ID K9FLQ5_PEND2 Unreviewed; 319 AA.
AC K9FLQ5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 03-MAY-2023, entry version 30.
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=PDIG_63500 {ECO:0000313|EMBL:EKV09217.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV09217.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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:EKV09217.1}.
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DR EMBL; AKCT01000245; EKV09217.1; -; Genomic_DNA.
DR AlphaFoldDB; K9FLQ5; -.
DR STRING; 1170229.K9FLQ5; -.
DR eggNOG; KOG1594; Eukaryota.
DR HOGENOM; CLU_048345_2_0_1; -.
DR InParanoid; K9FLQ5; -.
DR OMA; TQALHSY; -.
DR OrthoDB; 915361at2759; -.
DR Proteomes; UP000009882; 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:UP000009882}.
FT ACT_SITE 185
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 293
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
SQ SEQUENCE 319 AA; 34901 MW; B71639FF677FDF7C CRC64;
MDRSNKPSAI GVGASLPQPT LSIKDNIIEA SLPTGQSVTV HLYGATVTSW KTGGQEQLFV
SEKSHLDGSK PIRGGIPLVF PVFGPPPQNH VTSPLPQHGF ARNSNWEFLG KSSSEAPGRD
SDQTDLAVKL DFGLSHSMLT DEFRAAWPYE FGLVYSVTLT TDSLETSLQV RNEGQQNFEF
QVLMHTYLRI AEISDVCVKG LESKTYIDKT LQATSHTESS PALAITQETD RIYQQLDPTV
PIVVASLKDD QPLFSVTREG LTDVVVWNPW IEKAQGMADF GPDEAYKNMI CVEAGSVSGW
QTLEAGEAWE GGQSIKSRL
//
