ID F4VG23_ECOLX Unreviewed; 301 AA.
AC F4VG23;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Putative glucose-6-phosphate 1-epimerase {ECO:0000256|PIRNR:PIRNR016020};
DE EC=5.1.3.15 {ECO:0000256|PIRNR:PIRNR016020};
GN ORFNames=ECPG_00320 {ECO:0000313|EMBL:EGI45433.1};
OS Escherichia coli H591.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=656408 {ECO:0000313|EMBL:EGI45433.1, ECO:0000313|Proteomes:UP000004681};
RN [1] {ECO:0000313|EMBL:EGI45433.1, ECO:0000313|Proteomes:UP000004681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H591 {ECO:0000313|EMBL:EGI45433.1,
RC ECO:0000313|Proteomes:UP000004681};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Escherichia coli H591.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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; GL884455; EGI45433.1; -; Genomic_DNA.
DR AlphaFoldDB; F4VG23; -.
DR HOGENOM; CLU_048345_4_1_6; -.
DR Proteomes; UP000004681; 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}.
FT ACT_SITE 171
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 274
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
SQ SEQUENCE 301 AA; 33490 MW; 7F697EEA48D79F7D CRC64;
MKLKDCVMIK KIFALPVIEQ ISPVLSRRKL DELDLIVVDH PQVKASFALQ GAHLLSWKPA
GEEEVLWLSN NTPFKNGVAI RGGVPVCWPW FGPAAQQGLP AHGFARNLPW TLKSHREDAD
GVALTFELTQ SEETKKFWPH DFTLLAHFRV GKTCEIDLES HGEFETTSAL HTYFNVGDIA
KVSVSGLGDR FIDKVNDAKE DVLTDGIQTF PDRTDRVYLN PQDCSVINDE ALNRIIAVGH
QHHLNVVGWN PGPALSVSMG DMPDDGYKTF VCVETAYASE TQKVTKEKPA HLAQSIRVAK
R
//
