ID A0A5Q3Q7W9_9PSEU Unreviewed; 306 AA.
AC A0A5Q3Q7W9;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 Name=kdgD {ECO:0000313|EMBL:QGK70463.1};
GN ORFNames=GIY23_13850 {ECO:0000313|EMBL:QGK70463.1};
OS Allosaccharopolyspora coralli.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Allosaccharopolyspora.
OX NCBI_TaxID=2665642 {ECO:0000313|EMBL:QGK70463.1, ECO:0000313|Proteomes:UP000371041};
RN [1] {ECO:0000313|Proteomes:UP000371041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2A {ECO:0000313|Proteomes:UP000371041};
RA Zhang G.;
RT "The complete genome sequence of Saccharopolyspora sp. E2A.";
RL Submitted (NOV-2019) 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 ---------------------------------------------------------------------------
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; CP045929; QGK70463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5Q3Q7W9; -.
DR KEGG; sace:GIY23_13850; -.
DR UniPathway; UPA00564; UER00628.
DR Proteomes; UP000371041; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000371041}.
FT ACT_SITE 144
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 170
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 57
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 306 AA; 33000 MW; F8A9D7DAF611823E CRC64;
MSRFSPPGVA DRLASGLLSF PVTHFRDDLT FDEPAYRDNI GWLSTFEPSG LFAAGGTGEL
FSLTPGEVES VVAAAVREAP SNVPVVAPAG YGTAMAVEMA RSAGRAGADG LLLLPPYLTE
TDQEGLIAHV RAVCAATDVG VILYSRANAI YTDTTVARLA DECPNLIGFK DGVGDIEKMT
RIHSRMGDRL TYIGGLPTAE TFALPYLEMG VTTYSSAMFN FVPEFASRFY AAVRERDRAT
VHRYLNQFVL PYCDIRNRRN GYAVSIVKAG MKVIGRPAGP VRSPLTDLDE SEVAMLADLV
KQGTEE
//
