(data stored in ACNUC9543 zone)

SWISSPROT: G6PI_YERPA

ID   G6PI_YERPA              Reviewed;         548 AA.
AC   Q1CC27;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, entry version 72.
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};
GN   OrderedLocusNames=YPA_0026;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-glucose 6-phosphate = keto-D-fructose 6-
CC         phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57579,
CC         ChEBI:CHEBI:57584; EC=5.3.1.9; Evidence={ECO:0000255|HAMAP-
CC         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}.
DR   EMBL; CP000308; ABG11995.1; -; Genomic_DNA.
DR   RefSeq; WP_002212085.1; NZ_CP009906.1.
DR   SMR; Q1CC27; -.
DR   PRIDE; Q1CC27; -.
DR   EnsemblBacteria; ABG11995; ABG11995; YPA_0026.
DR   KEGG; ypa:YPA_0026; -.
DR   HOGENOM; HOG000261370; -.
DR   KO; K01810; -.
DR   OMA; TNSQHAF; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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   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;
DR   PRODOM; Q1CC27.
DR   SWISS-2DPAGE; Q1CC27.
KW   Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN         1    548       Glucose-6-phosphate isomerase.
FT                                /FTId=PRO_1000014032.
FT   ACT_SITE    355    355       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00473}.
FT   ACT_SITE    386    386       {ECO:0000255|HAMAP-Rule:MF_00473}.
FT   ACT_SITE    514    514       {ECO:0000255|HAMAP-Rule:MF_00473}.
SQ   SEQUENCE   548 AA;  61161 MW;  3ED9D49B3A308A3B CRC64;
     MKNINPSQTA AWKALQQHFE QMKDVTISSL FAKDDQRFNR FSATFDDQML VDFSKNRITS
     ETLEKLQDLA KETDLAGAIK SMFSGEKINR TEDRAVLHIA LRNRSNTPIV VDGKDVMPEV
     NAVLAKMKQF CDRVISGDWK GYTGKAITDV VNIGIGGSDL GPYMVTEALR PYKNHLNMHF
     VSNVDGTHIA EALKPLNPET TLFLVASKTF TTQETMTNAH SARDWFLSAA GDPAHVAKHF
     AALSTNAKAV GEFGIDTNNM FEFWDWVGGR YSLWSAIGLS IALSVGFEHF EQLLSGAHAM
     DKHFAETPAE KNLPVLLALI GIWYNNFFGA ETEAILPYDQ YMHRFPAYFQ QGNMESNGKY
     VDRNGHPVDY QTGPIIWGEP GTNGQHAFYQ LIHQGTKLIP CDFIAPAISH NPLSDHHAKL
     LSNFFAQTEA LAFGKSLEDV EAEFAAAGKT PEQVAHVAPF KVFEGNRPTN SILLREITPF
     SLGALIALYE HKIFTQGVIL NIYTFDQWGV ELGKQLANRI LPELADDQEV TSHDSSTNAL
     INRFKNWR
//

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