ID A0A0K1QLQ0_PSEFL Unreviewed; 303 AA.
AC A0A0K1QLQ0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Probable 5-dehydro-4-deoxyglucarate dehydratase {ECO:0000256|HAMAP-Rule:MF_00694};
DE EC=4.2.1.41 {ECO:0000256|HAMAP-Rule:MF_00694};
DE AltName: Full=5-keto-4-deoxy-glucarate dehydratase {ECO:0000256|HAMAP-Rule:MF_00694};
DE Short=KDGDH {ECO:0000256|HAMAP-Rule:MF_00694};
GN ORFNames=B723_09605 {ECO:0000313|EMBL:AKV06638.1};
OS Pseudomonas fluorescens NCIMB 11764.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1221522 {ECO:0000313|EMBL:AKV06638.1, ECO:0000313|Proteomes:UP000017175};
RN [1] {ECO:0000313|EMBL:AKV06638.1, ECO:0000313|Proteomes:UP000017175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11764 {ECO:0000313|EMBL:AKV06638.1,
RC ECO:0000313|Proteomes:UP000017175};
RX PubMed=23144379; DOI=10.1128/JB.01670-12;
RA Vilo C.A., Benedik M.J., Kunz D.A., Dong Q.;
RT "Draft genome sequence of the cyanide-utilizing bacterium Pseudomonas
RT fluorescens strain NCIMB 11764.";
RL J. Bacteriol. 194:6618-6619(2012).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001446, ECO:0000256|HAMAP-
CC Rule:MF_00694};
CC -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-
CC dioxopentanoate from D-glucarate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004983, ECO:0000256|HAMAP-Rule:MF_00694}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000256|ARBA:ARBA00007592,
CC ECO:0000256|HAMAP-Rule:MF_00694, ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; CP010945; AKV06638.1; -; Genomic_DNA.
DR RefSeq; WP_017336515.1; NZ_CP010945.1.
DR AlphaFoldDB; A0A0K1QLQ0; -.
DR eggNOG; COG0329; Bacteria.
DR OrthoDB; 8995637at2; -.
DR UniPathway; UPA00564; UER00628.
DR Proteomes; UP000017175; 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; Aldolase class I; 1.
DR HAMAP; MF_00694; KDGDH; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR017655; Dehydro-deoxyglucarate_dehyd.
DR NCBIfam; TIGR03249; KdgD; 1.
DR PANTHER; PTHR12128:SF19; 5-DEHYDRO-4-DEOXYGLUCARATE DEHYDRATASE 2-RELATED; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00694}.
FT ACT_SITE 141
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 167
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 54
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 303 AA; 32681 MW; C8967BA5BA29017F CRC64;
MNPQELKSIL SSGLLSFPVT DFNAQGDFHR AGYIKRLEWL APYGASALFA AGGTGEFFSL
AASEYSEIIK TAVDTCETSV PILAGVGGST RQAIEYAQEA ERLGAKGLLL LPHYLTEASQ
DGVAAHVEAV CKSVKIGVVV YNRNVCRLTA PLLERLAERC PNLIGYKDGL GDIELMVSIR
RRLGDRFSYL GGLPTAEVYA AAYKALGVPV YSSAVFNFIP KTAMDFYHAI AREDHATVGK
IIDDFFLPYL DIRNRKAGYA VSIVKAGAKI AGYDAGPVRA PLTDLTGEEY EMLAALIDKQ
GAQ
//
