ID A0A1Y2GKW2_9FUNG Unreviewed; 289 AA.
AC A0A1Y2GKW2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 28-JUN-2023, entry version 15.
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=BCR41DRAFT_354555 {ECO:0000313|EMBL:ORZ14252.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ14252.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ14252.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ14252.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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}.
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:ORZ14252.1}.
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DR EMBL; MCFF01000021; ORZ14252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2GKW2; -.
DR STRING; 64571.A0A1Y2GKW2; -.
DR InParanoid; A0A1Y2GKW2; -.
DR OrthoDB; 915361at2759; -.
DR Proteomes; UP000193648; 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:UP000193648}.
FT ACT_SITE 157
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 264
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
SQ SEQUENCE 289 AA; 31994 MW; 6285388155FEE4EC CRC64;
MPVSHQSNKA TLSHPSGASA EVYLFGATLT SWKVSNKERI FLSAEAVLDE SKAIRGGIPL
VFPVFGKGKA PHITASLPQH GFARISRWKF VNSSDDDQTV TAQFGLDHSM ISDEHRSLWP
FDFSLIYTIK LTADTIETHL KVHNVGDKPF DFNTLLHTYF LIPDESKVRV IGLNGVDYAD
KVLQQSSRQD GEAVIRGEVD RVYANVKSTD IDIHYGADEQ QNGRGIKLSK NGLNDIVVWN
PWIEKSAGMA DFGDEEYHRM ICVEAGQVAE FIALASGDSW EGSQVLSLL
//
