ID   KDUI_OPITP              Reviewed;         274 AA.
AC   B1ZP50;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase;
DE            EC=5.3.1.17;
DE   AltName: Full=5-keto-4-deoxyuronate isomerase;
DE   AltName: Full=DKI isomerase;
GN   Name=kduI; OrderedLocusNames=Oter_4263;
OS   Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1).
OC   Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX   NCBI_TaxID=452637;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11246 / JCM 15787 / PB90-1;
RX   PubMed=21398538; DOI=10.1128/jb.00228-11;
RA   van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A.,
RA   Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., Schmutz J.,
RA   Larimer F.W., Land M.L., Hauser L., Kyrpides N., Mikhailova N.,
RA   Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.;
RT   "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an
RT   abundant inhabitant of rice paddy soil ecosystems.";
RL   J. Bacteriol. 193:2367-2368(2011).
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; CP001032; ACB77536.1; -; Genomic_DNA.
DR   RefSeq; WP_012377064.1; NC_010571.1.
DR   AlphaFoldDB; B1ZP50; -.
DR   SMR; B1ZP50; -.
DR   STRING; 452637.Oter_4263; -.
DR   EnsemblBacteria; ACB77536; ACB77536; Oter_4263.
DR   KEGG; ote:Oter_4263; -.
DR   eggNOG; COG3717; Bacteria.
DR   HOGENOM; CLU_062609_0_0_0; -.
DR   OMA; TFIWAMA; -.
DR   OrthoDB; 1047507at2; -.
DR   UniPathway; UPA00545; UER00826.
DR   Proteomes; UP000007013; 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   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   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
KW   Isomerase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..274
FT                   /note="4-deoxy-L-threo-5-hexosulose-uronate ketol-
FT                   isomerase"
FT                   /id="PRO_1000147780"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   274 AA;  30220 MW;  BF105837554201DC CRC64;
     MKLHYSPSPA ETKRLEPEQL RSAFLISDLF QPGQLITHYT DLDRMIAGGV TPTSAPLPLP
     NSKQATGTDF FLERREIGII NIGAPGAVRV GGKSYPLGSL DCLYVGKGER DVVFEAGSAG
     QAQYFFISTP AHMTYPTAHA ARAQGTQPIG DPAKCNRRRI NRYIHANGIK SCQLVMGFTE
     FEPGSVWNTM PPHTHSRRTE IYLYFDLGTD MVVHLMGEPQ ATRHLIVRDR EAILSPAWSI
     HAGVGTGAYR FIWAMGGDNQ TFEDMDQVAI ADLK