ID A2SKQ8_METPP Unreviewed; 276 AA.
AC A2SKQ8;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
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=Mpe_A3194 {ECO:0000313|EMBL:ABM96147.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM96147.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM96147.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM96147.1; -; Genomic_DNA.
DR RefSeq; WP_011830770.1; NC_008825.1.
DR AlphaFoldDB; A2SKQ8; -.
DR STRING; 420662.Mpe_A3194; -.
DR KEGG; mpt:Mpe_A3194; -.
DR eggNOG; COG0676; Bacteria.
DR HOGENOM; CLU_048345_2_0_4; -.
DR Proteomes; UP000000366; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000366}.
FT ACT_SITE 151
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 252
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
SQ SEQUENCE 276 AA; 30235 MW; 1CA70B8AFAFF8D9B CRC64;
MAMTEVLGQA AVVLRTADGA EATVLLHGAH VVSWRPAGLP EQLYLSPRAQ AGPGQAVRGG
IPVIFPQFER RGPLPRHGFA RDRAWTLVEH GPQRQHTQAV LSLTDTDATR AVWPHAFEAE
LTVSLSGRAL EMELAVLNTG DRAFEFTAAL HTYLRCDDVR EARVSGLLGG DFEDSLRGTT
HRQEIEPQAI VGEIDRIYWN VVSPVVLQAP QRRVSISAEG FPDRVLWNPG AEKAAAMADL
PDDDWLQMLC IETACIGRPV PLAAGQEWFA RQTLQA
//
