ID Q8EDI0_SHEON Unreviewed; 282 AA.
AC Q8EDI0;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 101.
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=SO_2769 {ECO:0000313|EMBL:AAN55794.1};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN55794.1, ECO:0000313|Proteomes:UP000008186};
RN [1] {ECO:0000313|EMBL:AAN55794.1, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN55794.1,
RC ECO:0000313|Proteomes:UP000008186};
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN55794.1; -; Genomic_DNA.
DR RefSeq; NP_718350.1; NC_004347.2.
DR RefSeq; WP_011072706.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EDI0; -.
DR STRING; 211586.SO_2769; -.
DR PaxDb; 211586-SO_2769; -.
DR KEGG; son:SO_2769; -.
DR PATRIC; fig|211586.12.peg.2670; -.
DR eggNOG; COG0676; Bacteria.
DR HOGENOM; CLU_048345_4_0_6; -.
DR OrthoDB; 9790727at2; -.
DR PhylomeDB; Q8EDI0; -.
DR BioCyc; SONE211586:G1GMP-2556-MONOMER; -.
DR Proteomes; UP000008186; 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, ECO:0000313|EMBL:AAN55794.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008186}.
FT ACT_SITE 155
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 255
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-2"
SQ SEQUENCE 282 AA; 31708 MW; CE7C68049BD5D2EA CRC64;
MGSVTTKKHA NGLDYVEVNT ALCQARIFLQ GAQIDHFQPV GKPPLLWVSS ADDYQPGNGI
RGGVPVCWPW FGMSSEANFP QHGFARTRVW ALESVEMRNQ LVDLRFSLTI SEEDKVFWPH
NTQVNVLFTL GETLSISLIN TNLGDVPVSL TQALHSYFPI EDIHQLKATG FSGAQYIEFA
KGPYPQTTDD VLFDRETDRV YTNLGPVQHL HTPKGIIEVS RENSRSAVLW NPWIEKSTRL
ARFNDNDYLT MVCLEAANVL EDKLTLAPGE SHSLITHIRW AD
//
