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Database: UniProt
Entry: A0A916SGE7_9MICO
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Original site: A0A916SGE7_9MICO 
ID   A0A916SGE7_9MICO        Unreviewed;       309 AA.
AC   A0A916SGE7;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   08-OCT-2025, entry version 13.
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=GCM10010979_10610 {ECO:0000313|EMBL:GGA98026.1};
OS   Conyzicola nivalis.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Microbacteriaceae; Conyzicola.
OX   NCBI_TaxID=1477021 {ECO:0000313|EMBL:GGA98026.1, ECO:0000313|Proteomes:UP000606922};
RN   [1] {ECO:0000313|EMBL:GGA98026.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.12813 {ECO:0000313|EMBL:GGA98026.1};
RX   PubMed=25193709;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Walter F., Albersmeier A., Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of Corynebacterium casei LMG S-19264T (=DSM
RT   44701T), isolated from a smear-ripened cheese.";
RL   Int. J. Syst. Evol. Microbiol. 189:76-77(2014).
RN   [2] {ECO:0000313|EMBL:GGA98026.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.12813 {ECO:0000313|EMBL:GGA98026.1};
RA   Sun Q., Zhou Y.;
RL   Submitted (SEP-2020) 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:GGA98026.1}.
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DR   EMBL; BMGB01000001; GGA98026.1; -; Genomic_DNA.
DR   RefSeq; WP_188509625.1; NZ_BMGB01000001.1.
DR   Proteomes; UP000606922; Unassembled WGS sequence.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:TreeGrafter.
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-UniRule.
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   NCBIfam; NF002958; PRK03620.1; 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:UP000606922}.
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   309 AA;  33693 MW;  FACEF603B0FCEA20 CRC64;
     MVEFSPQQLA DTVGSGLLSF PVTHFTDDLE FDEPSYREHL SWLSQYPVAG LFAAGGTGEF
     FSLTASEVSS VLTAAIEEVD GRVPVIAPAG LGTRTAIEQA RDAERVGAAG ILLFPHYLTE
     ASQEGIAAHV EAVCRSTSLG VIFYNRANAR ITVETLARLA DSCPNLVGFK DGLGDIELMT
     RIYARFGQRF VYIGGLPTAE TFALPYLELG VTTYSSALFN FAPEFALEFY ADVRAKRHDA
     VYAKLRDFVL PYLDIRDRRK GYAVSIIKAG LDAVGRRGGP VRPPLLGLTH EERDELRELT
     AANALQPAR
//
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