ID   UXAB_BACTN              Reviewed;         479 AA.
AC   Q8A9J0;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 112.
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=BT_0825;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO75932.1; -; Genomic_DNA.
DR   RefSeq; NP_809738.1; NC_004663.1.
DR   RefSeq; WP_008761512.1; NZ_UYXG01000019.1.
DR   AlphaFoldDB; Q8A9J0; -.
DR   SMR; Q8A9J0; -.
DR   STRING; 226186.BT_0825; -.
DR   PaxDb; 226186-BT_0825; -.
DR   EnsemblBacteria; AAO75932; AAO75932; BT_0825.
DR   GeneID; 60926795; -.
DR   KEGG; bth:BT_0825; -.
DR   PATRIC; fig|226186.12.peg.842; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_027324_1_0_10; -.
DR   InParanoid; Q8A9J0; -.
DR   OrthoDB; 9768714at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0009026; F:tagaturonate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019592; P:mannitol catabolic process; IBA:GO_Central.
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..479
FT                   /note="Altronate oxidoreductase"
FT                   /id="PRO_0000170740"
FT   BINDING         18..29
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00670"
SQ   SEQUENCE   479 AA;  53962 MW;  29F5AFD94429B071 CRC64;
     MKALNKETAP KVQRPERIIQ FGEGNFLRAF VDWIIYNMNQ KTDFNSSVVV VQPIDKGMVD
     MLNAQDDLYH VNLQGLDKGE VVNSLTMIDV ISRALNPYTQ NDEFMKLAEQ PEMRFVISNT
     TEAGIAFDPT CKLEDAPASS YPGKLTQLLY HRFKTFNGDK TKGLIIFPCE LIFLNGHKLK
     ETIYQYIDLW NLGNEFKTWF EEACGVYATL VDRIVPGFPR KDIAAIKEKI QYDDNLVVQA
     EIFHLWVIEA PQEVAKEFPA DKAGLNVLFV PSEAPYHERK VTLLNGPHTV LSPVAYLSGV
     NIVRDACQHE VIGKYIHKVM FDELMETLNL PKEELKKFAE DVLERFNNPF VDHAVTSIML
     NSFPKYETRD LPGLKTYLER KGELPKGLVL GLAAIITYYK GGVRADGAEI VPNDAPEIMN
     LLKELWATGC TKKVTEGVLA AEFIWGEDLN KIPGLAAAVK ADLDSIQEKG MLETVKGIL
//