ID   G6PI_BIFLO              Reviewed;         566 AA.
AC   Q8G7I6;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
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}; Synonyms=gpi;
GN   OrderedLocusNames=BL0279;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN24120.1; -; Genomic_DNA.
DR   RefSeq; NP_695484.1; NC_004307.2.
DR   RefSeq; WP_011068403.1; NC_004307.2.
DR   AlphaFoldDB; Q8G7I6; -.
DR   SMR; Q8G7I6; -.
DR   STRING; 206672.BL0279; -.
DR   PRIDE; Q8G7I6; -.
DR   EnsemblBacteria; AAN24120; AAN24120; BL0279.
DR   KEGG; blo:BL0279; -.
DR   PATRIC; fig|206672.9.peg.1016; -.
DR   HOGENOM; CLU_017947_3_1_11; -.
DR   OMA; IGVWYIN; -.
DR   PhylomeDB; Q8G7I6; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000439; 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   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; Reference proteome.
FT   CHAIN           1..566
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180600"
FT   ACT_SITE        374
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        405
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        529
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   566 AA;  62998 MW;  A68089F8BAD007B1 CRC64;
     MAINPPVDAT QTPEWAALQK HYDELQVEGV SLKKWFAEDA ERVEKLSFDA GDLHFDLSKN
     LIKPETLQLF ANLAKAVKLD ERTKAMYTGV HINNTEDRAV LHTALRRPVE DEGKYIVDGQ
     DTVKDVRETL DKIYAFADDV RSGKWTGVTG RKIETVVNIG IGGSDLGPVM VYEALKPYAD
     AGISARYISN IDPNDLAEKT KGLDPETTLF IIVSKTFTTL ETLTNAREAR TWLLEELTAN
     GAIAEGDEAQ KAEAIKKHFV AVSTNLEKVE EFGIDPNNAF GFWNWVGGRY SVDSAVGTSL
     AVVFGPARFE EFLHGFHEID EYFANTPFEK NVVVLLGMLN VWYRNFFKVA SHAVLPYDQY
     LHRFPAYLQQ LTMESNGKSV RWDGTPVTSE TGEIFWGEPG TNGQHAFYQL IHQGTQLIPA
     DFIAFVNTPN PTKDGDQDVH ELFLGNYFAQ TKALAFGKTA DEVRAEGTPE EIVPARVFSG
     NRPTTSIFGV ALTPFALGEL IALYEHITFV EGTVWGLDSY DQWGVELGKQ LAKQITPAIS
     QDDDALAAQD ASTQSLIKFY RANREF