ID   KDGD_CERS4              Reviewed;         301 AA.
AC   Q3IW19;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=RHOS4_36970; ORFNames=RSP_3655;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000144; ABA81265.1; -; Genomic_DNA.
DR   RefSeq; WP_011339506.1; NZ_CP030272.1.
DR   RefSeq; YP_355166.1; NC_007494.2.
DR   AlphaFoldDB; Q3IW19; -.
DR   SMR; Q3IW19; -.
DR   STRING; 272943.RSP_3655; -.
DR   EnsemblBacteria; ABA81265; ABA81265; RSP_3655.
DR   KEGG; rsp:RSP_3655; -.
DR   PATRIC; fig|272943.9.peg.4096; -.
DR   eggNOG; COG0329; Bacteria.
DR   OMA; MVYNRDN; -.
DR   PhylomeDB; Q3IW19; -.
DR   UniPathway; UPA00564; UER00628.
DR   Proteomes; UP000002703; Chromosome 2.
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..301
FT                   /note="Probable 5-dehydro-4-deoxyglucarate dehydratase"
FT                   /id="PRO_1000062045"
SQ   SEQUENCE   301 AA;  32004 MW;  F8502FAC031E9ECB CRC64;
     MDPQQIKAAL GSGLLSFPVT PFDAENRFAA APYQKHVEWL SGFDAPVLFA AGGTGEFFSL
     TPDEIPAIVK AAKESAGKTA IVSGCGYGTE IARGIARSVE AAGGDGILLL PHYLIDAPQE
     GLYAHVRAVC QATGMGVMVY NRDNAVLQAD TLARLCDDCP NLVGFKDGTG DIGLVRQITA
     KMGDRLTYLG GMPTAELFAE AYLGASFTTY SSAVFNFVPA LANKFYAALR AGDRATCESI
     LNSFFYPFME LRSRRKGYAV AAVKAGVRLV GFDAGPVRAP LSDLTGEEEE ILKALIDAHR
     E