ID   A0A136PYU8_9ACTN        Unreviewed;       292 AA.
AC   A0A136PYU8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Dihydrodipicolinate synthase family protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AWW66_02625 {ECO:0000313|EMBL:KXK63454.1};
OS   Micromonospora rosaria.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK63454.1, ECO:0000313|Proteomes:UP000070620};
RN   [1] {ECO:0000313|EMBL:KXK63454.1, ECO:0000313|Proteomes:UP000070620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 803 {ECO:0000313|EMBL:KXK63454.1,
RC   ECO:0000313|Proteomes:UP000070620};
RA   Yang H., He X., Zhu D.;
RT   "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT   which can produce antibacterial substance rosamicin.";
RL   Submitted (JAN-2016) 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:KXK63454.1}.
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DR   EMBL; LRQV01000005; KXK63454.1; -; Genomic_DNA.
DR   RefSeq; WP_067359680.1; NZ_LRQV01000005.1.
DR   AlphaFoldDB; A0A136PYU8; -.
DR   OrthoDB; 3175637at2; -.
DR   Proteomes; UP000070620; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070620}.
FT   ACT_SITE        137
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        164
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         49
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   BINDING         207
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   292 AA;  30097 MW;  8D411B5224BE857B CRC64;
     MTAHPAANLI SALPILFEAD GTVDLKATRA AYDQLAPHPL DGVFVAGTTG EFTTLTDDER
     LAVCVEAGEA FGPERTYWHV GHACTRQAVA LTRAAVDRGA RRFAALTPHY FPATEAALLG
     YYEAVVAAAA GRPVYGYLFA ARTTTTVSPA LLARLAGTGL AGVKISGEPT DVLTGYLAAL
     ADRAVPVYSG ADAEFTEVVD AGGAGVVSGV SSVLPGPFLA VRDALRSGDA AALAVARERS
     LRAVAATRQG NLAHLKAVLE LRGLPASGLR APLDPISPAD RRALEADVAD LL
//