KDGD_ACIAD
ID KDGD_ACIAD Reviewed; 303 AA.
AC Q6FFQ1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=ACIAD0130;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [2]
RP PATHWAY, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=18364348; DOI=10.1074/jbc.m800487200;
RA Aghaie A., Lechaplais C., Sirven P., Tricot S., Besnard-Gonnet M.,
RA Muselet D., de Berardinis V., Kreimeyer A., Gyapay G., Salanoubat M.,
RA Perret A.;
RT "New insights into the alternative D-glucarate degradation pathway.";
RL J. Biol. Chem. 283:15638-15646(2008).
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, ECO:0000269|PubMed:18364348};
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, ECO:0000269|PubMed:18364348}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP-
CC Rule:MF_00694}.
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DR EMBL; CR543861; CAG67106.1; -; Genomic_DNA.
DR RefSeq; WP_004930673.1; NC_005966.1.
DR AlphaFoldDB; Q6FFQ1; -.
DR SMR; Q6FFQ1; -.
DR STRING; 62977.ACIAD0130; -.
DR EnsemblBacteria; CAG67106; CAG67106; ACIAD0130.
DR GeneID; 45232652; -.
DR KEGG; aci:ACIAD0130; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_5_2_6; -.
DR OMA; EFHALTP; -.
DR OrthoDB; 1438588at2; -.
DR BioCyc; ASP62977:ACIAD_RS00610-MON; -.
DR BioCyc; MetaCyc:MON-15625; -.
DR BRENDA; 4.2.1.41; 8909.
DR SABIO-RK; Q6FFQ1; -.
DR UniPathway; UPA00564; UER00628.
DR Proteomes; UP000000430; 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 PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR TIGRFAMs; TIGR03249; KdgD; 1.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome.
FT CHAIN 1..303
FT /note="Probable 5-dehydro-4-deoxyglucarate dehydratase"
FT /id="PRO_1000045396"
SQ SEQUENCE 303 AA; 32624 MW; 55091529B63A1778 CRC64;
MDALELKNIV SDGLLSFPVT DFDQNGDFNA ASYAKRLEWL APYGASALFA AGGTGEFFSL
TGDEYSDVIK TAVDACKGSV PIIAGAGGPT RQAILQAQEA ERLGAHGILL MPHYLTEASQ
EGLVEHVKQV CNAVNFGVIF YNRSVSKLNV DSLQQLVESC PNLIGFKDSS GQIDMMTEVV
QTLGDRLSYL GGLPTAEIFA APYKALGSPV YSSAVFNFIP KTAMEFYNAL RNDDFATTQR
LIRDFFLPLI KIRNRKSGYA VSMVKAGAKI VGHDAGPVRP PLSDLTPQDY EDLAALIATL
GPQ