ID G6PI_CORGB Reviewed; 540 AA.
AC A4QCJ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=cgR_0966;
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=340322;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R;
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(2007).
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; AP009044; BAF53941.1; -; Genomic_DNA.
DR RefSeq; WP_003858374.1; NC_009342.1.
DR AlphaFoldDB; A4QCJ4; -.
DR SMR; A4QCJ4; -.
DR GeneID; 69621401; -.
DR KEGG; cgt:cgR_0966; -.
DR HOGENOM; CLU_017947_3_1_11; -.
DR PhylomeDB; A4QCJ4; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000006698; 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 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; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 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..540
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000013961"
FT ACT_SITE 351
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 382
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 506
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 540 AA; 59150 MW; E69811F6C9082AE5 CRC64;
MADISTTQAW QDLTDHYSNF QATTLRELFK EENRAEKYTF SAAGLHVDLS KNLLDDATLT
KLLALTEESG LRERIDAMFA GEHLNNTEDR AVLHTALRLP AEADLSVDGQ DVAADVHEVL
GRMRDFATAL RSGNWLGYTG HTIKKIVNIG IGGSDLGPAM ATKALRAYAT AGISAEFVSN
VDPADLVSVL EDLDAESTLF VVASKTFTTQ ETLSNARAAR AWLVEKLGEE AVAKHFVAVS
TNAEKVAEFG IDTDNMFGFW DWVGGRYSVD SAVGLSLMAV IGPRDFMRFL GGFHAMDEHF
RTTKFEENVP ILMALLGVWY SDFYGAETHA VLPYSEDLSR FAAYLQQLTM ESNGKSVHRD
GSPVSTGTGE IYWGEPGTNG QHAFFQLIHQ GTRLVPADFI GFARPKQDLP AGERTMHDLL
MSNFFAQTKV LAFGKNAEEI AAEGVAPELV NHKVMPGNRP TTTILAEELT PSILGALIAL
YEHIVMVQGV IWDINSFDQW GVELGKQQAN DLAPAVSGEE DVDSGDSSTD SLIKWYRANR
//
