G6PI_STAAC
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 03-AUG-2022, entry version 96.
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=SACOL0966;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; 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 EnsemblBacteria; AAW37934; AAW37934; SACOL0966.
DR KEGG; sac:SACOL0966; -.
DR HOGENOM; CLU_037303_0_1_9; -.
DR OMA; CPAYAYG; -.
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; 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 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
