KDUI2_ENTFA
ID KDUI2_ENTFA Reviewed; 276 AA.
AC Q832G5;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase 2;
DE EC=5.3.1.17;
DE AltName: Full=5-keto-4-deoxyuronate isomerase 2;
DE AltName: Full=DKI isomerase 2;
GN Name=kduI2; Synonyms=kduI-2; OrderedLocusNames=EF_2264;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
CC -!- FUNCTION: Catalyzes the isomerization of 5-dehydro-4-deoxy-D-
CC glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D-glycero-2,5-
CC hexodiulosonate; Xref=Rhea:RHEA:23896, ChEBI:CHEBI:17117,
CC ChEBI:CHEBI:29071; EC=5.3.1.17;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 4/5.
CC -!- SIMILARITY: Belongs to the KduI family. {ECO:0000305}.
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DR EMBL; AE016830; AAO81992.1; -; Genomic_DNA.
DR RefSeq; NP_815922.1; NC_004668.1.
DR RefSeq; WP_011109530.1; NZ_KE136528.1.
DR AlphaFoldDB; Q832G5; -.
DR SMR; Q832G5; -.
DR STRING; 226185.EF_2264; -.
DR EnsemblBacteria; AAO81992; AAO81992; EF_2264.
DR KEGG; efa:EF2264; -.
DR PATRIC; fig|226185.9.peg.2122; -.
DR eggNOG; COG3717; Bacteria.
DR HOGENOM; CLU_062609_0_0_9; -.
DR OMA; VYSMYDR; -.
DR UniPathway; UPA00545; UER00826.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0008697; F:4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.10; -; 1.
DR Gene3D; 2.60.120.520; -; 1.
DR HAMAP; MF_00687; KduI; 1.
DR InterPro; IPR007045; KduI.
DR InterPro; IPR021120; KduI/IolB_isomerase.
DR InterPro; IPR027449; KduI_N.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR38461; PTHR38461; 1.
DR Pfam; PF04962; KduI; 1.
DR PIRSF; PIRSF006625; KduI; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 3: Inferred from homology;
KW Isomerase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..276
FT /note="4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
FT 2"
FT /id="PRO_0000215489"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 276 AA; 31668 MW; C8D22956AF550EF5 CRC64;
MDTRYTHSPK DISHYSTEEL RKEFLVEKVF VPNEVSLTYT HNDRMIFGGV TPTTESLEII
LNKELGVDYF LERRELGVIN IGGPGFIEID GRKEAMKKQD GYYVGKETRQ VIFSSEDAAD
PAKFYISSAP AHHKYPNVKI SIDEIKPMET GEALTLNERK IYQYIHPNIC ESCQLQMGYT
ILEPGSSWNT MPCHTHERRM EAYVYFDMEE DTKIFHMMGD PAETKHLVMG NEQAVISPSW
SIHSGVGTSN YSFIWAMCGE NITYTDMDMV PMDELK