ID   G6PI_AYWBP              Reviewed;         426 AA.
AC   Q2NJ38;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
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}; OrderedLocusNames=AYWB_438;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AYWB;
RX   PubMed=16672622; DOI=10.1128/jb.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V.,
RA   Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to diverse
RT   environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(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}.
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DR   EMBL; CP000061; ABC65555.1; -; Genomic_DNA.
DR   RefSeq; WP_011412719.1; NC_007716.1.
DR   AlphaFoldDB; Q2NJ38; -.
DR   SMR; Q2NJ38; -.
DR   STRING; 322098.AYWB_438; -.
DR   EnsemblBacteria; ABC65555; ABC65555; AYWB_438.
DR   KEGG; ayw:AYWB_438; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_037303_0_1_14; -.
DR   OMA; CPAYAYG; -.
DR   OrthoDB; 417261at2; -.
DR   PhylomeDB; Q2NJ38; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001934; 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..426
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000252608"
FT   ACT_SITE        282
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        417
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   426 AA;  48652 MW;  78CA0E8CB7D8F3D0 CRC64;
     MLKLNLEGIY NFLDWRKHTQ TYAPQIKSIH QKLHQDKQLK EKYLGWLELP LHFDFKEIEK
     MKQLKNFHPN LDVLVVIGIG GSYLGAKAGI EFLQTPFKKT KPEILFAGHQ VSGNYLTNLL
     HFLKNKNWAI NVISKSGTTL EPALAFRILK KEIEEKYGKQ LAKNRIFVTT DSQKGVLLNL
     ALKEGYQTFV IPDSVGGRFS VFTSVGILPF VFANLDVASM MKGALQSYHD TFQEDLLQNQ
     AYKYALARYL FHTQQNKKME ILVSYEPNLL SFSEWWKQLF AESEGKEEKG LFVGATNNST
     DLHSLGQFIQ EGTKMLFETV LNVSSIKDDC VVPHILNELD NLNYVAGKTY SQINQKILQA
     TRQAHIEGKV PNLEIVIPTL DAYHFGYLAY FFQKACAMSG LLLGINPFNQ HGVEIYKQKM
     FALLKP