ID   UXAC_ECO8A              Reviewed;         470 AA.
AC   B7LZZ6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-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=ECIAI1_3238;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU928160; CAR00052.1; -; Genomic_DNA.
DR   RefSeq; WP_000187441.1; NC_011741.1.
DR   AlphaFoldDB; B7LZZ6; -.
DR   SMR; B7LZZ6; -.
DR   GeneID; 66673009; -.
DR   KEGG; ecr:ECIAI1_3238; -.
DR   HOGENOM; CLU_044465_1_0_6; -.
DR   OMA; TDHGHPT; -.
DR   UniPathway; UPA00246; -.
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_1000131591"
SQ   SEQUENCE   470 AA;  53983 MW;  793F43BCE7FDC4FF 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 RLAGEPLSEH EVAQFKTAVL VFLGAEYARR GWVQQYHIGA
     LRNNNLRQFK LLGPDVGFDS INDRPMAEEL SKLLSKQNEE NLLPKTILYC LNPRDNEVLG
     TMIGNFQGEG MPGKMQFGSG WWFNDQKDGM ERQMTQLAQL GLLSRFVGML TDSRSFLSYT
     RHEYFRRILC QMIGRWVEAG EAPADINLLG EMVKNICFNN ARDYFAIELN