ID L2GW85_VAVCU Unreviewed; 520 AA.
AC L2GW85;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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};
GN ORFNames=VCUG_00833 {ECO:0000313|EMBL:ELA47632.1};
OS Vavraia culicis (isolate floridensis) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC Vavraia.
OX NCBI_TaxID=948595 {ECO:0000313|EMBL:ELA47632.1, ECO:0000313|Proteomes:UP000011081};
RN [1] {ECO:0000313|Proteomes:UP000011081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=floridensis {ECO:0000313|Proteomes:UP000011081};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Becnel J., Sanscrainte N., 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 Vavraia culicis strain floridensis.";
RL Submitted (MAR-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|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; GL877414; ELA47632.1; -; Genomic_DNA.
DR RefSeq; XP_008073853.1; XM_008075662.1.
DR AlphaFoldDB; L2GW85; -.
DR STRING; 948595.L2GW85; -.
DR GeneID; 19878716; -.
DR VEuPathDB; MicrosporidiaDB:VCUG_00833; -.
DR HOGENOM; CLU_017947_3_1_1; -.
DR InParanoid; L2GW85; -.
DR OMA; DWYRQLW; -.
DR OrthoDB; 1657888at2759; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000011081; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011081};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 260..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 520 AA; 59650 MW; 59B9F6F934686764 CRC64;
MVDKNMITLL ELFQNDPHRT EKFILKVEVG DEALHFDYTK THIDTMLLYE LKRNFKNYKG
IKGMFNKEEI NFTEHRKVLH IALRNKKVLE AVERNSDGRN LCEEEQLVFR ELKKMREFEK
KFQKGEITGV TGKRLRNVVN IGIGGSDLGP RMVTDALDFY KKDGVKVFYI SNIDSTGTER
VFKEIDPEET LFIVVSKTFT TLETLANATL ALKLMEERLN VDKREIANKH FVAVSANKDE
VEKFGIKNSF DMWDFVGGRF SLWSAVGLSI VLYIGFTNFL SLLKGASVMD EHFENTMTEK
NVPIMQALIE IYYTNFRKYD SKCIVAYDEY LKDLYSYLQQ AEMESNGKMA TFSGSVSWNT
GMIIWGSVGT SAQHSFFQLL HQGTRRVLVE ILLPLQPLND QKVMDHSHFE MLFANGVAQS
QALMVGTETS NNHKYFGGNR PSITICYTKL TPAVLGALIA FYEHKIFVQG LYWCINSFDQ
FGVELGKKLA KEVLSHIDNE PNDVDASTKN LINMYKSYTK
//
