ID E2LWQ3_MONPE Unreviewed; 380 AA. AC E2LWQ3; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 12-OCT-2022, entry version 50. DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954}; DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954}; DE Flags: Fragment; GN ORFNames=MPER_11684 {ECO:0000313|EMBL:EEB90148.1}; OS Moniliophthora perniciosa (strain FA553 / isolate CP02) (Witches'-broom OS disease fungus) (Marasmius perniciosus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Agaricales; Marasmiaceae; Moniliophthora. OX NCBI_TaxID=554373 {ECO:0000313|EMBL:EEB90148.1, ECO:0000313|Proteomes:UP000000741}; RN [1] {ECO:0000313|EMBL:EEB90148.1, ECO:0000313|Proteomes:UP000000741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FA553 / isolate CP02 {ECO:0000313|Proteomes:UP000000741}; RX PubMed=19019209; DOI=10.1186/1471-2164-9-548; RA Mondego J.M., Carazzolle M.F., Costa G.G., Formighieri E.F., Parizzi L.P., RA Rincones J., Cotomacci C., Carraro D.M., Cunha A.F., Carrer H., Vidal R.O., RA Estrela R.C., Garcia O., Thomazella D.P., de Oliveira B.V., Pires A.B., RA Rio M.C., Araujo M.R., de Moraes M.H., Castro L.A., Gramacho K.P., RA Goncalves M.S., Neto J.P., Neto A.G., Barbosa L.V., Guiltinan M.J., RA Bailey B.A., Meinhardt L.W., Cascardo J.C., Pereira G.A.; RT "A genome survey of Moniliophthora perniciosa gives new insights into RT Witches' broom disease of cacao."; RL BMC Genomics 9:548-548(2008). CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP- CC alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; CC Evidence={ECO:0000256|ARBA:ARBA00000874}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate CC biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step CC 1/1. {ECO:0000256|ARBA:ARBA00004701}. CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase CC family. {ECO:0000256|ARBA:ARBA00006601}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EEB90148.1}. 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; ABRE01016750; EEB90148.1; -; Genomic_DNA. DR STRING; 554373.E2LWQ3; -. DR EnsemblFungi; EEB90148; EEB90148; MPER_11684. DR KEGG; mpr:MPER_11684; -. DR HOGENOM; CLU_023810_7_2_1; -. DR InParanoid; E2LWQ3; -. DR OMA; EDFTRPD; -. DR UniPathway; UPA00038; UER00491. DR Proteomes; UP000000741; Unassembled WGS sequence. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR017476; UDP-Glc/GDP-Man. DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C. DR InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf. DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer. DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N. DR InterPro; IPR028357; UDPglc_DH_bac. DR InterPro; IPR028356; UDPglc_DH_euk. DR PANTHER; PTHR11374; PTHR11374; 1. DR Pfam; PF00984; UDPG_MGDP_dh; 1. DR Pfam; PF03720; UDPG_MGDP_dh_C; 1. DR Pfam; PF03721; UDPG_MGDP_dh_N; 1. DR PIRSF; PIRSF500134; UDPglc_DH_bac; 1. DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1. DR SMART; SM00984; UDPG_MGDP_dh_C; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF52413; SSF52413; 1. DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1. PE 3: Inferred from homology; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR500134-3}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000000741}. FT DOMAIN 255..371 FT /note="UDPG_MGDP_dh_C" FT /evidence="ECO:0000259|SMART:SM00984" FT ACT_SITE 199 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-1" FT BINDING 14 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 54 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 85..88 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 88 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 143 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 188..192 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 196 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 202 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 262 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 269 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT NON_TER 380 FT /evidence="ECO:0000313|EMBL:EEB90148.1" SQ SEQUENCE 380 AA; 41957 MW; 0D571A13D99D787F CRC64; MYTRGRLIFV SVNTPTKKTG VGAGFAADLN YVELATRRIA AVANTSKIVV EKSTVPCRTA ESMRTILEAN SKPNCRFDIL SNPEFLAEGT AIQDLFKPDR VLIGSLQTPE GIAACKSLSE IYANWVSEDR ILAVGLWSSE LTKLAANAML AQRISSVNAL SAICEATGAN IDEVAHAVGY DSRIGPKFLK ASVGFGGSCF QKDILNLVYL SESCHLPEVA AYWRQVVELN EYQKRRFSKR VVDTLFNTIT GKRIAVLGFA FKADTGDTRE SAAITLIKDF QNERALVNIY DPQVPHDQIW TDLSEASPHL PLETIRKQVT ICGSALEACK NAEAVVISTE WKEFKAIDWE MVYQNMNKPA FVFDGRLLVD AEKLTKIGFK //