ID   UXAC_ECOK1              Reviewed;         470 AA.
AC   A1AG09;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Ecok1_31050;
GN   ORFNames=APECO1_3327;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ02599.1; -; Genomic_DNA.
DR   RefSeq; WP_000187442.1; NC_008563.1.
DR   AlphaFoldDB; A1AG09; -.
DR   SMR; A1AG09; -.
DR   EnsemblBacteria; ABJ02599; ABJ02599; APECO1_3327.
DR   GeneID; 67414961; -.
DR   KEGG; ecv:APECO1_3327; -.
DR   HOGENOM; CLU_044465_1_0_6; -.
DR   OMA; TDHGHPT; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000008216; 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_1000044764"
SQ   SEQUENCE   470 AA;  53987 MW;  9E51AA7B88411281 CRC64;
     MTPFMTEDFL LDTEFARRLY HDYAKDQPIF DYHCHLPPQQ IAEDYRFKNL YDIWLKGDHY
     KWRAMRTNGV AERLCTGDAS DREKFDAWAA TVPHTIGNPL YHWTHLELRR PFGITGKLLS
     PSTADEIWNE CNELLAQDNF SARGIMQQMN VKMVGTTDDP IDSLEHHAEI AKDGSFTIKV
     LPSWRPDKAF NIEQATFNDY MAKLGEVSDT DIRRFADLQT ALTKRLDHFA AHGCKVSDHA
     LDVVMFAEAN EAELDSILAR RLAGETLSEH EVAQFKTAVL VFLGAEYARR GWVQQYHIGA
     LRNNNLRQFK LLGPDVGFDS INDRPMAEEL SKLLSKQNEE NLLPKTILYC LNPRDNEVLG
     TMIGNFQGEG MPGKMQFGSG WWFNDQKDGM ERQMTQLAQL GLLSRFVGML TDSRSFLSYT
     RHEYFRRILC QMIGRWVEAG EAPADINLLG EMVKNICFNN ARDYFAIELN