ID   UXAC_STRE4              Reviewed;         465 AA.
AC   C0MA32;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-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=SEQ_0716;
OS   Streptococcus equi subsp. equi (strain 4047).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4047;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(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; FM204883; CAW93089.1; -; Genomic_DNA.
DR   RefSeq; WP_012679238.1; NC_012471.1.
DR   AlphaFoldDB; C0MA32; -.
DR   SMR; C0MA32; -.
DR   EnsemblBacteria; CAW93089; CAW93089; SEQ_0716.
DR   KEGG; seu:SEQ_0716; -.
DR   HOGENOM; CLU_044465_1_0_9; -.
DR   OMA; TDHGHPT; -.
DR   OrthoDB; 167900at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000001365; 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..465
FT                   /note="Uronate isomerase"
FT                   /id="PRO_1000147692"
SQ   SEQUENCE   465 AA;  53499 MW;  F4BE68C768519664 CRC64;
     MAFNDDNFML KNEAAKRLYQ QIKDQPIFDY HCHLDPKEIF EDKVYDNIVD LWLGGDHYKW
     RLMRANGISE EEITGSASKL DKFKAFARTL QRSYGNPVYH WSVMELKNVF GVCELLTEDN
     AEEIYHRINA YLVEHQISPR KLIADSRVRF IGTTDHPLDD LAWHKRLAAD DTFETVVAPT
     FRPDEAFIEH QRFADFVARL AQATGRTITD FKSFIAAMEE RIAYFAENGC KASDISFTEI
     VFEAAEPEQL DRLMTRVLEG YQPQPLEVKQ WQTAVFAELC RLYKHYGFVT QVHFGALRNN
     HSAIFNKLGA DVGVDSLGDQ TGLAINMNRL LDHLVQRDSL PKMIWYNLNP SYNIAVANTL
     ANFQANENGI AGYLQFGAGW WFADTKLGMI SQMNALAEQG LLANFVGMLT DSRSFLSYQR
     HDYFRRILST YLGEWIEEGE VPEDYQALGK MAQDIAYNNA IQYFN