ID UXAB_KLEP7 Reviewed; 483 AA. AC A6T900; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=Altronate oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00670}; DE EC=1.1.1.58 {ECO:0000255|HAMAP-Rule:MF_00670}; DE AltName: Full=Tagaturonate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00670}; DE AltName: Full=Tagaturonate reductase {ECO:0000255|HAMAP-Rule:MF_00670}; GN Name=uxaB {ECO:0000255|HAMAP-Rule:MF_00670}; GN OrderedLocusNames=KPN78578_16100; ORFNames=KPN_01640; OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=272620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700721 / MGH 78578; RG The Klebsiella pneumonia Genome Sequencing Project; RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-altronate + NAD(+) = H(+) + keto-D-tagaturonate + NADH; CC Xref=Rhea:RHEA:17813, ChEBI:CHEBI:15378, ChEBI:CHEBI:17360, CC ChEBI:CHEBI:17886, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.58; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00670}; CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate CC interconversion. {ECO:0000255|HAMAP-Rule:MF_00670}. CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family. UxaB CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00670}. 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; CP000647; ABR77071.1; -; Genomic_DNA. DR RefSeq; WP_015958391.1; NC_009648.1. DR AlphaFoldDB; A6T900; -. DR SMR; A6T900; -. DR STRING; 272620.KPN_01640; -. DR PaxDb; 272620-KPN_01640; -. DR EnsemblBacteria; ABR77071; ABR77071; KPN_01640. DR KEGG; kpn:KPN_01640; -. DR HOGENOM; CLU_027324_1_0_6; -. DR UniPathway; UPA00246; -. DR Proteomes; UP000000265; Chromosome. DR GO; GO:0009026; F:tagaturonate reductase activity; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00670; Altron_oxidoreduct; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013328; 6PGD_dom2. DR InterPro; IPR023668; Altronate_OxRdtase. DR InterPro; IPR013118; Mannitol_DH_C. DR InterPro; IPR013131; Mannitol_DH_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR30524:SF0; ALTRONATE OXIDOREDUCTASE-RELATED; 1. DR PANTHER; PTHR30524; MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE; 1. DR Pfam; PF01232; Mannitol_dh; 1. DR Pfam; PF08125; Mannitol_dh_C; 1. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 3: Inferred from homology; KW NAD; Oxidoreductase. FT CHAIN 1..483 FT /note="Altronate oxidoreductase" FT /id="PRO_1000044706" FT BINDING 18..29 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00670" SQ SEQUENCE 483 AA; 54042 MW; 41BA1BF5D4B90137 CRC64; MKTLNRRDFP GAQYPDRIIQ FGEGNFLRAF VDWQIDLLNE HTDLNAGIVV VRPIATDFPP SLNTQDGLYT TIIRGLNEQG EAVSDARLIR SVNREISAYA DFDAFLRLAH NPEMRFVFSN TTEAGISYHA GDRFDDAPPV SYPAKLTRLL FERYQHFAGA ADKGWVIIPC ELIDYNGEAL QALVLRYASE WELPQAFITW LTSANTFCST LVDRIVTGYP RDEVAALEAQ TGYKDAFLDT AEHFYLFVIQ GPASLAAELR LDKLPLNVRI VDDIKPYKER KVAILNGAHT ALVPVAFQAG IDTVGEAMND AEICAFVEKA IYDEIIPVLD LPRDELVSFA SAVTGRFRNP YIKHQLLSIA LNGMTKYRTR ILPQLLAGQK AHGALPPRLT FALAALIAFY RGERDGESYP VQDDADWISR YQTLWARHRD GQMSTRELVT AVLSVADHWQ QDLSQTPGLV ELVTADLDAI LTCGMRDAVK PLC //