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Database: UniProt
Entry: A0A2C5XKY1_9HYPO
LinkDB: A0A2C5XKY1_9HYPO
Original site: A0A2C5XKY1_9HYPO 
ID   A0A2C5XKY1_9HYPO        Unreviewed;       553 AA.
AC   A0A2C5XKY1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=CDD81_543 {ECO:0000313|EMBL:PHH66018.1};
OS   Ophiocordyceps australis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH66018.1, ECO:0000313|Proteomes:UP000226192};
RN   [1] {ECO:0000313|EMBL:PHH66018.1, ECO:0000313|Proteomes:UP000226192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Map64 {ECO:0000313|EMBL:PHH66018.1,
RC   ECO:0000313|Proteomes:UP000226192};
RA   De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT   "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT   behavioral manipulation genes and a possible major role for enterotoxins.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHH66018.1}.
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DR   EMBL; NJET01000011; PHH66018.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C5XKY1; -.
DR   STRING; 1399860.A0A2C5XKY1; -.
DR   OrthoDB; 1657888at2759; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000226192; 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: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:UP000226192}.
SQ   SEQUENCE   553 AA;  60748 MW;  24F241E755511FDE CRC64;
     MAPANTLPAW AELQAHRDGV GKNFVLKEAF ASDTDRFSRF SRTFTSGGVS ADILFDFSKN
     FLTEETLDLL VKLAEQAGVT RKRDAMFAGD KINFTENRAV YHAALRNVGG WDMKVDGKDV
     MNNPGGVNDV LKHMKQFSDQ VRSGEWKGFT GKKLTTIINI GIGGSDLGPV MVTEALKYYG
     ADDMTLHFVS NIDGTHMSEA LKESDPETTL FLVASKTFTT AETTTNANTA KAWFLEKTGN
     KGEIAKHFVA LSTNEAEVTK FGIDSKNMFG FESWVGGRYS VWSAIGLSVA IYIGYENFHK
     FLGGAHAMDK HFRETPLKEN IPVIGGLLSV WYSDFFQAQT HLVAPFDQYL HRFPAYLQQL
     SMESNGKSIA SDGSSVKYTT GPIVFGEPCT NAQHSFFQLL HQGTKLIPAD FILAAKSHNP
     ISNNLHQKML ASNFFAQAEA LMVGKTDEEV KAEGAAGDLV PHKRFLGNRP TTSILVEGAI
     GPAELGALIV YYEHLTFTEG AIWDINSFDQ WGVELGKVLA KKILKELDEP GKSQGHDGST
     DGLITTFKKY AKI
//
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