ID A0A178B7R1_9PLEO Unreviewed; 320 AA.
AC A0A178B7R1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 16.
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=IQ06DRAFT_290264 {ECO:0000313|EMBL:OAL06275.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL06275.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL06275.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL06275.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV441706; OAL06275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178B7R1; -.
DR STRING; 765868.A0A178B7R1; -.
DR InParanoid; A0A178B7R1; -.
DR OrthoDB; 915361at2759; -.
DR Proteomes; UP000077206; 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:UP000077206}.
FT ACT_SITE 189
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
SQ SEQUENCE 320 AA; 34880 MW; CA23E098A9E5E59C CRC64;
MVDRANRPSA LSAPKASAPG AQVDIVGQGG SQKVVATLST GESIEVLLFG ATVTSWKSDG
GKTENLWLSE KADLTGTKAV RGGIPVVFPV FGPPPKSGHA TSSLPQHGFA RASRWEFLGK
SDTEDASESN SVKLDFGLDK SGLSEEARKA WPLDFGLVYS VTLSKGTLQT VMTVRNEGEE
SFEFQFLLHS YWKVQDISKV SVTGLSGTEY VDKVLDATTH QQKDNTLKFT GEVDRVYKAI
PQDTTSILED GKPRFDVIRD NVKDTVTWNP WIEKAKAMGD FSPDDGYKNM VCIEIGAVDD
WQKLEKGEVW EGGQLVKSLL
//
