ID A0A2N5TU63_9BASI Unreviewed; 257 AA.
AC A0A2N5TU63;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE RecName: Full=glucose-6-phosphate 1-epimerase {ECO:0000256|ARBA:ARBA00012083};
DE EC=5.1.3.15 {ECO:0000256|ARBA:ARBA00012083};
DE Flags: Fragment;
GN ORFNames=PCANC_24027 {ECO:0000313|EMBL:PLW29043.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW29043.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|EMBL:PLW29043.1, ECO:0000313|Proteomes:UP000235388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW29043.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PLW29043.1}.
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DR EMBL; PGCJ01000423; PLW29043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5TU63; -.
DR STRING; 200324.A0A2N5TU63; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IEA:UniProtKB-EC.
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 Reference proteome {ECO:0000313|Proteomes:UP000235388}.
FT ACT_SITE 125
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 232
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PLW29043.1"
SQ SEQUENCE 257 AA; 28026 MW; E2A13345E4788392 CRC64;
SWKVAGQEQL FLSSASSISG PAAIRGGIPI CFPVFGPPPP REPYSSLKQH GFARNTIWSF
DGVEQGNEWI EARFRLSSNN PEVQKVFKPA FECVYKVKIC ERSLLTSLEV TNPSDTSLEI
QALLHTYLRL PAQGLPQDVT LGALKGLSFA DKVAGGAVGT EERSAVDFLA GEVDRVYTNV
PAEINVDLGH GKRISIKTSG LPDLTVWNPH EAKSNAMADM ESEGWKRFVC IEPGQTTFVS
LEPKASWTGS QELIAHL
//
