UGA4E_AGRRK
ID UGA4E_AGRRK Reviewed; 334 AA.
AC B9J8R3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=UDP-glucuronate 4-epimerase {ECO:0000303|Ref.2};
DE Short=UGA4E {ECO:0000303|Ref.2};
DE EC=5.1.3.6 {ECO:0000269|Ref.2};
DE AltName: Full=ArUGAE {ECO:0000303|Ref.2};
GN Name=lpsL {ECO:0000312|EMBL:ACM27451.1};
GN OrderedLocusNames=Arad_3521 {ECO:0000312|EMBL:ACM27451.1};
OS Agrobacterium radiobacter (strain K84 / ATCC BAA-868).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=311403;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K84 / ATCC BAA-868;
RX PubMed=19251847; DOI=10.1128/jb.01779-08;
RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT "Genome sequences of three Agrobacterium biovars help elucidate the
RT evolution of multichromosome genomes in bacteria.";
RL J. Bacteriol. 191:2501-2511(2009).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX DOI=10.3390/catal10020222;
RA Gevaert O., Van Overtveldt S., Da Costa M., Beerens K., Desmet T.;
RT "Novel insights into the existence of the putative UDP-glucuronate 5-
RT epimerase specificity.";
RL Catalysts 10:222-222(2020).
CC -!- FUNCTION: Catalyzes the interconversion of UDP-D-glucuronic acid (UDP-
CC GlcA) and UDP-D-galacturonic acid (UDP-GalA). {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucuronate = UDP-alpha-D-galacturonate;
CC Xref=Rhea:RHEA:11404, ChEBI:CHEBI:57635, ChEBI:CHEBI:58052;
CC EC=5.1.3.6; Evidence={ECO:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:Q14376};
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; CP000628; ACM27451.1; -; Genomic_DNA.
DR RefSeq; WP_012652135.1; NC_011985.1.
DR AlphaFoldDB; B9J8R3; -.
DR SMR; B9J8R3; -.
DR STRING; 311403.Arad_3521; -.
DR EnsemblBacteria; ACM27451; ACM27451; Arad_3521.
DR KEGG; ara:Arad_3521; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_1_7_5; -.
DR OMA; EPIKVFN; -.
DR OrthoDB; 1180629at2; -.
DR Proteomes; UP000001600; Chromosome 1.
DR GO; GO:0050378; F:UDP-glucuronate 4-epimerase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Isomerase; NAD; Reference proteome.
FT CHAIN 1..334
FT /note="UDP-glucuronate 4-epimerase"
FT /id="PRO_0000450327"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 10..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
SQ SEQUENCE 334 AA; 37237 MW; 8D37D48314A5C2C4 CRC64;
MRYLITGTAG FIGFHLAKRL LDDGHFVVGF DGMTPYYDVK LKEKRTAILA RSNGFKAVTG
MLEDKAALDH AAELAEPDVI VHLAAQAGVR YSLENPRSYV DSNLVGSFNV LELARSIQPK
HLLLASTSSV YGANEKIPFA ESDKADEQMT IYAATKKSME LMAHSYAHLF HIPTTVFRFF
TVYGPWGRPD MALFKFVEAI KHDRPIEIYG EGKMSRDFTY IDDLVEGIVK LIGVIPSEEN
RVVSDTISDT LSKNAPFRIV NIGGGQPVGL MAFVETIEAM LGKRAIRHML PMQPGDVHNT
YAVPDLLVAL TGFKPQIEVD AGVRRFVEWY QENY