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Database: UniProt
Entry: A0A0N0MX66_9ACTN
LinkDB: A0A0N0MX66_9ACTN
Original site: A0A0N0MX66_9ACTN 
ID   A0A0N0MX66_9ACTN        Unreviewed;       302 AA.
AC   A0A0N0MX66;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=5-dehydro-4-deoxyglucarate dehydratase {ECO:0000313|EMBL:KPI10429.1};
DE            EC=4.2.1.41 {ECO:0000313|EMBL:KPI10429.1};
GN   ORFNames=OK006_4611 {ECO:0000313|EMBL:KPI10429.1};
OS   Actinobacteria bacterium OK006.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI10429.1, ECO:0000313|Proteomes:UP000037912};
RN   [1] {ECO:0000313|EMBL:KPI10429.1, ECO:0000313|Proteomes:UP000037912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK006 {ECO:0000313|EMBL:KPI10429.1,
RC   ECO:0000313|Proteomes:UP000037912};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT   and OV320.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DapA family.
CC       {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:KPI10429.1}.
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DR   EMBL; LJCU01000197; KPI10429.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0MX66; -.
DR   PATRIC; fig|1592326.3.peg.5708; -.
DR   Proteomes; UP000037912; Unassembled WGS sequence.
DR   GO; GO:0047448; F:5-dehydro-4-deoxyglucarate dehydratase activity; IEA:UniProtKB-EC.
DR   CDD; cd00408; DHDPS-like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
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|PIRNR:PIRNR001365}.
FT   ACT_SITE        143
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        168
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         55
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   302 AA;  32437 MW;  E45E6C16BB337307 CRC64;
     MTATYETQRA ALAEVVAIPV TPFTEDGTID GDTHRALLRR LLDGGIRTLT PNGNTGEFYA
     LTPEERNLVT ELTIDEAGDR ADVRVGVGHD VPTAVASARH ARELGAQMVM VHQPVHPYVS
     EGGWVDYHRA IAEAVPELGV VPYIRNPVLP GARLADLADV CPNVIGVKYA VPDAARFAAF
     ARDAGLDRFV WVAGLAEPYA PSYFSAGATG FTSGLVNVAP AVSLNMIEAL RVGDYPAAMK
     VWEQIRRFEE LRAANTSANN VTVVKEALAS LGLCRREVRP PSRELPESER AEVAAIAAGW
     SI
//
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