ID A9WF67_CHLAA Unreviewed; 446 AA. AC A9WF67; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 28-JAN-2026, entry version 85. DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124}; DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124}; GN OrderedLocusNames=Caur_2850 {ECO:0000313|EMBL:ABY36051.1}; OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl). OC Bacteria; Bacillati; Chloroflexota; Chloroflexia; Chloroflexales; OC Chloroflexineae; Chloroflexaceae; Chloroflexus. OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY36051.1, ECO:0000313|Proteomes:UP000002008}; RN [1] {ECO:0000313|Proteomes:UP000002008} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl RC {ECO:0000313|Proteomes:UP000002008}; RX PubMed=21714912; DOI=10.1186/1471-2164-12-334; RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J., RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W., RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.; RT "Complete genome sequence of the filamentous anoxygenic phototrophic RT bacterium Chloroflexus aurantiacus."; RL BMC Genomics 12:334-334(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=UDP-alpha-D-glucose + 2 NAD(+) + H2O = UDP-alpha-D-glucuronate CC + 2 NADH + 3 H(+); 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:ARBA00047473, CC ECO:0000256|PIRNR:PIRNR000124}; 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, ECO:0000256|PIRNR:PIRNR000124}. 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; CP000909; ABY36051.1; -; Genomic_DNA. DR RefSeq; WP_012258704.1; NC_010175.1. DR AlphaFoldDB; A9WF67; -. DR FunCoup; A9WF67; 392. DR STRING; 324602.Caur_2850; -. DR EnsemblBacteria; ABY36051; ABY36051; Caur_2850. DR KEGG; cau:Caur_2850; -. DR PATRIC; fig|324602.8.peg.3209; -. DR eggNOG; COG1004; Bacteria. DR HOGENOM; CLU_023810_1_2_0; -. DR InParanoid; A9WF67; -. DR UniPathway; UPA00038; UER00491. DR Proteomes; UP000002008; Chromosome. 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 Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2. 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 NCBIfam; TIGR03026; NDP-sugDHase; 1. DR PANTHER; PTHR43750; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1. DR PANTHER; PTHR43750:SF3; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1. PE 3: Inferred from homology; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000124}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000124}; KW Reference proteome {ECO:0000313|Proteomes:UP000002008}. FT DOMAIN 314..415 FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal" FT /evidence="ECO:0000259|SMART:SM00984" FT ACT_SITE 261 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-1" FT BINDING 36 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 87 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 122 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 153..156 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 156 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 205 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 250..254 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 258 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 264 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 321 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 328 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" SQ SEQUENCE 446 AA; 48882 MW; 5334FB9F9253B7A0 CRC64; MKNICVVGTG YVGLTTGVCF ADLGHSVTCI EIDLHKLELL RSGKSPIFEP GLEELQERNM RAGRLRFTDD YAVGIPDAEF IFITVGTPMG EDGSADLTYV KAAARSIGQY LRSGSIIIDK STVPVGTGDM VENIIAEYAG PDVKFDVVSN PEFLREGSAL SDFFKPDRIV LGAKNREAAQ RVAALHETLG APIIITDLRT AEMIKYASNA FLATRISFIN EIAQICERLG ADVREVARGM GADKRIGPHF LEAGVGYGGS CFPKDVLALY HMAASAGCHP QLLQAVMDIN SDARKRFVKK VETVLGDLEG RVIGVLGLSF KPNTDDMREA PSVDIINSLL KKGARVKAYD PVAMARAEEL LPTVTFTATA YDVAKDADAL LLVTEWNEFK QLDWQRIKRY MRQPVVIDGR NLYDPREMRN LGFIYWGVGR GEAPVPIMEE AQNIGD //