ID   G6PI_MYCSM              Reviewed;         549 AA.
AC   P96803;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 91.
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};
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=mc(2)743;
RX   PubMed=9098072; DOI=10.1128/jb.179.8.2724-2730.1997;
RA   Tuckman D., Donnelly R.J., Zhao F.X., Jacobs W.R. Jr., Connell N.D.;
RT   "Interruption of the phosphoglucose isomerase gene results in glucose
RT   auxotrophy in Mycobacterium smegmatis.";
RL   J. Bacteriol. 179:2724-2730(1997).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB52545.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U88433; AAB52545.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; P96803; -.
DR   SMR; P96803; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
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   Gene3D; 1.10.1390.10; -; 1.
DR   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR023096; G6P_Isomerase_C.
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..549
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180676"
FT   ACT_SITE        353
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        384
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        510
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   549 AA;  59673 MW;  EC850980E57EF9BC CRC64;
     MSADITETPA WQALSDHHAE IGDRHLTELF ADDPARGTEL ALTVGDLYID YSKHRVTRRT
     LDLLVDLARA AGLEERRDAM FAGEHINTSE DRAVLHTALR LPRDAKLVVD GQDVVADVHD
     VLDRMGDFTD RLRSGEWTGA TGERITTVVN IGIGGSDLGP VMVYDALRHY ADAGISARFV
     SNVDPADLVA KLDGLEPAKT LFIVASKTFS TLETLTNATA ARRWLTDALG DAAVAKHSSR
     CPPTRSWSTK FGINTDNMFG FWDWVGGRYS VDSAIGLSVM AVIGKERFAE FLAGFHIVDE
     HFRTAPLHQN APALLGLIGL WYSNFFGAQS RAVLPYSNDL SRFAAYLQQL TMESNGKSVR
     ADGTPVSTDT GEIFWGEPGT NGQHAFYQLL HQGTRLVPAD FIGFSQPTDD LPTADGTGSM
     HDLLMSNFFA QTQVLAFGKT ADAIASEGTP ADVVPHKVMP GNRPTTSILA TKLTPSVVGQ
     LIALYEHQVF TEGVIWGIDS FDQWGVELGK TQAKALLPVL TGDKSPAAQS DTSTDALVRR
     YRTERGRPA