ID D5BB98_ZUNPS Unreviewed; 401 AA. AC D5BB98; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAR-2024, entry version 68. DE RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096}; DE EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096}; GN OrderedLocusNames=ZPR_4336 {ECO:0000313|EMBL:ADF54638.1}; OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia OS profunda). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Zunongwangia. OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF54638.1, ECO:0000313|Proteomes:UP000001654}; RN [1] {ECO:0000313|EMBL:ADF54638.1, ECO:0000313|Proteomes:UP000001654} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87 RC {ECO:0000313|Proteomes:UP000001654}; RX PubMed=20398413; DOI=10.1186/1471-2164-11-247; RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y., RA Zhou B.C., Yu J., Zhang Y.Z.; RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation RT to the deep-sea environment and ecological role in sedimentary organic RT nitrogen degradation."; RL BMC Genomics 11:247-247(2010). CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucose = beta-D-glucose; Xref=Rhea:RHEA:10264, CC ChEBI:CHEBI:15903, ChEBI:CHEBI:17925; EC=5.1.3.3; CC Evidence={ECO:0000256|PIRNR:PIRNR005096}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism. CC {ECO:0000256|ARBA:ARBA00005028, ECO:0000256|PIRNR:PIRNR005096}. CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the aldose epimerase family. CC {ECO:0000256|ARBA:ARBA00006206, ECO:0000256|PIRNR:PIRNR005096}. 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; CP001650; ADF54638.1; -; Genomic_DNA. DR RefSeq; WP_013073698.1; NC_014041.1. DR AlphaFoldDB; D5BB98; -. DR STRING; 655815.ZPR_4336; -. DR KEGG; zpr:ZPR_4336; -. DR eggNOG; COG2017; Bacteria. DR HOGENOM; CLU_031753_2_0_10; -. DR OrthoDB; 9779408at2; -. DR UniPathway; UPA00242; -. DR Proteomes; UP000001654; Chromosome. DR GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd09019; galactose_mutarotase_like; 1. DR Gene3D; 2.70.98.10; -; 1. DR InterPro; IPR015443; Aldose_1-epimerase. DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase. DR InterPro; IPR011013; Gal_mutarotase_sf_dom. DR InterPro; IPR047215; Galactose_mutarotase-like. DR InterPro; IPR014718; GH-type_carb-bd. DR PANTHER; PTHR10091; ALDOSE-1-EPIMERASE; 1. DR PANTHER; PTHR10091:SF0; GALACTOSE MUTAROTASE; 1. DR Pfam; PF01263; Aldose_epim; 1. DR PIRSF; PIRSF005096; GALM; 1. DR SUPFAM; SSF74650; Galactose mutarotase-like; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|ARBA:ARBA00022837}; KW Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR005096}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}. FT ACT_SITE 218 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1" FT ACT_SITE 364 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1" FT BINDING 121..122 FT /ligand="beta-D-galactose" FT /ligand_id="ChEBI:CHEBI:27667" FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3" FT BINDING 290 FT /ligand="beta-D-galactose" FT /ligand_id="ChEBI:CHEBI:27667" FT /evidence="ECO:0000256|PIRSR:PIRSR005096-2" SQ SEQUENCE 401 AA; 44400 MW; DA6915FD65288F6B CRC64; MRNVKNTFLA TFLVLLALAC KEKPSEDEKG VAEIADHPEN FYGLEKEKFD TIIDGKEVKL YWIKNDDIAV AFTNYGGRIV GLWVPDKTGK MTDVVVGMNS VSGFANATEP YFGATIGRVG NRIAKGKFTL NGTEYSIPKN NNGNTLHGGN KGFQYVVWEA KQPDDKTLVF TYDSPDMEEG FPGNLEVKVT YSVTDDQSIL MEYEATTDKA TPVNLTNHAF FNLNGEGSGA ILDHKVQIFA NQFTPVDAGL IPSGESKDVK GTPFDFTQAH TIGERIETEN DQLKNGGGYD HNFVLIQDKN ADQQTTKNKG MNHAATFTGD QSGIVMDVYT QEPGVQFYSG NFMQSKNTFK SGVKDDYRTA FALETQHFPD APNQENFPSI ILEPGDTYHT ISEYHFSTTN N //