ID A0A066WY11_COLSU Unreviewed; 318 AA.
AC A0A066WY11;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 03-MAY-2023, entry version 31.
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=CSUB01_01412 {ECO:0000313|EMBL:KDN61587.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN61587.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(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}.
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:KDN61587.1}.
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DR EMBL; JMSE01001398; KDN61587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066WY11; -.
DR STRING; 1173701.A0A066WY11; -.
DR eggNOG; KOG1594; Eukaryota.
DR HOGENOM; CLU_048345_1_0_1; -.
DR OMA; TQALHSY; -.
DR OrthoDB; 915361at2759; -.
DR Proteomes; UP000027238; 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:UP000027238}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 293
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
SQ SEQUENCE 318 AA; 33817 MW; A3191E9C7E284141 CRC64;
MVDRPNKPTA LATTPGLPPQ ATVSITHGNS RVEATLPTGE SVEILLHGAT VLSWKSATGA
DRLWLSSSTA LDGSRPVRGG IPLVFPVFGA PSDAHPPTAS LAQHGFARTS RWEFLGKSTS
EGSAGSESSV KLDFGLSSAN LDEETKAKWG YKFGAIYSVS LDRETLSTSM VITNEGDEAF
DCQTLMHTYL RVNDITKVTV QGLDGAPYTD KVDAGAVKTQ SGDVTITSET DRIYTPTGGP
KAPVVVLEDG EPIYSIVRDN LEDVVVWNPW VDKAASIGDF SPDDGYKNML CVEPGAVKGW
QKLEPGDAFE GAQVISVK
//
