ID A0A094HND5_9PEZI Unreviewed; 320 AA.
AC A0A094HND5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 03-MAY-2023, entry version 26.
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=V502_05138 {ECO:0000313|EMBL:KFZ16352.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ16352.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ16352.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFZ16352.1}.
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DR EMBL; JPKE01002001; KFZ16352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094HND5; -.
DR STRING; 1420915.A0A094HND5; -.
DR HOGENOM; CLU_048345_1_1_1; -.
DR OrthoDB; 915361at2759; -.
DR Proteomes; UP000029308; 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:UP000029308}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
SQ SEQUENCE 320 AA; 33863 MW; 1DAF4EA6BCF1D2DB CRC64;
MSSTRPKPNN LSLSATPAQP PASATITHDN GRVTATLPTG ESIAVLLYGA TVVSWKDKGG
EKLWVSEGAD LSGGSAVRGG VPLVFPVFGK STDHPATAAL PQHGFARTSR WEFLGKSTTE
SDGKGGDGGV KLDFGLGPEN LSAEAREAWK GEFGLIYSVA LTRGALRTSM LVRNDGGEAW
DFQVLMHTYL RVKDITTTTV EGLAGAPYFD KVTASTTTAP TSPATLSITG ETDRVYTPAS
VETTLTVSAN GTPAFEIVRE NFENVVVWNP WEEKAKGIKD FAPKDGWKEM LCVEAGQVAG
WTKLEGGDAW EGGVTIKALL
//
