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G6PI_NATPD
ID   G6PI_NATPD              Reviewed;         428 AA.
AC   Q3IMS0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Probable 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=NP_4992A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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}.
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DR   EMBL; CR936257; CAI50587.1; -; Genomic_DNA.
DR   RefSeq; WP_011324198.1; NC_007426.1.
DR   AlphaFoldDB; Q3IMS0; -.
DR   SMR; Q3IMS0; -.
DR   STRING; 348780.NP_4992A; -.
DR   EnsemblBacteria; CAI50587; CAI50587; NP_4992A.
DR   GeneID; 3703019; -.
DR   KEGG; nph:NP_4992A; -.
DR   eggNOG; arCOG00052; Archaea.
DR   HOGENOM; CLU_037303_1_0_2; -.
DR   OMA; CPAYAYG; -.
DR   OrthoDB; 24853at2157; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002698; 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; 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   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..428
FT                   /note="Probable glucose-6-phosphate isomerase"
FT                   /id="PRO_0000230944"
FT   ACT_SITE        269
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        401
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   428 AA;  44803 MW;  79194EECAC97C7AE CRC64;
     MNVDFGNALA AEAVTGVSEA SLERLDDRVA DAHDRIEANI EARRFGYASL ALPTDTDPDA
     IYEAVSGFDP EAVLTVGIGG SALGAETITA ALGAESHYTL DNVDPAPTRQ LLDELPLSST
     LVNVVSRSGT TAETLANFLV VREAMADAGV DWTDRTVVTT GAEGPLRTLA DAHDLPSCTV
     PEGVPGRFSA LSAVGLLPAA ALGCDIEAVL AGGAAGRESL APSLFESPAY AYGAVAYATE
     QRGATTNAIV PYAEQLEPFA EWFAQLWAES LGKDGLGQTP ARALGATDQH SQLQLYRAGR
     KDKLVTLVRP RERAGVDIPE TDIDALSYLG GESLESLLDA EFEATEASLA AAGQPNVRIE
     LDSLDAHGVG ELLYGMEAAC ILYGELLGIE TFTQPAVEWG KRAARGLLGG GDFEEAEAVA
     DKTVRRVE
 
 
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