ID   UXAC_ESCF3              Reviewed;         470 AA.
AC   B7LMX3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=EFER_4383;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
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}.
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DR   EMBL; CU928158; CAQ91801.1; -; Genomic_DNA.
DR   RefSeq; WP_000187461.1; NC_011740.1.
DR   AlphaFoldDB; B7LMX3; -.
DR   SMR; B7LMX3; -.
DR   EnsemblBacteria; CAQ91801; CAQ91801; EFER_4383.
DR   GeneID; 60903145; -.
DR   KEGG; efe:EFER_4383; -.
DR   HOGENOM; CLU_044465_1_0_6; -.
DR   OMA; TDHGHPT; -.
DR   OrthoDB; 167900at2; -.
DR   BioCyc; EFER585054:EFER_RS21865-MON; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000000745; 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_1000131596"
SQ   SEQUENCE   470 AA;  54000 MW;  491EF31DB17D0E9D CRC64;
     MTPFMTEDFL LDTEFARRLY HEYAKDQPIF DYHCHLPPQQ IAEDYRFKNL YDIWLKGDHY
     KWRAMRTNGV AERLCTGDAS DREKFDAWAA TVPHTIGNPL YHWTHLELRR PFGITGKLLS
     PSTADEIWNQ 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