ID   UXAC_BACFN              Reviewed;         468 AA.
AC   Q5LCT3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=BF2382;
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
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; CR626927; CAH08080.1; -; Genomic_DNA.
DR   RefSeq; WP_005793937.1; NC_003228.3.
DR   AlphaFoldDB; Q5LCT3; -.
DR   SMR; Q5LCT3; -.
DR   STRING; 272559.BF9343_2299; -.
DR   EnsemblBacteria; CAH08080; CAH08080; BF9343_2299.
DR   KEGG; bfs:BF9343_2299; -.
DR   eggNOG; COG1904; Bacteria.
DR   HOGENOM; CLU_044465_1_0_10; -.
DR   OMA; TDHGHPT; -.
DR   OrthoDB; 167900at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000006731; 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; Reference proteome.
FT   CHAIN           1..468
FT                   /note="Uronate isomerase"
FT                   /id="PRO_1000044761"
SQ   SEQUENCE   468 AA;  54658 MW;  B4271EE3A2CBE3B5 CRC64;
     MKNFMDKNFL LQTETAQELY HNHAAKMPII DYHCHLNPQM VADDYRFKSL TEIWLGGDHY
     KWRAMRSNGV DECFCTGKET SDWEKFEKWA ETVPYTFRNP LYHWTHLELK TAFGIDKVLN
     PKTAREIYDE CNEKLSSQEY SARGMMRRYH VETVCTTDDP IDSLEYHIRT RESGFEIKML
     PTWRPDKVMA VEVPSDFRTY IEKLSEISEI TISDYNDMIL ALRKRHDYFA EQGCKLSDHG
     IEEFYAEDYT EGEIKTIFNK IYGGSELTKE EVLKFKSAML IVLGEMDWEK GWTQQFHYGA
     IRNNNSRMFK QLGPDTGFDS IGEFATAKAM SKFLDRLNSK GKLTKTILYN LNPCANEVIA
     TMIGNFQDGS IPGKIQFGSG WWFLDQKDGM ERQLNALSLL GLLSRFVGML TDSRSFLSYP
     RHEYFRRTLC NLLGCDVENG EIPLSEMERV CQMVEDISYF NAKNFFHF