ID E8WVV4_GRATM Unreviewed; 297 AA. AC E8WVV4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 51. 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=AciX9_3712 {ECO:0000313|EMBL:ADW70713.1}; OS Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9). OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae; OC Granulicella. OX NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343}; RN [1] {ECO:0000313|Proteomes:UP000000343} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., RA Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M., RA Haggblom M.M., Woyke T.; RT "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9."; RL Submitted (JAN-2011) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002480; ADW70713.1; -; Genomic_DNA. DR RefSeq; WP_013582022.1; NC_015064.1. DR AlphaFoldDB; E8WVV4; -. DR STRING; 1198114.AciX9_3712; -. DR PaxDb; 1198114-AciX9_3712; -. DR KEGG; acm:AciX9_3712; -. DR eggNOG; COG0676; Bacteria. DR HOGENOM; CLU_048345_4_0_0; -. DR OrthoDB; 9790727at2; -. DR Proteomes; UP000000343; 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:UP000000343}. FT ACT_SITE 167 FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1" FT ACT_SITE 269 FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1" SQ SEQUENCE 297 AA; 32133 MW; 26ECB628FBD2B939 CRC64; MNLTELNDHF GLSGVLTFED HNGLTRLQVK TPACTATVYL HGAHLTHWQP TGAQPVLFLS DRSDFAPDKA IRGGIPVCFP WFGPRAGGKP GPSHGFARIQ PWEVAFAALS GENVHLTLTL GPTALSRSLG FDGFRVAYEM VLGKKLTLRL TVANYGEGML KYEEALHTYF SIGEVRRTTI AGLESALFVD KTDGLKEKET PPEALILSGQ TDRVFPENVS STTIGDGPRT ITINKSNSAT TVVWNPWTEG SVTLKDLRPD AWPGFVCVET ANTGEDAITL APNDAHTMQA EITLGKA //