR   RefSeq; WP_010871130.1; NC_000909.1.
DR   AlphaFoldDB; Q59000; -.
DR   SMR; Q59000; -.
DR   STRING; 243232.MJ_1605; -.
DR   EnsemblBacteria; AAB99624; AAB99624; MJ_1605.
DR   GeneID; 1452514; -.
DR   KEGG; mja:MJ_1605; -.
DR   eggNOG; arCOG00052; Archaea.
DR   HOGENOM; CLU_037303_1_0_2; -.
DR   InParanoid; Q59000; -.
DR   OMA; CPAYAYG; -.
DR   OrthoDB; 24853at2157; -.
DR   PhylomeDB; Q59000; -.
DR   SABIO-RK; Q59000; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IDA:UniProtKB.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; PTHR11469; 1.
DR   Pfam; PF00342; PGI; 1.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   SUPFAM; SSF53697; SSF53697; 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   1: Evidence at protein level;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..401
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180780"
FT   ACT_SITE        261
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        392
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   401 AA;  45675 MW;  D5B766A9F2230ED9 CRC64;
     MLSYDYENAL KVGEISLEDI NKVDFANAYS NLMEKLDNGV VGFRDVIYDE NLDKYKSLNG
     YENVVVIGMG GSILGTMAIY YAISPFNNNA YFIDNSDPEK TLSILKKVDL NESIIYIISK
     SGNTLETLVN YYLIKKRIEK LNSFKGKLVF ITNGGKLKRE AEKNNYDIFS IPENVPGRFS
     VFTAVGLAPL YSLGVDISKI LEGAREMDKI CQNEDILKNP ALLNGVIHYL YDKRGKDISV
     IMSYVESLKY FGDWYKQLIG ESLGKNKHGI TPLLSIGAKD QHSLLQLYMD GKKDKIITFM
     VAKKYRLDEE IEFEDINDEK ISCRYSDIIR SQQKATEIAL TNNGVPNVRI TLDEINEMAM
     GALLYMYEMQ VGFMGELYNI NAYNQPAVEE EKKICWRLIK Q