ID   G6PI_XANCI              Reviewed;         504 AA.
AC   P0A0T1; O68824;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 54.
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   Xanthomonas citri (Xanthomonas campestris pv. citri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=XW47;
RX   PubMed=10584018; DOI=10.1128/aem.65.12.5564-5573.1999;
RA   Tung S.Y., Kuo T.T.;
RT   "Requirement for phosphoglucose isomerase of Xanthomonas campestris in
RT   pathogenesis of citrus canker.";
RL   Appl. Environ. Microbiol. 65:5564-5570(1999).
CC   -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC       to fructose-6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}.
CC   -!- FUNCTION: Required for pathogenicity.
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   -!- INDUCTION: Inhibited by growth in complex medium but induced by culture
CC       in plant extract.
CC   -!- MISCELLANEOUS: Mutation in pgi results in the inability of X.c.citri to
CC       utilize fructose or glycerol as carbon sources, to grow in plant
CC       tissue, and to cause typical canker symptoms.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00473, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC08426.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF054807; AAC08426.1; ALT_INIT; Genomic_DNA.
DR   PIR; T46970; T46970.
DR   RefSeq; WP_011051139.1; NZ_CP059992.1.
DR   AlphaFoldDB; P0A0T1; -.
DR   SMR; P0A0T1; -.
DR   GeneID; 66910936; -.
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   1: Evidence at protein level;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN           1..504
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180771"
FT   ACT_SITE        333
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        364
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        473
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   504 AA;  54454 MW;  03C410C3F8E8A504 CRC64;
     MTQTNGFDAL HAHAQRLRGA AIPALLAAEP ERPTQYARQV GPLYFNFARQ KYDRAALDAL
     FAIARERDLS GAFQRLFRGE QVNVTEQRAA LHTALRGDLT DAPVASEAYA TAEEVRQRMG
     SLIQQLEATD VTDIVSVGIG GSDLGPRLVA DALRAPSGAR FRVHFVSNVD GAAMQRTLAT
     LDPARTAGIL ISKTFGTQET LLNGSILHAW LGGSERLYAV SANPERAAKA FDIAPGRVLP
     MWDWVGGRYS LWSAVGFPIA LAIGFERFEQ LLEGAAQFDA HVLNTPLEEN VAVLHGLTAV
     WNRNLLGSAT HAVMTYDQRL ALLPAYLQQL VMESLGKRVK LDGSAVDSDT VSVWWGGAGT
     DVQHSFFQAL HQGTSVVPAD FIGTVHNDDP YAENHTALMA NVLAQTEALA NGQDSSDPHR
     SYPGGRPSTV ILLDALTPQA LGALISMYEH SVYVQSVMWG INAFDQFGVE LGKQLASQLL
     PALKGESVDV ADPVTRELLN KLRG