ID UXAB_CITK8 Reviewed; 483 AA. AC A8AGR0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 88. 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=CKO_01541; OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=290338; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696; RG The Citrobacter koseri Genome Sequencing Project; RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., RA Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (AUG-2007) 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; CP000822; ABV12673.1; -; Genomic_DNA. DR RefSeq; WP_012132414.1; NC_009792.1. DR AlphaFoldDB; A8AGR0; -. DR SMR; A8AGR0; -. DR STRING; 290338.CKO_01541; -. DR GeneID; 45135605; -. DR KEGG; cko:CKO_01541; -. DR HOGENOM; CLU_027324_1_0_6; -. DR OrthoDB; 9768714at2; -. DR UniPathway; UPA00246; -. DR Proteomes; UP000008148; 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; Reference proteome. FT CHAIN 1..483 FT /note="Altronate oxidoreductase" FT /id="PRO_1000044701" 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; 54486 MW; 6680F00440B36A51 CRC64; MKTLNRRDFP GASYPERIIQ FGEGNFLRAF VDWQVDLLNE HTDLNAGVVI VRPIESTFPP SLSTQDGLYT TIIRGLNEKG EAVSDARLIR SVNREISVYD NYDEFLKLAH NPDMRFVFSN TTEAGISYHA GDAFDDAPAV SYPAKLTRLL FERYTCFDGA LDKGWIIIPC ELIDYNGEAL RELVLRYAQE WNLSAAFVQW LDQANTFCST LVDRIVTGYP RDEVTQLEAE LGYHDAFLDT AEHFYLFVIQ GPKKVASELR LDKYPLNVLI VDDIKPYKER KVAILNGAHT ALVPVAFQAG LDTVGEAMND RDICAFVEKA IYEEIIPVLD LPRDELMSFA SAVTGRFQNP YIKHQLLSIA LNGMTKFRTR ILPQLLAGQQ VSGVLPARLT FALAALTAFY RGERRGETYP LQDDAHWIER YQQLWHQHSD GLISTQDLVH AVLAVDAHWG QNLTHVAGLV EQVTTDLDAI LTKGMREAVK PLC //