ID   UXAC_STRU0              Reviewed;         467 AA.
AC   B9DSL9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=SUB1203;
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J;
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA   Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA   Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA   Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(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; AM946015; CAR42641.1; -; Genomic_DNA.
DR   RefSeq; WP_012658683.1; NC_012004.1.
DR   AlphaFoldDB; B9DSL9; -.
DR   SMR; B9DSL9; -.
DR   STRING; 218495.SUB1203; -.
DR   EnsemblBacteria; CAR42641; CAR42641; SUB1203.
DR   KEGG; sub:SUB1203; -.
DR   eggNOG; COG1904; Bacteria.
DR   HOGENOM; CLU_044465_1_0_9; -.
DR   OMA; TDHGHPT; -.
DR   OrthoDB; 167900at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000000449; 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..467
FT                   /note="Uronate isomerase"
FT                   /id="PRO_1000147694"
SQ   SEQUENCE   467 AA;  53730 MW;  EE4EB3DDD4799CF5 CRC64;
     MTFNDKNFML KNQAAKQLYT AVQDQPIFDY HCHLDPKEIF EDKVFENIVD LWLGGDHYKW
     RLMRANGISE EEITGSASQL DKFKAFARTL QRSYGNPVYH WSAMELKNVF GIEEVLTEEN
     AEEIYNRLNT YLLENKVSPR KLIADSKVTF IGTTDHPLDT LEWHQKLAED KSFETIVAPT
     FRPDEAFIEH HNFKGFLDKL SQATGKEMTE FKDFISAMED RIAYFAENGC KASDISFTEI
     VFEAAEESEL NELLAKVKDG YKPNALEVKQ WQTAVFAELC QLYKKYGFVT QVHFGALRNN
     HSKLYQKLGA DVGIDSLGDQ TALTSNMNKL LDNLVQKDAL PKMIWYNLNP SYNIAVANTL
     ANFQANEEGV KSYLQFGAGW WFADTKLGMI SQMNALAEQG MLANFVGMLT DSRSFLSYQR
     HDYFRRILCT YLGEWIEEGE VPEDYEALGH MAKDIAYHNA VNYFKHE