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Database: UniProt
Entry: A7TLK0_VANPO
LinkDB: A7TLK0_VANPO
Original site: A7TLK0_VANPO 
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
//
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