ID   UXAB_ECOSE              Reviewed;         483 AA.
AC   B6IAS4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
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=ECSE_1611;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(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; AP009240; BAG77135.1; -; Genomic_DNA.
DR   RefSeq; WP_000854624.1; NC_011415.1.
DR   AlphaFoldDB; B6IAS4; -.
DR   SMR; B6IAS4; -.
DR   GeneID; 75202151; -.
DR   KEGG; ecy:ECSE_1611; -.
DR   HOGENOM; CLU_027324_1_0_6; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000008199; Chromosome.
DR   GO; GO:0009026; F:tagaturonate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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_1000131511"
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;  54822 MW;  ABF5226CB25CC297 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 AKGTLPARLT FALAALIAFY RGERNGETYP VQDDAHWLER
     YQQLWSQHRD RVIGTQELVA IVLAEKDHWE QDLTQVPGLV EQVANDLDAI LEKGMREAVR
     PLC
//