ID   KDGD_ACIBT              Reviewed;         303 AA.
AC   A3M3N7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   25-MAY-2022, entry version 78.
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=A1S_1101;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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; CP000521; ABO11531.2; -; Genomic_DNA.
DR   RefSeq; WP_000339250.1; NZ_CP053098.1.
DR   AlphaFoldDB; A3M3N7; -.
DR   SMR; A3M3N7; -.
DR   GeneID; 56377608; -.
DR   KEGG; acb:A1S_1101; -.
DR   HOGENOM; CLU_049343_5_2_6; -.
DR   UniPathway; UPA00564; UER00628.
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   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   TIGRFAMs; TIGR03249; KdgD; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..303
FT                   /note="Probable 5-dehydro-4-deoxyglucarate dehydratase"
FT                   /id="PRO_1000132267"
SQ   SEQUENCE   303 AA;  32813 MW;  BF09C20A6732B2B5 CRC64;
     MDALELKNII SDGLLSFPVT DFDQNGDFNK SSYAKRLEWL APYGASALFA AGGTGEFFSL
     TGNEYSEVIK TAVDTCKGSV PIIAGAGGPT RQAIEQAKEA ERLGAHGILL MPHYLTEASQ
     EGLIEHVKQV CNSVDFGVIF YNRSVSRLNL DSIQKLTEMC PNLIGFKDSS GQIDMMTAVT
     QTIGDRLSYL GGLPTAEVFA APYKALGCPV YSSAVFNFIP KTAMEFYNAL RSDDFETTNR
     LIKDFFLPLI KIRDRKSGYA VSMIKAGAKI VGHDAGPVRP PLSDLTQADY EDLAALIATL
     GPQ