KDUI_DICD3
ID KDUI_DICD3 Reviewed; 278 AA.
AC Q05529; E0SDC3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 96.
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=Dda3937_03727;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PECTIN DEGRADATION,
RP DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=3937;
RX PubMed=1766386; DOI=10.1111/j.1365-2958.1991.tb02149.x;
RA Condemine G., Robert-Baudouy J.;
RT "Analysis of an Erwinia chrysanthemi gene cluster involved in pectin
RT degradation.";
RL Mol. Microbiol. 5:2191-2202(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
CC -!- FUNCTION: Catalyzes the isomerization of 5-dehydro-4-deoxy-D-
CC glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate.
CC {ECO:0000305|PubMed:1766386}.
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 -!- INDUCTION: Induced by galacturonate and at a higher level by
CC polygalacturonate. Is expressed under the control of KdgR, but is not
CC controlled by PecS. Is repressed by glucose.
CC {ECO:0000269|PubMed:1766386}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC polygalacturonate (PGA) or digalacturonate, but can grow on
CC galacturonate. {ECO:0000269|PubMed:1766386}.
CC -!- SIMILARITY: Belongs to the KduI family. {ECO:0000305}.
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DR EMBL; X62073; CAA43988.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM98615.1; -; Genomic_DNA.
DR PIR; S17710; S17710.
DR RefSeq; WP_013318065.1; NC_014500.1.
DR AlphaFoldDB; Q05529; -.
DR SMR; Q05529; -.
DR STRING; 198628.Dda3937_03727; -.
DR EnsemblBacteria; ADM98615; ADM98615; Dda3937_03727.
DR GeneID; 9733850; -.
DR KEGG; ddd:Dda3937_03727; -.
DR PATRIC; fig|198628.6.peg.2392; -.
DR eggNOG; COG3717; Bacteria.
DR HOGENOM; CLU_062609_0_0_6; -.
DR OMA; TFIWAMA; -.
DR OrthoDB; 1047507at2; -.
DR BioCyc; DDAD198628:DDA3937_RS11330-MON; -.
DR BioCyc; MetaCyc:MON-17020; -.
DR UniPathway; UPA00545; UER00826.
DR Proteomes; UP000006859; 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 Isomerase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..278
FT /note="4-deoxy-L-threo-5-hexosulose-uronate ketol-
FT isomerase"
FT /id="PRO_0000215491"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 63
FT /note="V -> D (in Ref. 1; CAA43988)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="S -> T (in Ref. 1; CAA43988)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 278 AA; 31240 MW; 9D052B0C9B8B4A5C CRC64;
MQVRQSIHSD HARQLDTAGL RREFLIEHIF DADACTMTYS HIDRIIVGGV MPVHQAVTVG
EDVGKQLGVS YFLERRELGA INIGGAGVVS VDGERYAIGH EEAIYIGKGA RDIRFTSVDP
AKPARFYYNS APAHTTFPTR KITAAEASPQ TIGDDATSNR RTINKYIVPD VLPTCQLTMG
LTKLAEGNLW NTMPCHTHER RMEVYFYFDM DEETAVFHMM GQPQETRHIL VHNEQAVISP
SWSIHSGVGT KRYTFIWGMV GENQVFSDMD HVKVSELR
