ID   UXAC_CROS8              Reviewed;         470 AA.
AC   A7MIR9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=ESA_03503;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU78718.1; -; Genomic_DNA.
DR   RefSeq; WP_012125925.1; NC_009778.1.
DR   AlphaFoldDB; A7MIR9; -.
DR   SMR; A7MIR9; -.
DR   EnsemblBacteria; ABU78718; ABU78718; ESA_03503.
DR   KEGG; esa:ESA_03503; -.
DR   PATRIC; fig|290339.8.peg.3116; -.
DR   HOGENOM; CLU_044465_1_0_6; -.
DR   OMA; TDHGHPT; -.
DR   OrthoDB; 167900at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000000260; 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..470
FT                   /note="Uronate isomerase"
FT                   /id="PRO_1000044766"
SQ   SEQUENCE   470 AA;  53954 MW;  BAAEB4835B3C1ECB CRC64;
     MTPFMTEDFL LDTEFARRLY HDYAKDQPIF DYHCHLPPQQ IAENYRFKNL YDIWLKGDHY
     KWRAMRTNGV PERLCTGDAS DREKFDAWAA TVPHTIGNPL YHWTHLELRR PFGITGKLLS
     PKTADEIWNQ CNDLLAQDAF SARGIMQQMN VKMVGTTDDP IDSLEHHATI AKDSAFTVKV
     LPSWRPDKAF NIEQATFADY MAKLAEVSDT DIRRFSDLQT ALTKRLDHFA AHGCKVSDHA
     LDVVLFAEAS ESELNAILSR RLAGETLSGH EIAQFKTAVL VWLGAEYARR GWVQQYHIGA
     LRNNNQRQFR LLGPDVGFDS INDRPLAEEL SKLLSKQNEE NLLPKTILYC LNPRDNEVLG
     TMIGNFQGEG MPGKMQFGSG WWFNDQKDGM ERQMTQLAQL GLLSRFVGML TDSRSFLSYT
     RHEYFRRILC QMIGRWVEAG EAPADIDLLG EMVKNICFNN ARDYFAIELH