UXAC_ECOBW
ID UXAC_ECOBW Reviewed; 470 AA.
AC C4ZR08;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=BWG_2802;
OS Escherichia coli (strain K12 / MC4100 / BW2952).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=595496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MC4100 / BW2952;
RX PubMed=19376874; DOI=10.1128/jb.00118-09;
RA Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA Wang L.;
RT "Genomic sequencing reveals regulatory mutations and recombinational events
RT in the widely used MC4100 lineage of Escherichia coli K-12.";
RL J. Bacteriol. 191:4025-4029(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; CP001396; ACR65773.1; -; Genomic_DNA.
DR RefSeq; WP_000187442.1; NC_012759.1.
DR AlphaFoldDB; C4ZR08; -.
DR SMR; C4ZR08; -.
DR GeneID; 67414961; -.
DR KEGG; ebw:BWG_2802; -.
DR HOGENOM; CLU_044465_1_0_6; -.
DR OMA; TDHGHPT; -.
DR UniPathway; UPA00246; -.
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_1000212516"
SQ SEQUENCE 470 AA; 53987 MW; 9E51AA7B88411281 CRC64;
MTPFMTEDFL LDTEFARRLY HDYAKDQPIF DYHCHLPPQQ IAEDYRFKNL YDIWLKGDHY
KWRAMRTNGV AERLCTGDAS DREKFDAWAA TVPHTIGNPL YHWTHLELRR PFGITGKLLS
PSTADEIWNE CNELLAQDNF SARGIMQQMN VKMVGTTDDP IDSLEHHAEI AKDGSFTIKV
LPSWRPDKAF NIEQATFNDY MAKLGEVSDT DIRRFADLQT ALTKRLDHFA AHGCKVSDHA
LDVVMFAEAN EAELDSILAR RLAGETLSEH EVAQFKTAVL VFLGAEYARR GWVQQYHIGA
LRNNNLRQFK LLGPDVGFDS INDRPMAEEL SKLLSKQNEE NLLPKTILYC LNPRDNEVLG
TMIGNFQGEG MPGKMQFGSG WWFNDQKDGM ERQMTQLAQL GLLSRFVGML TDSRSFLSYT
RHEYFRRILC QMIGRWVEAG EAPADINLLG EMVKNICFNN ARDYFAIELN