ID   UXAC_STRS7              Reviewed;         465 AA.
AC   C0MCL4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=SZO_13120;
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70;
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; FM204884; CAW99848.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MCL4; -.
DR   SMR; C0MCL4; -.
DR   PRIDE; C0MCL4; -.
DR   EnsemblBacteria; CAW99848; CAW99848; SZO_13120.
DR   KEGG; seq:SZO_13120; -.
DR   PATRIC; fig|40041.11.peg.1390; -.
DR   eggNOG; COG1904; Bacteria.
DR   HOGENOM; CLU_044465_1_0_9; -.
DR   OMA; TDHGHPT; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000001368; 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_1000212520"
SQ   SEQUENCE   465 AA;  53330 MW;  2C83EEF0AB08AB85 CRC64;
     MAFNDDNFML KNEAAKRLYQ QIKDQPIFDY HCHLDPKEIF EDKVYDNIVD LWLGGDHYKW
     RLMRANGISE EEITGSASKL DKFKAFARTL QRSYGNPVYH WSVMELKNVF GVCELLTEDN
     AEEIYHRINA YLVEHQISPR KLIADSLVRF IGTTDHPLDD LAWHKRLAAD DTFETVVAPT
     FRPDEAFIEH QCFADFVARL AQATGRTITD FKSFIAAMEE RIAYFAENGC KASDISFTEI
     VFEAAEPEQL DHLMTRVLEG YQPQPLEIKQ WQTAVFAELC RVYKHYGFVT QVHFGALRNN
     HSAIFNKLGA DVGVDSLGDQ AALAINMNRL LDHLVQRDSL PKMIWYNLNP SYNITVANTL
     ANFQANENGI AGYLQFGAGW WFADTKLGMI SQMNALAEQG LLANFVGMLT DSRSFLSYQR
     HDYFRRILST YLGEWIEEGE VPEDYQALGS MAKDIAYNNA IQYFS