KDUD_DICD3
ID KDUD_DICD3 Reviewed; 253 AA.
AC Q05528; E0SDC4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase;
DE EC=1.1.1.127;
DE AltName: Full=2-keto-3-deoxygluconate 5-dehydrogenase;
DE AltName: Full=2-keto-3-deoxygluconate oxidoreductase;
DE Short=KDG oxidoreductase;
GN Name=kduD; OrderedLocusNames=Dda3937_04595;
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], CATALYTIC ACTIVITY, AND FUNCTION IN
RP PECTIN DEGRADATION.
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 reduction of 2,5-diketo-3-deoxygluconate (DKII
CC or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto-3-deoxygluconate (KDG
CC or 2-dehydro-3-deoxygluconate) with a concomitant oxidation of NADH.
CC {ECO:0000269|PubMed:1766386}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-D-gluconate + NAD(+) = 3-deoxy-D-glycero-
CC 2,5-hexodiulosonate + H(+) + NADH; Xref=Rhea:RHEA:24232,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29071, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57990; EC=1.1.1.127;
CC Evidence={ECO:0000269|PubMed:1766386};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 5/5.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; X62073; CAA43989.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM98616.1; -; Genomic_DNA.
DR PIR; S17711; S17711.
DR RefSeq; WP_013318066.1; NC_014500.1.
DR AlphaFoldDB; Q05528; -.
DR SMR; Q05528; -.
DR STRING; 198628.Dda3937_04595; -.
DR EnsemblBacteria; ADM98616; ADM98616; Dda3937_04595.
DR GeneID; 9733851; -.
DR KEGG; ddd:Dda3937_04595; -.
DR PATRIC; fig|198628.6.peg.2393; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_1_6; -.
DR OMA; RIWDSKV; -.
DR OrthoDB; 1294334at2; -.
DR BioCyc; DDAD198628:DDA3937_RS11335-MON; -.
DR BioCyc; MetaCyc:MON-15643; -.
DR UniPathway; UPA00545; UER00827.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0047001; F:2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008678; F:2-deoxy-D-gluconate 3-dehydrogenase activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR011286; 2-deoxy-D-gluc_3_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01832; kduD; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..253
FT /note="2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase"
FT /id="PRO_0000054716"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 14..38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 154
FT /note="R -> P (in Ref. 1; CAA43989)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..164
FT /note="SA -> KR (in Ref. 1; CAA43989)"
FT /evidence="ECO:0000305"
FT CONFLICT 171..172
FT /note="LL -> IV (in Ref. 1; CAA43989)"
FT /evidence="ECO:0000305"
FT CONFLICT 198..199
FT /note="QL -> HV (in Ref. 1; CAA43989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 27227 MW; 53D15DE7E1FAD8DA CRC64;
MILNTFNLQG KVALITGCDT GLGQGMAVGL AEAGCDIVGV NIVEPKETIE KVTAVGRRFL
SLTADMSDIS GHAALVEKAV AEFGKVDILV NNAGIIRRED AIEFSEKNWD DVMNLNIKSV
FFMSQTVARQ FIKQGHGGKI INIASMLSFQ GGIRVPSYTA SKSAVMGITR LLANEWAKHN
INVNAIAPGY MATNNTQQLR ADQDRSKEIL DRIPAGRWGL PQDLQGPAVF LASSASDYVN
GYTIAVDGGW LAR
