ID A7TLK0_VANPO Unreviewed; 555 AA.
AC A7TLK0;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 03-MAY-2023, entry version 80.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00018388, ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
GN ORFNames=Kpol_1024p40 {ECO:0000313|EMBL:EDO16886.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO16886.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC -!- FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-
CC phosphate to fructose-6-phosphate, the second step in glycolysis, and
CC the reverse reaction during gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00024178}.
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:0000256|ARBA:ARBA00029321,
CC ECO:0000256|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004926, ECO:0000256|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC ECO:0000256|RuleBase:RU000612}.
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DR EMBL; DS480415; EDO16886.1; -; Genomic_DNA.
DR RefSeq; XP_001644744.1; XM_001644694.1.
DR AlphaFoldDB; A7TLK0; -.
DR STRING; 436907.A7TLK0; -.
DR GeneID; 5545070; -.
DR KEGG; vpo:Kpol_1024p40; -.
DR eggNOG; KOG2446; Eukaryota.
DR HOGENOM; CLU_017947_3_1_1; -.
DR InParanoid; A7TLK0; -.
DR OMA; IGVWYIN; -.
DR OrthoDB; 1657888at2759; -.
DR PhylomeDB; A7TLK0; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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 Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW ECO:0000256|RuleBase:RU000612};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612};
KW Reference proteome {ECO:0000313|Proteomes:UP000000267}.
SQ SEQUENCE 555 AA; 61395 MW; EE3EB406ADAEB1A0 CRC64;
MASENTFSNF KLASELPAWT KLQKLYDAQG KTLNVKSEFD SDAKRYEKYS HTFTNYDGSK
ILFDFSKNLV NDEIMQALIE LAKEANVAGL RDEMFAGDHI NFTEDRAVYH VALRNRANRV
MKVDGVNVAP EVDAVLAHMK EFSEEVRSGK WTGYTGKKIT DVVNIGIGGS DLGPVMVTEA
LKHYSGVLDV HFVSNIDGTH LAETLKPLNP ETTLFLVASK TFTTAETITN ATSAKNWFLS
KTGNNPAHIA KHFAALSTNK EEVAKFGIDT KNMFGFESWV GGRYSVWSAI GLSVALYIGY
DNFDDFLKGA EAVDRHFVDT PLEQNIPLLG GLLSVWYNNF HGAQTHLVAP YDQYLHRFPA
YLQQLSMESN GKSVTRGNVF ANYSTGSILF GEPCTNAQHS FFQLVHQGTK LIPTDFIMAA
QSHNPIDDKK HQKMLASNYF AQAEALLVGK DAAKVEAEGA KGGLVPHKVF SGNRPTTSIL
AQKITPATLG ALIAYYEFLT FTEGAIWNIN SFDQWGVELG KVLAKVIVNE LQDTSAVANH
DPSTNALINQ FKQWM
//