UXAC_SALEP
ID UXAC_SALEP Reviewed; 470 AA.
AC B5QYB2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 61.
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=SEN2980;
OS Salmonella enteritidis PT4 (strain P125109).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P125109;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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; AM933172; CAR34556.1; -; Genomic_DNA.
DR RefSeq; WP_000190182.1; NC_011294.1.
DR AlphaFoldDB; B5QYB2; -.
DR SMR; B5QYB2; -.
DR KEGG; set:SEN2980; -.
DR HOGENOM; CLU_044465_1_0_6; -.
DR OMA; IWHQCNE; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000000613; 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_1000131602"
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