ID UXAB_CLOAB Reviewed; 482 AA. AC Q97L67; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 16-JUN-2009, entry version 43. DE RecName: Full=Altronate oxidoreductase; DE EC=1.1.1.58; DE AltName: Full=Tagaturonate reductase; DE AltName: Full=Tagaturonate dehydrogenase; GN Name=uxaB; OrderedLocusNames=CA_C0695; OS Clostridium acetobutylicum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX MEDLINE=21359325; PubMed=11466286; RX DOI=10.1128/JB.183.16.4823-4838.2001; RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., RA Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., RA Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., RA Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). CC -!- CATALYTIC ACTIVITY: D-altronate + NAD(+) = D-tagaturonate + NADH. CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate CC interconversion. CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family. UxaB CC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE001437; AAK78672.1; -; Genomic_DNA. DR PIR; E96985; E96985. DR RefSeq; NP_347332.1; -. DR GeneID; 1116878; -. DR GenomeReviews; AE001437_GR; CA_C0695. DR KEGG; cac:CAC0695; -. DR NMPDR; fig|272562.1.peg.861; -. DR HOGENOM; Q97L67; -. DR OMA; Q97L67; SIFPCEL. DR BioCyc; CACE272562:CAC0695-MON; -. DR BRENDA; 1.1.1.58; 2866. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0009026; F:tagaturonate reductase activity; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_00670; -; 1. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR013118; Mannitol_DH_C. DR InterPro; IPR000669; Mannitol_DH_core. DR InterPro; IPR013131; Mannitol_DH_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1. DR Pfam; PF01232; Mannitol_dh; 1. DR Pfam; PF08125; Mannitol_dh_C; 1. DR PRINTS; PR00084; MTLDHDRGNASE. PE 3: Inferred from homology; KW Complete proteome; NAD; Oxidoreductase. FT CHAIN 1 482 Altronate oxidoreductase. FT /FTId=PRO_0000170741. FT NP_BIND 18 29 NAD (By similarity). SQ SEQUENCE 482 AA; 55250 MW; A569F3B18D0919CA CRC64; MKLNRSNFSE FKKYPEKILQ FGEGNFLRAF VDWQVDRMNK AADFNAGVVI VQPLEQGLVD MLNEQDGLYT LYLQGLKEGK AVKEHSVIDC VTRGLNPYTQ YEEYLKLAEN PEMEIVISNT TEAGIAFDEN DKLGRTCQNS YPGKLTAFLY RRFKTFNGDK SKGMLIIPCE LIDRNGEKLK ATILKFAELW NLEKEFADWI EEANTFCCTL VDRIVPGYPR DTIEEVHAEL GYEDSLVDVG EQFHLWVIEG PEWIKDILPF EKAGVNIQVV KDVTPYRTRK VRILNGAHTA LVPVAYLYGL DTVGHSVEDK VIGKYLTELV YDEIIPTLDL PEEELKYFAG AVLERFLNPF VNHYLMSIAL NSMPKFETRD LPSLLEYKKR KGQLPKKLVF SLAALIEFYK GKRGDEDIKL ADGEDILELY KDLWSKFDGT DACYRNIVET VLGYEKNWKM NLNELEGLTD AVTENLIKID KLGMKEAVKS VM //