ID A0A0E0Y1Q9_ECO1C Unreviewed; 294 AA.
AC A0A0E0Y1Q9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Putative glucose-6-phosphate 1-epimerase {ECO:0000256|PIRNR:PIRNR016020};
DE EC=5.1.3.15 {ECO:0000256|PIRNR:PIRNR016020};
GN OrderedLocusNames=O3K_11060 {ECO:0000313|EMBL:AFS74106.1};
OS Escherichia coli O104:H4 (strain 2011C-3493).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=1133852 {ECO:0000313|EMBL:AFS74106.1, ECO:0000313|Proteomes:UP000006167};
RN [1] {ECO:0000313|EMBL:AFS74106.1, ECO:0000313|Proteomes:UP000006167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2011C-3493 {ECO:0000313|EMBL:AFS74106.1,
RC ECO:0000313|Proteomes:UP000006167};
RX PubMed=23133618; DOI=10.1371/journal.pone.0048228;
RG Threat Characterization Consortium;
RA Ahmed S.A., Awosika J., Baldwin C., Bishop-Lilly K.A., Biswas B.,
RA Broomall S., Chain P.S., Chertkov O., Chokoshvili O., Coyne S.,
RA Davenport K., Detter J.C., Dorman W., Erkkila T.H., Folster J.P.,
RA Frey K.G., George M., Gleasner C., Henry M., Hill K.K., Hubbard K.,
RA Insalaco J., Johnson S., Kitzmiller A., Krepps M., Lo C.C., Luu T.,
RA McNew L.A., Minogue T., Munk C.A., Osborne B., Patel M., Reitenga K.G.,
RA Rosenzweig C.N., Shea A., Shen X., Strockbine N., Tarr C., Teshima H.,
RA van Gieson E., Verratti K., Wolcott M., Xie G., Sozhamannan S.,
RA Gibbons H.S.;
RT "Genomic comparison of Escherichia coli O104:H4 isolates from 2009 and 2011
RT reveals plasmid, and prophage heterogeneity, including Shiga toxin encoding
RT phage stx2.";
RL PLoS ONE 7:E48228-E48228(2012).
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; CP003289; AFS74106.1; -; Genomic_DNA.
DR RefSeq; WP_001299317.1; NC_018658.1.
DR RefSeq; YP_006778907.1; NC_018658.1.
DR AlphaFoldDB; A0A0E0Y1Q9; -.
DR GeneID; 66674333; -.
DR KEGG; esl:O3K_11060; -.
DR PATRIC; fig|1133852.3.peg.2305; -.
DR HOGENOM; CLU_048345_4_1_6; -.
DR Proteomes; UP000006167; Chromosome.
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}.
FT ACT_SITE 164
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 267
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
SQ SEQUENCE 294 AA; 32672 MW; 3AC924E0A435BFCA CRC64;
MIKKIFALPV IEQISPVLSR RKLDELDLIV VDHPQVKASF ALQGAHLLSW KPAGEEEVLW
LSNNTPFKNG VAIRGGVPVC WPWFGPAAQQ GLPAHGFARN LPWTLKSHRE DADGVALTFE
LTQSEETKKF WPHDFTLLAH FRVGKTCEID LESHGEFETT SALHTYFNVG DIAKVSVSGL
GDRFIDKVND AKEDVLTDGI QTFPDRTDRV YLNPQDCSVI NDEALNRIIA VGHQHHLNVV
GWNPGPALSV SMGDMPDDGY KTFVCVETAY ASETQKVTKE KPAHLAQSIR VAKR
//
