KDUI1_ENTFA
ID KDUI1_ENTFA Reviewed; 276 AA.
AC Q838L9;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase 1;
DE EC=5.3.1.17;
DE AltName: Full=5-keto-4-deoxyuronate isomerase 1;
DE AltName: Full=DKI isomerase 1;
GN Name=kduI1; Synonyms=kduI-1; OrderedLocusNames=EF_0425;
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; AAO80282.1; -; Genomic_DNA.
DR RefSeq; NP_814211.1; NC_004668.1.
DR RefSeq; WP_011109446.1; NZ_KE136524.1.
DR PDB; 1YWK; X-ray; 2.95 A; A/B/C/D/E/F=1-276.
DR PDBsum; 1YWK; -.
DR AlphaFoldDB; Q838L9; -.
DR SMR; Q838L9; -.
DR STRING; 226185.EF_0425; -.
DR DNASU; 1199341; -.
DR EnsemblBacteria; AAO80282; AAO80282; EF_0425.
DR KEGG; efa:EF0425; -.
DR PATRIC; fig|226185.9.peg.394; -.
DR eggNOG; COG3717; Bacteria.
DR HOGENOM; CLU_062609_0_0_9; -.
DR OMA; TFIWAMA; -.
DR UniPathway; UPA00545; UER00826.
DR EvolutionaryTrace; Q838L9; -.
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 1: Evidence at protein level;
KW 3D-structure; Isomerase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..276
FT /note="4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
FT 1"
FT /id="PRO_0000215488"
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"
FT STRAND 1..4
FT /evidence="ECO:0007829|PDB:1YWK"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:1YWK"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1YWK"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1YWK"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1YWK"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1YWK"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1YWK"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:1YWK"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1YWK"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:1YWK"
SQ SEQUENCE 276 AA; 31745 MW; 2E3EF367E13A24B9 CRC64;
METRYTHSPA DIRHYSTEQL RDEFLVEKVF IPGAISLTYT HNDRMIFGGV TPTTEELEII
LDKELGVDYF LERRELGVIN IGGPGFIEID GAKETMKKQD GYYIGKETKH VRFSSENPDN
PAKFYISCVP AHHKYPNVKI SIDEITPMET GDPLTLNQRK IYQYIHPNVC ESCQLQMGYT
ILEPGSAWNT MPCHTHERRM EAYVYFDMEE DTRIFHMMGK PDETKHLVMS NEQAAISPSW
SIHSGVGTSN YSFIWAMCGE NITYTDMDMV AMDQLK
