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Database: UniProt
Entry: A0A4R4M8S0_9ACTN
LinkDB: A0A4R4M8S0_9ACTN
Original site: A0A4R4M8S0_9ACTN 
ID   A0A4R4M8S0_9ACTN        Unreviewed;       291 AA.
AC   A0A4R4M8S0;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000313|EMBL:TDB91810.1};
GN   ORFNames=E1264_00550 {ECO:0000313|EMBL:TDB91810.1};
OS   Actinomadura sp. KC216.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=2530370 {ECO:0000313|EMBL:TDB91810.1, ECO:0000313|Proteomes:UP000294687};
RN   [1] {ECO:0000313|EMBL:TDB91810.1, ECO:0000313|Proteomes:UP000294687}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KC216 {ECO:0000313|EMBL:TDB91810.1,
RC   ECO:0000313|Proteomes:UP000294687};
RA   Sahin N., Ay H., Saygin H.;
RT   "Draft genome sequences of novel Actinobacteria.";
RL   Submitted (MAR-2019) 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:TDB91810.1}.
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DR   EMBL; SMJX01000002; TDB91810.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R4M8S0; -.
DR   OrthoDB; 9782828at2; -.
DR   Proteomes; UP000294687; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR   InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR   PANTHER; PTHR12128:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00665; DHDPS_1; 1.
DR   PROSITE; PS00666; DHDPS_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT   ACT_SITE        135
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        163
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         47
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   BINDING         205
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   291 AA;  29993 MW;  05E6F4E617DB34CB CRC64;
     MRAVHGIHAS LVTPFTRSGE VDVKSLERLA VHCLDGGADG LVALGTTGEA AMLSPAEQRT
     VLEVCRAVSI EHGTPLTVGA GTIGTEDSIR QARERAPLAD ALLVVVPYYL RPSDDGVIDH
     FAAIGSAVDV PLIAYHVPYR TGKPLPAGTL LRILALDCVA GIKQCAGAVD HDTLAVLAAH
     TRKAVLCGDD AYLYPMLQLG ASGGVTASAC LAPAAYAAMA AATRDGNAPR ALALHNALLP
     MADALFGEPS PSVLKACLVD EGLIDEPAVR APLHAPRPES VAAALRAFRA V
//
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