ID   UXAC_SALPA              Reviewed;         470 AA.
AC   Q5PMP8;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=SPA3005;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV78842.1; -; Genomic_DNA.
DR   RefSeq; WP_000190186.1; NC_006511.1.
DR   AlphaFoldDB; Q5PMP8; -.
DR   SMR; Q5PMP8; -.
DR   EnsemblBacteria; AAV78842; AAV78842; SPA3005.
DR   KEGG; spt:SPA3005; -.
DR   HOGENOM; CLU_044465_1_0_6; -.
DR   OMA; IWHQCNE; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000008185; 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_0000172783"
SQ   SEQUENCE   470 AA;  53540 MW;  043E34AC98976E2C CRC64;
     MATFMTEDFL LKNDIARTLY HKYAAPMPIY DFHCHLSPQE IADDRRFDNL GQIWLEGDHY
     KWRALRSAGV DESLITGKET SDYEKYMAWA NTVPKTLGNP LYHWTHLELR RPFGITSTLF
     GPDTAESIWT QCNEKLATPA FSARGIMQQM NVRMVGTTDD PIDSLEYHRQ IAADDSINIE
     VAPSWRPDKV FKIELDGFVD YLGKLEAAAD 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