ID   G6PI_CORK4              Reviewed;         556 AA.
AC   C4LHE0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, 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=ckrop_0469;
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS   CCUG 35717).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=645127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717;
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA   Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium that
RT   lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(2008).
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; CP001620; ACR17245.1; -; Genomic_DNA.
DR   RefSeq; WP_012731133.1; NC_012704.1.
DR   AlphaFoldDB; C4LHE0; -.
DR   SMR; C4LHE0; -.
DR   STRING; 645127.ckrop_0469; -.
DR   KEGG; ckp:ckrop_0469; -.
DR   eggNOG; COG0166; Bacteria.
DR   HOGENOM; CLU_017947_3_1_11; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001473; 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; Reference proteome.
FT   CHAIN           1..556
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_1000206360"
FT   ACT_SITE        364
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        395
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        521
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   556 AA;  60426 MW;  0C48E2A6EDA6024A CRC64;
     MNSPLPDITA TDEWSALKDN AKSIESTTLR DLFANDQDRA KNLSFSVADL HVDLSKNLIN
     DDTLTALIAL AKKADLEDHR EAMFSGRHIN STEDRAVLHT ALRLPAEESL HVDEQNVAAD
     VHDVLARMRD FAHALRSGEW LGVTGHTIKT VVNIGIGGSD LGPAMTTQAL RSFATAGISG
     RFVSNVDPAD FTSKVADLDP AETLFVVASK TFTTQETLAN AHAARRWFLD SLHLEDGTDE
     ANDAIAKHFV AVSTNAEKVS EFGIDTNNMF GFWDWVGGRY SVDSAIGLSL MAVVGPQNFM
     SFLEGFHAVD EHFRNTPLEK NVPVLMGLLG VWYDDFLGAQ SHAVLPYSQD LARFPAYLQQ
     LTMESNGKSV RIDGTPVTAP TGEIYWGEPG TNGQHAFFQL LHQGTQLVPA DFIGFATPND
     DLPTADGTGS MHDLLMSNFF AQTKVLAFGK TADEITAEGV DPSIVPHKVM PGNRPTTTIL
     APALTPSVLG QLIALYEHIV FTEGTIWSIN SFDQWGVELG KKQAGELLPA VTGEKGVDTG
     DASTDSLISW YRENRK
//