ID   UXAB_ECO5E              Reviewed;         483 AA.
AC   B5Z1X8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=ECH74115_2134;
OS   Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=444450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC4115 / EHEC;
RX   PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA   Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
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; CP001164; ACI35444.1; -; Genomic_DNA.
DR   RefSeq; WP_000854633.1; NC_011353.1.
DR   AlphaFoldDB; B5Z1X8; -.
DR   SMR; B5Z1X8; -.
DR   KEGG; ecf:ECH74115_2134; -.
DR   HOGENOM; CLU_027324_1_0_6; -.
DR   OMA; VVIVRPI; -.
DR   UniPathway; UPA00246; -.
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_1000131507"
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;  54808 MW;  AFA4677CF35BC2E0 CRC64;
     MKTLNRRDFP GAQYPERIIQ FGEGNFLRAF VDWQIDLLNE HTDLNSGVVV VRPIETSFPP
     SLSTQDGLYT TIIRGLNEKG EAVSDARLIR SVNREISVYS EYDEFLKLAH NPEMRFVFSN
     TTEAGISYHA GDKFDDAPAV SYPAKLTRLL FERFSHFNGA LDKGWIIIPC ELIDYNGDAL
     RELVLRYAQE WALPEAFIQW LDQANSFCST LVDRIVTGYP RDEVAKLEEE LGYHDGFLDT
     AEHFYLFVIQ GPKSLATELR LDKYPLNVLI VDDIKPYKER KVAILNGAHT ALVPVAFQAG
     LDTVGEAMND AEICAFVEKA IYEEIIPVLD LPRDELESFA SAVTGRFRNP YIKHQLLSIA
     LNGMTKFRTR ILPQLLAGQK ANGTLPARLT FALAALIAFY RGERNGETYP VQDDAHWLER
     YQQLWSQHRD RVIGTQELVA IVLAEKDHWE QDLTQVPGLV EQVANDLDAI LEKGMREAVR
     PLC