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Database: UniProt
Entry: G2XZ45_BOTF4
LinkDB: G2XZ45_BOTF4
Original site: G2XZ45_BOTF4 
ID   G2XZ45_BOTF4            Unreviewed;       324 AA.
AC   G2XZ45;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   03-MAY-2023, entry version 42.
DE   RecName: Full=Glucose-6-phosphate 1-epimerase {ECO:0000256|ARBA:ARBA00012083, ECO:0000256|PIRNR:PIRNR016020};
DE            EC=5.1.3.15 {ECO:0000256|ARBA:ARBA00012083, ECO:0000256|PIRNR:PIRNR016020};
GN   ORFNames=BofuT4_P047500.1 {ECO:0000313|EMBL:CCD45732.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD45732.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- FUNCTION: Catalyzes the interconversion between the alpha and beta
CC       anomers from at least three hexose 6-phosphate sugars (Glc6P, Gal6P,
CC       and Man6P). {ECO:0000256|PIRNR:PIRNR016020}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:16249, ChEBI:CHEBI:58225, ChEBI:CHEBI:58247;
CC         EC=5.1.3.15; Evidence={ECO:0000256|ARBA:ARBA00001096};
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate 1-epimerase family.
CC       {ECO:0000256|ARBA:ARBA00005866, ECO:0000256|PIRNR:PIRNR016020}.
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DR   EMBL; FQ790278; CCD45732.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2XZ45; -.
DR   STRING; 999810.G2XZ45; -.
DR   eggNOG; KOG1594; Eukaryota.
DR   HOGENOM; CLU_048345_2_0_1; -.
DR   InParanoid; G2XZ45; -.
DR   Proteomes; UP000008177; Unplaced contigs.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd09020; D-hex-6-P-epi_like; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR   InterPro; IPR025532; G6P_1-epimerase.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   PANTHER; PTHR11122; APOSPORY-ASSOCIATED PROTEIN C-RELATED; 1.
DR   PANTHER; PTHR11122:SF39; GLUCOSE-6-PHOSPHATE 1-EPIMERASE; 1.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   PIRSF; PIRSF016020; PHexose_mutarotase; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PIRNR:PIRNR016020};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008177}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        191
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT   ACT_SITE        298
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
SQ   SEQUENCE   324 AA;  34861 MW;  FC73664074297F76 CRC64;
     MDRPKKPSAL SATPGLAPHA QINTTHSNSR VSAVLPTGES VEILLYGATI ISWKDAAGTE
     KLWLSEKAAL DGTKAVRGGI PLVFPVFGKV EGEEGKAKGV DTLPQHGFAR NCRWEFLGKS
     TSESSTTKGG DSSVKLDFGL SASNLPDETR KLWGGEFGLI YSVTLGREGL ATSMVVRNEG
     TTAWEFQILM HTYLKIQDIS QISITGLENA TYVDKLTEPI STNTAPTDPL TISAKTDRVY
     TPAGGPSTEI IVSEGGKKKY TVARDNMNQV VVWNPWIDAK DIGDFAPKDG WRTMICVEAG
     SVSGWQKLEA GETWEGGQII TIAN
//
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