ID   UXAB_KLEP3              Reviewed;         483 AA.
AC   B5XQU5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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}; OrderedLocusNames=KPK_2739;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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}.
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DR   EMBL; CP000964; ACI08566.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XQU5; -.
DR   SMR; B5XQU5; -.
DR   EnsemblBacteria; ACI08566; ACI08566; KPK_2739.
DR   KEGG; kpe:KPK_2739; -.
DR   HOGENOM; CLU_027324_1_0_6; -.
DR   OMA; VVIVRPI; -.
DR   OrthoDB; 1442117at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000001734; Chromosome.
DR   GO; GO:0009026; F:tagaturonate reductase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1040.10; -; 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   Pfam; PF01232; Mannitol_dh; 1.
DR   Pfam; PF08125; Mannitol_dh_C; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..483
FT                   /note="Altronate oxidoreductase"
FT                   /id="PRO_1000131514"
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;  54393 MW;  2A09B068A2DB14B0 CRC64;
     MKTLNRRDFP GAQYPDRIIQ FGEGNFLRAF VDWQIDLLNE HTDLNAGIVV VRPIATDFPP
     SLSTQDGLYT TIIRGLNEQG EAVSDARLIR SVNREISAYA DFDAFLRLAH NPEMRFVFSN
     TTEAGISYHA GDRFDDAPPV SYPAKLTRLL FERYQHFAGA ADKGWVIIPC ELIDYNGEAL
     QALVLRYAAE WQLPQAFIRW LTSANTFCST LVDRIVTGYP RDEVAALEAQ TGYKDAFLDT
     AEHFYLFVIQ GPASLAAELR LDKLPLNVRI VDDIKPYKER KVAILNGAHT ALVPVAFLAG
     IDTVGEAMND AEICAFVEKA IYDEIIPVLD LPRDELESFA SAVTGRFRNP YIKHQLLSIA
     LNGMTKYRTR ILPQLLAGQQ KSGQLPPRLT FALAALIAFY RGEREGERYP VQDDAEWLAR
     YQTLWARHRD RQMSTRELVT AVLSVEAHWE QDLSQIPGLV EQVTADLDAI LSRGMRDAVQ
     PLC