ID N2J1G5_9PSED Unreviewed; 303 AA.
AC N2J1G5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=HMPREF1487_07089 {ECO:0000313|EMBL:ENA31658.1},
GN HMPREF1487_08035 {ECO:0000313|EMBL:ENA29781.1};
OS Pseudomonas sp. HPB0071.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1203578 {ECO:0000313|EMBL:ENA29781.1, ECO:0000313|Proteomes:UP000017050};
RN [1] {ECO:0000313|EMBL:ENA29781.1, ECO:0000313|Proteomes:UP000017050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPB0071 {ECO:0000313|EMBL:ENA29781.1,
RC ECO:0000313|Proteomes:UP000017050};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T., Dover J., Dai D.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Pseudomonas sp. HPB0071.";
RL Submitted (MAR-2013) 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;
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENA29781.1}.
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DR EMBL; AQFP01000012; ENA29781.1; -; Genomic_DNA.
DR EMBL; AQFP01000010; ENA31658.1; -; Genomic_DNA.
DR RefSeq; WP_010797261.1; NZ_KI517367.1.
DR AlphaFoldDB; N2J1G5; -.
DR GeneID; 84597942; -.
DR PATRIC; fig|1203578.3.peg.2794; -.
DR HOGENOM; CLU_049343_5_2_6; -.
DR OrthoDB; 8995637at2; -.
DR UniPathway; UPA00564; UER00628.
DR Proteomes; UP000017050; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000017050}.
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; 32971 MW; BE87BC6BD0E5523D CRC64;
MTPQELKHTL SSGLLSFPVT DFDAQGDFRR DTYIKRLEWL APYGASALFA AGGTGEFFSL
DQKEYSDIIK TAVDTCKGMV PILAGAGGPT RVAIQQAQEA ERLGAQGILL LPHYLTEASP
EGVAAHVEAV CKSVKFGVVV YNRNVCRLKP DQLEMLAERC PNLIGFKDGM GDIELMVSIR
RRLGDRFTYL GGLPTAEVYA AAYKALGVPV YSSAVFNFVP KTAMDFYKAI AADDHETVGK
LIDDFFLPYL DIRNRCAGYA VSIVKAGAKI AGYDAGPVRA PLTDLKPDEY ERLAALMDKL
GPQ
//
