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G6PI_HALSA
ID   G6PI_HALSA              Reviewed;         426 AA.
AC   Q9HNQ6;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=VNG_1992G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(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; AE004437; AAG20164.1; -; Genomic_DNA.
DR   PIR; H84349; H84349.
DR   RefSeq; WP_010903465.1; NC_002607.1.
DR   AlphaFoldDB; Q9HNQ6; -.
DR   SMR; Q9HNQ6; -.
DR   STRING; 64091.VNG_1992G; -.
DR   PaxDb; Q9HNQ6; -.
DR   EnsemblBacteria; AAG20164; AAG20164; VNG_1992G.
DR   GeneID; 5953195; -.
DR   KEGG; hal:VNG_1992G; -.
DR   PATRIC; fig|64091.14.peg.1521; -.
DR   HOGENOM; CLU_037303_1_0_2; -.
DR   InParanoid; Q9HNQ6; -.
DR   OMA; CPAYAYG; -.
DR   OrthoDB; 24853at2157; -.
DR   PhylomeDB; Q9HNQ6; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000554; 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; IBA:GO_Central.
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; 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..426
FT                   /note="Probable glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180779"
FT   ACT_SITE        272
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   426 AA;  44202 MW;  00D4A2C5187D8672 CRC64;
     MRIDIGAALD ATATPGVPPD ALDRLDDRVA HAHDRITAGM DGDEFGYAAL NLPRTVDVDA
     ITAAADAVAD ADTLVTVGIG GSALGAATLV DALGDDDLDY HALDNVDPAH VTRLLDRIDL
     STSAVHVVSR SGTTAETLAN FLVVRDAMDD AGVDWTARTL VTTGDDGPLR ALADTHDLPV
     LDAPRGVPGR FAALSTVALP AAAIAGVDVG ELVAGAADGR AALAGSLEDC SAYAYGATAY
     ALDQRGAGVN AMLPYAERLE TFAEWFAQLW AESLGKDGVG QTPARALGAT DQHSQLQLYR
     AGPRDKLVTM LRPASRPDCA IPEAELADID YLTGGDLGAL LDAEFEATAA SLAASGVPTV
     RVEVPAVDAR SVGRLLFDFE AACVLAGELY GVETFTQPAV EWGKNAAREL LRGEDPLPET
     ETHIVE
 
 
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