ID   KDGD_LEPCP              Reviewed;         303 AA.
AC   B1Y3Z2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Probable 5-dehydro-4-deoxyglucarate dehydratase {ECO:0000255|HAMAP-Rule:MF_00694};
DE            EC=4.2.1.41 {ECO:0000255|HAMAP-Rule:MF_00694};
DE   AltName: Full=5-keto-4-deoxy-glucarate dehydratase {ECO:0000255|HAMAP-Rule:MF_00694};
DE            Short=KDGDH {ECO:0000255|HAMAP-Rule:MF_00694};
GN   OrderedLocusNames=Lcho_1117;
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Leptothrix.
OX   NCBI_TaxID=395495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-dehydro-4-deoxy-D-glucarate + H(+) = 2,5-dioxopentanoate +
CC         CO2 + H2O; Xref=Rhea:RHEA:24608, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:42819,
CC         ChEBI:CHEBI:58136; EC=4.2.1.41; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00694};
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-
CC       dioxopentanoate from D-glucarate: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00694}.
CC   -!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00694}.
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DR   EMBL; CP001013; ACB33386.1; -; Genomic_DNA.
DR   RefSeq; WP_012346148.1; NC_010524.1.
DR   AlphaFoldDB; B1Y3Z2; -.
DR   SMR; B1Y3Z2; -.
DR   STRING; 395495.Lcho_1117; -.
DR   PRIDE; B1Y3Z2; -.
DR   EnsemblBacteria; ACB33386; ACB33386; Lcho_1117.
DR   KEGG; lch:Lcho_1117; -.
DR   eggNOG; COG0329; Bacteria.
DR   HOGENOM; CLU_049343_5_2_4; -.
DR   OMA; EFHALTP; -.
DR   OrthoDB; 1438588at2; -.
DR   UniPathway; UPA00564; UER00628.
DR   Proteomes; UP000001693; Chromosome.
DR   GO; GO:0047448; F:5-dehydro-4-deoxyglucarate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042838; P:D-glucarate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00951; KDGDH; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00694; KDGDH; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR017655; Dehydro-deoxyglucarate_dehyd.
DR   PANTHER; PTHR12128; PTHR12128; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   SMART; SM01130; DHDPS; 1.
DR   TIGRFAMs; TIGR03249; KdgD; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..303
FT                   /note="Probable 5-dehydro-4-deoxyglucarate dehydratase"
FT                   /id="PRO_1000132270"
SQ   SEQUENCE   303 AA;  32362 MW;  0D4F116A9035A00F CRC64;
     MSPQELKNVL QSGLLSFPLT DFDRELNFAP KPYAERLKWL QPYGASALFA AGGTGEFFSL
     EPGEYSDVIK VALDTCRGRT PIIAGAGGGT RVAIQYAQEA ERLGAQGVLL LPHYLTEASQ
     EGLIAHVQAV CRSVRFGVTV YNRGACKLTP ASLLVLAETC PNLIGFKDGI GDIETFVSIR
     QTLGERFAYL GGLPTAEVFA GAYKAMGCPV YSSAVFNFIP KTAMEFYNAH AAGDSATCDR
     LIRDFFLPYI ALRNKNHGYA VSIVKAGATL IGHGAGPVRP PLSDLKPAEV AELAALMAKL
     GPQ