ID   G6PI_STAAC              Reviewed;         443 AA.
AC   Q5HHC2;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 101.
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};
GN   OrderedLocusNames=SACOL0966;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000046; AAW37934.1; -; Genomic_DNA.
DR   RefSeq; WP_000148855.1; NC_002951.2.
DR   PDB; 3FF1; X-ray; 1.65 A; A/B=1-443.
DR   PDBsum; 3FF1; -.
DR   AlphaFoldDB; Q5HHC2; -.
DR   SMR; Q5HHC2; -.
DR   KEGG; sac:SACOL0966; -.
DR   HOGENOM; CLU_037303_0_1_9; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   EvolutionaryTrace; Q5HHC2; -.
DR   Proteomes; UP000000530; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN           1..443
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180726"
FT   ACT_SITE        285
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        420
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           17..21
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           24..36
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   TURN            46..49
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           50..53
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           56..72
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   STRAND          74..79
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           82..84
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           86..95
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   STRAND          107..114
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           117..126
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           127..129
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           144..161
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           163..169
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   STRAND          170..174
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           180..188
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   STRAND          191..194
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           201..203
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           208..216
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           221..234
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           240..242
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           244..257
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   STRAND          262..269
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           270..272
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           273..287
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   STRAND          295..300
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           303..306
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           309..314
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   STRAND          319..328
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           345..348
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           353..370
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   STRAND          375..381
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           385..406
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           414..416
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           417..426
FT                   /evidence="ECO:0007829|PDB:3FF1"
FT   HELIX           433..441
FT                   /evidence="ECO:0007829|PDB:3FF1"
SQ   SEQUENCE   443 AA;  49808 MW;  DF9A8E633F8BD099 CRC64;
     MTHIQLDFSK TLEFFGEHEL KQQQEIVKSI HKTIHEGTGA GSDFLGWVDL PVDYDKEEFS
     RIVEASKRIK ENSDVLVVIG IGGSYLGARA AIEMLTSSFR NSNEYPEIVF VGNHLSSTYT
     KELVDYLADK DFSVNVISKS GTTTEPAVAF RLFKQLVEER YGKEEAQKRI FATTDKEKGA
     LKQLATNEGY ETFIVPDDVG GRYSVLTAVG LLPIATAGIN IEAMMIGAAK AREELSSDKL
     EENIAYQYAT IRNILYAKGY TTEMLINYEP SMQYFNEWWK QLFGESEGKD FKGIYPSSAN
     YTTDLHSLGQ YVQEGRRFLF ETVVKVNHPK YDITIEKDSD DLDGLNYLAG KTIDEVNTKA
     FEGTLLAHTD GGVPNMVVNI PQLDEETFGY VVYFFELACA MSGYQLGVNP FNQPGVEAYK
     QNMFALLGKP GFEDLKKELE ERL
//