ID   G6PI_STRPF              Reviewed;         449 AA.
AC   Q1J8N2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 81.
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=MGAS10750_Spy0179;
OS   Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS10750;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABF37129.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000262; ABF37129.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003058262.1; NC_008024.1.
DR   AlphaFoldDB; Q1J8N2; -.
DR   SMR; Q1J8N2; -.
DR   EnsemblBacteria; ABF37129; ABF37129; MGAS10750_Spy0179.
DR   GeneID; 66901677; -.
DR   KEGG; spi:MGAS10750_Spy0179; -.
DR   HOGENOM; CLU_037303_0_1_9; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002434; 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.
FT   CHAIN           1..449
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000252653"
FT   ACT_SITE        291
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   449 AA;  49541 MW;  125735131B6FC88B CRC64;
     MSHITFDYSK VLESFAGQHE IDFLQGQVTE ADKLLREGTG PGSDFLGWLD LPENYDKDEF
     ARILTAAEKI KSDSEVLVVI GIGGSYLGAK AAIDFLNHHF ANLQTAKERK APQILYAGNS
     ISSTYLADLV EYVQDKEFSV NVISKSGTTT EPAIAFRVFK ELLVKKYGQE EANKRIYATT
     DKVKGAVKVE ADANNWETFV VPDNVGGRFS VLTAVGLLPI AASGADITAL MEGANAARKD
     LSSDKISENI AYQYAAVRNV LYRKGYITEI LANYEPSLQY FGEWWKQLAG ESEGKDQKGI
     YPTSANFSTD LHSLGQFIQE GYRNLFETVI RVDKPRKNVI IPELAEDLDG LGYLQGKDVD
     FVNKKATDGV LLAHTDGGVP NMFVTLPAQD EFTLGYTIYF FELAIAVSGY MNAVNPFDQP
     GVEAYKRNMF ALLGKPGFEE LSAELNARL