G6PI_XYLFM
ID G6PI_XYLFM Reviewed; 502 AA.
AC B0U1Q5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Xfasm12_0200;
OS Xylella fastidiosa (strain M12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405440;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12;
RX PubMed=20601474; DOI=10.1128/jb.00651-10;
RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT causing almond leaf scorch disease in California.";
RL J. Bacteriol. 192:4534-4534(2010).
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; CP000941; ACA11233.1; -; Genomic_DNA.
DR RefSeq; WP_004086271.1; NC_010513.1.
DR AlphaFoldDB; B0U1Q5; -.
DR SMR; B0U1Q5; -.
DR KEGG; xfm:Xfasm12_0200; -.
DR HOGENOM; CLU_017947_3_1_6; -.
DR OMA; IGVWYIN; -.
DR OrthoDB; 417261at2; -.
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..502
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000125778"
FT ACT_SITE 331
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 362
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 471
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 502 AA; 54814 MW; 7647061959ECD7C1 CRC64;
MHNGFDALQL HANRLRGVTI PDLLAAELKR PEQYARQVGP LYFNFARQKY DCVALEALFA
LARNHNVTGA FQRMFCGEQV NVTEGRAVLH TALRGDLSGT SVAVAAYTAA AKVRERMYAL
IAGLDASEVT DIVSVGIGGS DLGPRLVVDA LRPISQGRFR VHFVSNVDGA AMRRTLDMLD
PSRTAGILIS KTFGTQETLL NGRILYDWLG GSERLYAVSA NPERAVHAFD IVPTQVLPIW
DWVGGRYSLW SAVGFPIALA IGSQRFEELL AGAAEFDAYA LRVPLEENVA VLHGLTAVWN
RNFLGCATYA VMAYDQRLAL LPAYLQQLVM ESLGKRVKCD GTPVDRDTVP VWWGGVGTDV
QHSFFQALHQ GTNIVPADFI GTIRNDDLYT ENHFALNANL LAQIEVLANG QLSDDPHRVY
PGGNPSTLIL LDALTPQALG GLIAMYEHSV YVQSVIWGIN AFDQFGVELG KHLAVQLLPA
LKGESVEVVD PVTRAVLVRL RG
