ID   UXAB_BACSU              Reviewed;         480 AA.
AC   O34354;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
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}; Synonyms=yjmI;
GN   OrderedLocusNames=BSU12380;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE OPERON STRUCTURE.
RC   STRAIN=168;
RX   PubMed=9579062; DOI=10.1099/00221287-144-4-877;
RA   Rivolta C., Soldo B., Lazarevic V., Joris B., Mauel C., Karamata D.;
RT   "A 35.7 kb DNA fragment from the Bacillus subtilis chromosome containing a
RT   putative 12.3 kb operon involved in hexuronate catabolism and a perfectly
RT   symmetrical hypothetical catabolite-responsive element.";
RL   Microbiology 144:877-884(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   PROBABLE OPERON STRUCTURE, AND INDUCTION.
RC   STRAIN=168 / MB24;
RX   PubMed=9882655; DOI=10.1128/jb.181.2.426-433.1999;
RA   Mekjian K.R., Bryan E.M., Beall B.W., Moran C.P. Jr.;
RT   "Regulation of hexuronate utilization in Bacillus subtilis.";
RL   J. Bacteriol. 181:426-433(1999).
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   -!- INDUCTION: Induced by galacturonate, repressed by glucose.
CC       {ECO:0000305|PubMed:9882655}.
CC   -!- MISCELLANEOUS: Member of the exu locus which is required for
CC       galacturonate utilization.
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family. UxaB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00670}.
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DR   EMBL; AF015825; AAC46334.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13095.1; -; Genomic_DNA.
DR   PIR; C69853; C69853.
DR   RefSeq; NP_389120.1; NC_000964.3.
DR   RefSeq; WP_003245710.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O34354; -.
DR   SMR; O34354; -.
DR   STRING; 224308.BSU12380; -.
DR   PaxDb; O34354; -.
DR   EnsemblBacteria; CAB13095; CAB13095; BSU_12380.
DR   GeneID; 936468; -.
DR   KEGG; bsu:BSU12380; -.
DR   PATRIC; fig|224308.179.peg.1339; -.
DR   eggNOG; COG0246; Bacteria.
DR   InParanoid; O34354; -.
DR   OMA; VVIVRPI; -.
DR   PhylomeDB; O34354; -.
DR   BioCyc; BSUB:BSU12380-MON; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000001570; 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; IBA:GO_Central.
DR   GO; GO:0019698; P:D-galacturonate catabolic process; IBA:GO_Central.
DR   GO; GO:0019592; P:mannitol catabolic process; IBA:GO_Central.
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; IPR000669; Mannitol_DH.
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   PRINTS; PR00084; MTLDHDRGNASE.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..480
FT                   /note="Altronate oxidoreductase"
FT                   /id="PRO_0000170739"
FT   BINDING         19..30
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00670"
SQ   SEQUENCE   480 AA;  55361 MW;  DC7DBC8DA500F8D4 CRC64;
     MQKLNKNVYD HYTQYPEKIL QFGEGNFLRG FIDWQIDQLN QHTDFNGSVA VVQPRGSEKI
     KRLNEQDGLY TLFLQGMKDG EAVNEHMIIN SISRGIDLFS DYEAYKELAS SERLRFIISN
     TTEAGIVCDE KDRLEDRPQK TFPGKLTAFL YFRYQAFKGD QTKGCVLIPC ELIENNGEKL
     RETVLHYAHL WKLEEGFTQW IHEANTFCNS LVDRIVPGFP VDSIDEITAD LGYQDDLIVV
     GEQYYLWVIE GPDWIGKELP FAAAGLHTKI VSDLTPYRTK KVRILNGAHT AMTPVALLYG
     LKTVRDAVEH PEVGRFIREL IDDEILPVLK MEGLSQYADD VLNRFKNPYI KHYLESIALN
     AISKFKTRNL PTLKEYAEQK GQLPERLVFS FSALLYFYHD NETLQDDPAV LQFFKEVWCQ
     EDGDMLRIAS RVLGEQRLWG ADLNEIPKLT DRVAVYLNHI HELGMQRALE QYCIQGGEVR