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Database: UniProt
Entry: L2GKG7_VITCO
LinkDB: L2GKG7_VITCO
Original site: L2GKG7_VITCO 
ID   L2GKG7_VITCO            Unreviewed;       342 AA.
AC   L2GKG7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE            EC=5.3.1.9 {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE   Flags: Fragment;
GN   ORFNames=VICG_01619 {ECO:0000313|EMBL:ELA41378.1};
OS   Vittaforma corneae (strain ATCC 50505) (Microsporidian parasite) (Nosema
OS   corneum).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC   Vittaforma.
OX   NCBI_TaxID=993615 {ECO:0000313|EMBL:ELA41378.1, ECO:0000313|Proteomes:UP000011082};
RN   [1] {ECO:0000313|Proteomes:UP000011082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50505 {ECO:0000313|Proteomes:UP000011082};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Didier E., Bowers L., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The genome sequence of Vittaforma corneae strain ATCC 50505.";
RL   Submitted (MAY-2011) 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|RuleBase:RU000612};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC       {ECO:0000256|RuleBase:RU000612}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|RuleBase:RU000612}.
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DR   EMBL; JH370145; ELA41378.1; -; Genomic_DNA.
DR   RefSeq; XP_007605064.1; XM_007605002.1.
DR   AlphaFoldDB; L2GKG7; -.
DR   STRING; 993615.L2GKG7; -.
DR   GeneID; 19882329; -.
DR   VEuPathDB; MicrosporidiaDB:VICG_01619; -.
DR   HOGENOM; CLU_017947_0_0_1; -.
DR   InParanoid; L2GKG7; -.
DR   OrthoDB; 1657888at2759; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000011082; 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; cd05016; SIS_PGI_2; 1.
DR   Gene3D; 1.10.1390.10; -; 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; 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:UP000011082}.
FT   REGION          320..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ELA41378.1"
SQ   SEQUENCE   342 AA;  38617 MW;  3AF6FD0F9CADAA29 CRC64;
     VRVFKKIDVE RTLFIVVSKT FTTVETMENF KLALGLMKSR LNGRFSEEEI CNKHFVAVSS
     NVPETSKYGI QTVFKMWDFV GGRYSLWSAV GLSISLYIGF DNYAGLLKGA SQADKNFFTR
     KLDSVSFRMA VNELFYISRG FNNKCLVCYD SYLELLYKYL QQAEMESNGK HGCKQMIIWG
     GVGTDVQHSF FQLLHQGEQN IYLELLCPVK NISEEETDRS VVENMDMIKR HHLLLATSCL
     AQSRSMLVGK ESEDANHYFA GDKPSVTILY SKLAPEVLGA VLAVYEHKIF VVGTYFNINS
     FDQFGVELGK ALTKELMGEL SGEAPTNPDA STSKLLSFMK KN
//
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