ID   UXAC_LACE2              Reviewed;         468 AA.
AC   C4Z5P8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, 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};
GN   OrderedLocusNames=EUBELI_00905;
OS   Lachnospira eligens (strain ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4)
OS   (Eubacterium eligens).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnospira.
OX   NCBI_TaxID=515620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4;
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(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; CP001104; ACR71907.1; -; Genomic_DNA.
DR   RefSeq; WP_012739143.1; NC_012778.1.
DR   AlphaFoldDB; C4Z5P8; -.
DR   SMR; C4Z5P8; -.
DR   STRING; 515620.EUBELI_00905; -.
DR   EnsemblBacteria; ACR71907; ACR71907; EUBELI_00905.
DR   GeneID; 41355640; -.
DR   KEGG; eel:EUBELI_00905; -.
DR   eggNOG; COG1904; Bacteria.
DR   HOGENOM; CLU_044465_1_0_9; -.
DR   OMA; TDHGHPT; -.
DR   OrthoDB; 167900at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000001476; 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_1000212518"
SQ   SEQUENCE   468 AA;  53930 MW;  543827EAE326E538 CRC64;
     MKQFMDKDFL LSTPTAQHLF HDYAAKMPIL DYHCHINPRE IAEDRKFENI TQVWLGGDHY
     KWRQMRTNGV DEKYITGDAS DREKFQKWAE TLEMAIGNPL YHWSHLELQR YFGYNGILNG
     DTAEEVWNLC NAKLQEDSMS VRNLIKQSNV TLICTTDDPV DSLEWHQVLK DDKTFDVQVL
     PAWRPDKAMN IEKPEYLDYL ETLSNVSGIK VNSFASLIDA LKNRMDFFAS MGCSVSDHAL
     EYVMYKPYTE EEIEAIFAKR FSGSAITTEE MNKFKTAFMV SVGKEYNKRN WVMQIHYGTI
     RDNNRFRYDQ LGPDTGFDCI NTYDCSAEMA QFLNALNATD ELPKTIIYSL NPSVNAAIGT
     VIGCFQDSKA VGKIQQGSAW WFNDHKVGMT NQMTSLANLS LLGNFIGMLT DSRSFLSYTR
     HEYFRRIMCE LIGGWVENGE YPADEKALKK IVEGISYNNA VRYFGFDL