ID   A0A371JGI0_9FIRM        Unreviewed;       295 AA.
AC   A0A371JGI0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Dihydrodipicolinate synthase family protein {ECO:0000313|EMBL:RDY31854.1};
GN   ORFNames=CG710_007675 {ECO:0000313|EMBL:RDY31854.1};
OS   Lachnotalea glycerini.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnotalea.
OX   NCBI_TaxID=1763509 {ECO:0000313|EMBL:RDY31854.1, ECO:0000313|Proteomes:UP000216411};
RN   [1] {ECO:0000313|EMBL:RDY31854.1, ECO:0000313|Proteomes:UP000216411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCRI-19302 {ECO:0000313|EMBL:RDY31854.1,
RC   ECO:0000313|Proteomes:UP000216411};
RX   PubMed=29051240;
RA   Maheux A.F., Boudreau D.K., Berube E., Boissinot M., Raymond F.,
RA   Brodeur S., Corbeil J., Isabel S., Omar R.F., Bergeron M.G.;
RT   "Draft Genome Sequence of a Sporulating and Motile Strain of Lachnotalea
RT   glycerini Isolated from Water in Quebec City, Canada.";
RL   Genome Announc. 5:e01059-17(2017).
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:RDY31854.1}.
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DR   EMBL; NOKA02000009; RDY31854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371JGI0; -.
DR   OrthoDB; 9771791at2; -.
DR   Proteomes; UP000216411; 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:UP000216411}.
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         207
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   295 AA;  32464 MW;  D1C5D7D119FE1AA1 CRC64;
     MIKPHGIVPP IITPMTEDGK FNEPVFRQMI NHLIREGVHG IFPLGTTGEF YAFNNEEVKH
     ILKVAVEEAN GRVTVYAGAN HITTRGVITQ VKIAEEVGVD AVSVLTPMFV SQTQEEIYDF
     YKTIAESTSL PILIYNNKPK TNVTVTPETI AKLALIDNII GVKDSTGDFT NTEEYIRLTR
     HIENFSVLLG RDTLIFAGLC YGAAGAIASC ANVAPRIAAD IYDKYMAGDF EGAREAQFIL
     APLRIACNMG TFPAVIKEGL VLEGYAVGKC LEPIAELKEQ EKKKLETILK EMKLI
//