ID   G6PI_LEGPN              Reviewed;         497 AA.
AC   Q9RDY2;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 80.
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;
OS   Legionella pneumophila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=446;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43109 / NCTC 12008 / RC1 / Olda / Serogroup 1;
RX   PubMed=11043980; DOI=10.1016/s1438-4221(00)80104-6;
RA   Lueneberg E., Zetzmann N., Hartmann M., Knirel Y.A., Kooistra O.,
RA   Zaehringer U., Helbig J., Frosch M.;
RT   "Cloning and functional characterization of a 30 kb gene locus required for
RT   lipopolysaccharide biosynthesis in Legionella pneumophila.";
RL   Int. J. Med. Microbiol. 290:37-49(2000).
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}.
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DR   EMBL; AJ007311; CAB65205.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RDY2; -.
DR   SMR; Q9RDY2; -.
DR   STRING; 91892.BIZ52_04115; -.
DR   eggNOG; COG0166; Bacteria.
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   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   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN           1..497
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180661"
FT   ACT_SITE        350
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        485
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   497 AA;  56092 MW;  8CDA94027718310C CRC64;
     MIRNSMKSHT ELLSWNLLQK EADRVRLNSD SLTCVVPDSN NYESSKQINC IEYDYSRQRV
     NRTIIDLLID LANEVKLQEK IDNLINGKKI NISENRPALH TALRDLGNKS IMIDGLDIMS
     AVINTREKIK VISNQIREKK WLGHSGLPIT DIVNIGIGGS DLGPRVCINA LSNYISKEFN
     YHFISDVDPA SFNDVIAKIN PQTTLFIVSS KSFTTKETLL NARKAFALYE DTASIDQHFI
     AVTAHPERAY QMGIKTVLPI WDWVGGRFSF CSAVNLITAI AIGYEQFVEL LAGAHDIDTH
     VQFTDFKNNI PVLMALIGIW NNNFLNIHYD LIGYNFKEYF VPYVQQLDME SNGKSIDVNG
     RMVDYATGPI VWGGLGNQAQ HSYFQLLCQG THRCVGDFIT LKTNDEHEIN SMCHYKMKVL
     SEGIQTIENP YGYIPGNMPM NHLILSDCSP YTLGALVALY EHKIFEQSVI WNINPFDQPG
     IESAKSAHRE ITLSSES
//