ID   A0A074YJL1_AURPU        Unreviewed;       316 AA.
AC   A0A074YJL1;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   03-MAY-2023, entry version 23.
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=M438DRAFT_291962 {ECO:0000313|EMBL:KEQ87071.1};
OS   Aureobasidium pullulans EXF-150.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ87071.1, ECO:0000313|Proteomes:UP000030706};
RN   [1] {ECO:0000313|EMBL:KEQ87071.1, ECO:0000313|Proteomes:UP000030706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ87071.1,
RC   ECO:0000313|Proteomes:UP000030706};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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; KL584977; KEQ87071.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074YJL1; -.
DR   STRING; 1043002.A0A074YJL1; -.
DR   HOGENOM; CLU_048345_2_0_1; -.
DR   OrthoDB; 915361at2759; -.
DR   Proteomes; UP000030706; Unassembled WGS sequence.
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:UP000030706}.
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
SQ   SEQUENCE   316 AA;  34797 MW;  2B0ADE9AEEB786FB CRC64;
     MVDRAHKPSA LSPSTTGPQP RVNSDGKKVT ASLPSGDSVE VMLYGATVIS WKNNGKENMW
     LSSNANLEGK KAIRGGVPVV FPNFGPAPKN HATSSLPQHG FARISSWEYL GTTSSESGNQ
     GKGSDDSIRL DFGLTPNNLS DDMKKAWPYD FSLQYSVTLS KDGLQTMLNV RNEGDKPFDF
     QTLFHTYFAV PDISKVKVTG LSGIRYIDKI LNATEHDSKG NELRFEGTVD RVYKSFTQDT
     TSILVDDKPR LDVIRDNMQD TVIWNPWKEG AEAIADFEPK DGYKNMVCVE AGAVNGWITL
     EAQDGFEAGQ ILKSYL
//