ID   UXAC_BACSU              Reviewed;         473 AA.
AC   O34808;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Uronate isomerase;
DE            EC=5.3.1.12;
DE   AltName: Full=Glucuronate isomerase;
DE   AltName: Full=Uronic isomerase;
GN   Name=uxaC; Synonyms=yjmA; OrderedLocusNames=BSU12300;
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-glucuronate = D-fructuronate; Xref=Rhea:RHEA:13049,
CC         ChEBI:CHEBI:58720, ChEBI:CHEBI:59863; EC=5.3.1.12;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-galacturonate = keto-D-tagaturonate;
CC         Xref=Rhea:RHEA:27702, ChEBI:CHEBI:12952, ChEBI:CHEBI:17886;
CC         EC=5.3.1.12;
CC   -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC       interconversion.
CC   -!- INDUCTION: Induced by galacturonate, repressed by glucose.
CC       {ECO:0000269|PubMed:9882655}.
CC   -!- MISCELLANEOUS: Member of the exu locus which is required for
CC       galacturonate utilization.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Uronate isomerase family. {ECO:0000305}.
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DR   EMBL; AF015825; AAC46326.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13087.1; -; Genomic_DNA.
DR   PIR; C69852; C69852.
DR   RefSeq; NP_389112.1; NC_000964.3.
DR   RefSeq; WP_003245001.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O34808; -.
DR   SMR; O34808; -.
DR   STRING; 224308.BSU12300; -.
DR   PaxDb; O34808; -.
DR   PRIDE; O34808; -.
DR   EnsemblBacteria; CAB13087; CAB13087; BSU_12300.
DR   GeneID; 936461; -.
DR   KEGG; bsu:BSU12300; -.
DR   PATRIC; fig|224308.179.peg.1331; -.
DR   eggNOG; COG1904; Bacteria.
DR   InParanoid; O34808; -.
DR   OMA; TDHGHPT; -.
DR   PhylomeDB; O34808; -.
DR   BioCyc; BSUB:BSU12300-MON; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0008880; F:glucuronate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019698; P:D-galacturonate catabolic process; IBA:GO_Central.
DR   GO; GO:0042840; P:D-glucuronate catabolic process; IBA:GO_Central.
DR   HAMAP; MF_00675; UxaC; 1.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR003766; Uronate_isomerase.
DR   Pfam; PF02614; UxaC; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   2: Evidence at transcript level;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..473
FT                   /note="Uronate isomerase"
FT                   /id="PRO_0000172762"
SQ   SEQUENCE   473 AA;  54612 MW;  5ECB71610DBD9652 CRC64;
     MEPFMGKNFL LKNETAVSLY HNYAKDMPII DYHCHLSPKE IYENKTFQNI TEAWLYGDHY
     KWRIMRANGI EETYITGDAP DEEKFMAWAK TVPMAIGNPL YNWTHLELQR FFGIYEILNE
     KSGSAIWKQT NKLLKGEGFG ARDLIVKSNV KVVCTTDDPV DSLEYHLLLK EDKDFPVSVL
     PGFRPDKGLE INREGFPEWV QALEDAAAIS ITTYDEFLKA LEKRVRFFHS AGGRVSDHAI
     DTMVFAETTK EEAGRIFSDR LQGTEVSCED EKKFKTYTLQ FLCGLYAELD WAMQFHINAL
     RNTNTKMMKR LGPDTGYDSM NDEEIAKPLY KLLNSVEMKN QLPKTILYSL NPNDNYVIAS
     MINSFQDGIT PGKIQFGTAW WFNDTKDGML DQMKALSNVG LFSRFIGMLT DSRSFLSYTR
     HEYFRRIVCN LIGEWVENGE VPRDMELLGS IVQGICYDNA KHYFQFQEEK ANV