ID   UXAC_SALPB              Reviewed;         470 AA.
AC   A9N4U7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Uronate isomerase {ECO:0000255|HAMAP-Rule:MF_00675};
DE            EC=5.3.1.12 {ECO:0000255|HAMAP-Rule:MF_00675};
DE   AltName: Full=Glucuronate isomerase {ECO:0000255|HAMAP-Rule:MF_00675};
DE   AltName: Full=Uronic isomerase {ECO:0000255|HAMAP-Rule:MF_00675};
GN   Name=uxaC {ECO:0000255|HAMAP-Rule:MF_00675}; OrderedLocusNames=SPAB_03917;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00675};
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00675};
CC   -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC       interconversion. {ECO:0000255|HAMAP-Rule:MF_00675}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Uronate isomerase family. {ECO:0000255|HAMAP-Rule:MF_00675}.
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DR   EMBL; CP000886; ABX69247.1; -; Genomic_DNA.
DR   RefSeq; WP_000190182.1; NC_010102.1.
DR   AlphaFoldDB; A9N4U7; -.
DR   SMR; A9N4U7; -.
DR   KEGG; spq:SPAB_03917; -.
DR   PATRIC; fig|1016998.12.peg.3690; -.
DR   HOGENOM; CLU_044465_1_0_6; -.
DR   OMA; IWHQCNE; -.
DR   BioCyc; SENT1016998:SPAB_RS15900-MON; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000008556; Chromosome.
DR   GO; GO:0008880; F:glucuronate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Isomerase.
FT   CHAIN           1..470
FT                   /note="Uronate isomerase"
FT                   /id="PRO_1000082966"
SQ   SEQUENCE   470 AA;  53610 MW;  78D5EE0CB2B11218 CRC64;
     MATFMTEDFL LKNDIARTLY HKYAAPMPIY DFHCHLSPQE IADDRRFDNL GQIWLEGDHY
     KWRALRSAGV DESLITGKET SDYEKYMAWA NTVPKTLGNP LYHWTHLELR RPFGITGTLF
     GPDTAESIWT QCNEKLATPA FSARGIMQQM NVRMVGTTDD PIDSLEYHRQ IAADDSIDIE
     VAPSWRPDKV FKIELDGFVD YLRKLEAAAD VSITRFDDLR QALTRRLDHF AACGCRASDH
     GIETLRFAPV PDDAQLDAIL GKRLAGETLS ELEIAQFTTA VLVWLGRQYA ARGWVMQLHI
     GAIRNNNTRM FRLLGPDTGF DSIGDNNISW ALSRLLDSMD VTNELPKTIL YCLNPRDNEV
     LATMIGNFQG PGIAGKVQFG SGWWFNDQKD GMLRQLEQLS QMGLLSQFVG MLTDSRSFLS
     YTRHEYFRRI LCNLLGQWAQ DGEIPDDEAM LSRMVQDICF NNAQRYFTIK