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   16-JUN-2009, entry version 51.
DE   RecName: Full=Altronate oxidoreductase;
DE            EC=1.1.1.58;
DE   AltName: Full=Tagaturonate reductase;
DE   AltName: Full=Tagaturonate dehydrogenase;
GN   Name=uxaB; Synonyms=yjmI; OrderedLocusNames=BSU12380;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE OPERON STRUCTURE.
RC   STRAIN=168;
RX   MEDLINE=98240225; PubMed=9579062;
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
RT   containing a putative 12.3 kb operon involved in hexuronate catabolism
RT   and a perfectly symmetrical hypothetical catabolite-responsive
RT   element.";
RL   Microbiology 144:877-884(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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;
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: D-altronate + NAD(+) = D-tagaturonate + NADH.
CC   -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC       interconversion.
CC   -!- INDUCTION: Induced by galacturonate, repressed by glucose
CC       (Probable).
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.
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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; -.
DR   GeneID; 936468; -.
DR   GenomeReviews; AL009126_GR; BSU12380.
DR   KEGG; bsu:BSU12380; -.
DR   NMPDR; fig|224308.1.peg.1239; -.
DR   SubtiList; BG13212; uxaB.
DR   HOGENOM; O34354; -.
DR   OMA; O34354; SIFPCEL.
DR   BioCyc; BSUB224308:BSU1239-MON; -.
DR   BRENDA; 1.1.1.58; 150.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0009026; F:tagaturonate reductase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00670; -; 1.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR013118; Mannitol_DH_C.
DR   InterPro; IPR000669; Mannitol_DH_core.
DR   InterPro; IPR013131; Mannitol_DH_N.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1.
DR   Pfam; PF01232; Mannitol_dh; 1.
DR   Pfam; PF08125; Mannitol_dh_C; 1.
DR   PRINTS; PR00084; MTLDHDRGNASE.
PE   2: Evidence at transcript level;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    480       Altronate oxidoreductase.
FT                                /FTId=PRO_0000170739.
FT   NP_BIND      19     30       NAD (By similarity).
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
//