G6PI_SALTY
ID G6PI_SALTY Reviewed; 549 AA.
AC Q8ZKI4;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=atbR;
GN OrderedLocusNames=STM4221;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=9573193; DOI=10.1128/jb.180.9.2409-2417.1998;
RA Bearson B.L., Wilson L., Foster J.W.;
RT "A low pH-inducible, PhoPQ-dependent acid tolerance response protects
RT Salmonella typhimurium against inorganic acid stress.";
RL J. Bacteriol. 180:2409-2417(1998).
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 -!- DISRUPTION PHENOTYPE: Increases acid tolerance in rpoS mutants,
CC defective in glucose metabolism. {ECO:0000269|PubMed:9573193}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473}.
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DR EMBL; AE006468; AAL23045.1; -; Genomic_DNA.
DR RefSeq; NP_463086.1; NC_003197.2.
DR RefSeq; WP_000790037.1; NC_003197.2.
DR AlphaFoldDB; Q8ZKI4; -.
DR SMR; Q8ZKI4; -.
DR STRING; 99287.STM4221; -.
DR PaxDb; Q8ZKI4; -.
DR EnsemblBacteria; AAL23045; AAL23045; STM4221.
DR GeneID; 1255747; -.
DR KEGG; stm:STM4221; -.
DR PATRIC; fig|99287.12.peg.4441; -.
DR HOGENOM; CLU_017947_3_1_6; -.
DR OMA; IGVWYIN; -.
DR PhylomeDB; Q8ZKI4; -.
DR BioCyc; SENT99287:STM4221-MON; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..549
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180723"
FT ACT_SITE 355
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 386
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 514
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 549 AA; 61429 MW; 85642951920C4E6C CRC64;
MKNINPTQTS AWQALQKHYD EMKDVTIAEL FANDSDRFAK FSATFDDLML VDFSKNRITE
ETLAKLQDLA KETDLAGAIK SMFSGEKINR TEDRAVLHVA LRNRSNTPII VDGKDVMPEV
NAVLEKMKTF SQAIISGQWK GYTGKAITDV VNIGIGGSDL GPFMVTEALR PYKNHLTMHF
VSNVDGTHIA EVLKKVNPET TLFLVASKTF TTQETMTNAH SARDWFLKTA GDEKHVAKHF
AALSTNAKAV GEFGIDTANM FEFWDWVGGR YSLWSAIGLS IILSVGFDNF VELLSGAHAM
DKHFSTTPAE KNLPILLALI GIWYNNFFGA ETEAILPYDQ YMHRFAAYFQ QGNMESNGKY
VDRNGNAVDY QTGPIIWGEP GTNGQHAFYQ LIHQGTKMVP CDFIAPAITH NPLSDHHQKL
LSNFFAQTEA LAFGKSREVV EQEYRDQGKD PAQLEHVVPF KVFEGNRPTN SILLREITPF
SLGALIALYE HKIFTQGVIL NIFTFDQWGV ELGKQLANRI LPELGDDKAI SSHDSSTNGL
INRYKAWRA
