ID A2C5U6_PROM3 Unreviewed; 324 AA. AC A2C5U6; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 80. DE SubName: Full=Nucleoside-diphosphate-sugar epimerase {ECO:0000313|EMBL:ABM76856.1}; DE EC=4.2.1.46 {ECO:0000313|EMBL:ABM76856.1}; DE EC=4.2.1.47 {ECO:0000313|EMBL:ABM76856.1}; DE EC=5.1.3.2 {ECO:0000313|EMBL:ABM76856.1}; DE EC=5.1.3.7 {ECO:0000313|EMBL:ABM76856.1}; GN OrderedLocusNames=P9303_01011 {ECO:0000313|EMBL:ABM76856.1}; OS Prochlorococcus marinus (strain MIT 9303). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM76856.1, ECO:0000313|Proteomes:UP000002274}; RN [1] {ECO:0000313|EMBL:ABM76856.1, ECO:0000313|Proteomes:UP000002274} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM76856.1, RC ECO:0000313|Proteomes:UP000002274}; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., RA Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000256|ARBA:ARBA00001911}; 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; CP000554; ABM76856.1; -; Genomic_DNA. DR AlphaFoldDB; A2C5U6; -. DR STRING; 59922.P9303_01011; -. DR KEGG; pmf:P9303_01011; -. DR HOGENOM; CLU_007383_1_7_3; -. DR BioCyc; PMAR59922:G1G80-97-MONOMER; -. DR Proteomes; UP000002274; Chromosome. DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro. DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IEA:InterPro. DR GO; GO:0003974; F:UDP-N-acetylglucosamine 4-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0042732; P:D-xylose metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR001509; Epimerase_deHydtase. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR044516; UXS. DR PANTHER; PTHR43078:SF6; UDP-GLUCURONIC ACID DECARBOXYLASE 1; 1. DR PANTHER; PTHR43078; UDP-GLUCURONIC ACID DECARBOXYLASE-RELATED; 1. DR Pfam; PF01370; Epimerase; 1. DR PRINTS; PR01713; NUCEPIMERASE. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 4: Predicted; KW Isomerase {ECO:0000313|EMBL:ABM76856.1}; KW Lyase {ECO:0000313|EMBL:ABM76856.1}. FT DOMAIN 4..237 FT /note="NAD-dependent epimerase/dehydratase" FT /evidence="ECO:0000259|Pfam:PF01370" SQ SEQUENCE 324 AA; 35853 MW; AF82A277BFD69F8D CRC64; MKAVVTGGAG FIGSHLVEQL LELGHSVSII DNYSTGRPEN ISHVINQVTV DQSDLSIRGS WEHLIRESDI IFHLASLADI VPSIENPQLY FHSNVTSTVN IMEVAKERKN RVIYAASSSC YGIPDSYPTA ENAEIRPEYP YALTKWLGEQ IVIHWGKIYN IPVISTRFFN VYGTRSRTSG TYGAVFGVFL AQKLANKPLT IVGNGEQKRD FTYVTDVCNG LIKAALSSVT NSIINIGSGN PQTINYLANL IGGERVFIPQ RPGEPDITHA DITLARELLG YSPKITFEEG VQKVMDSISY WSEAPVWTPE SISRATDSWF KHLS //