ID   B3Q4L3_RHIE6            Unreviewed;       300 AA.
AC   B3Q4L3;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Putative dihydrodipicolinate synthetase protein {ECO:0000313|EMBL:ACE94144.1};
GN   OrderedLocusNames=RHECIAT_PC0000063 {ECO:0000313|EMBL:ACE94144.1};
OS   Rhizobium etli (strain CIAT 652).
OG   Plasmid pC {ECO:0000313|EMBL:ACE94144.1,
OG   ECO:0000313|Proteomes:UP000008817}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916 {ECO:0000313|EMBL:ACE94144.1, ECO:0000313|Proteomes:UP000008817};
RN   [1] {ECO:0000313|EMBL:ACE94144.1, ECO:0000313|Proteomes:UP000008817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652 {ECO:0000313|EMBL:ACE94144.1,
RC   ECO:0000313|Proteomes:UP000008817};
RC   PLASMID=Plasmid pC {ECO:0000313|Proteomes:UP000008817};
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA   Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA   Palacios R., Davila G.;
RT   "Genome diversity and DNA divergence of Rhizobium etli.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DapA family.
CC       {ECO:0000256|PIRNR:PIRNR001365}.
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DR   EMBL; CP001077; ACE94144.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3Q4L3; -.
DR   KEGG; rec:RHECIAT_PC0000063; -.
DR   eggNOG; COG0329; Bacteria.
DR   HOGENOM; CLU_049343_5_0_5; -.
DR   Proteomes; UP000008817; Plasmid pC.
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; IPR020625; Schiff_base-form_aldolases_AS.
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; PS00666; DHDPS_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Plasmid {ECO:0000313|EMBL:ACE94144.1};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT   ACT_SITE        142
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         54
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   BINDING         209
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   300 AA;  32168 MW;  E978DC466A02033B CRC64;
     MGLQSMTTFP FPGLNLAITT PFDDAGRIDY GRLEVNIERY LAAGVRSFLL SSGTGMHVYL
     SKAESEELVR RGARIVNGRA KVIAQTSALL VEDVVERTAR ARDAGAEGVM VLPPFFEGPT
     DDEGILDFYA EVAKAGLPVI GYNVPQAVGV AITPELLDKL NAIPGFSAVK DSSGDLGKQA
     ALIRTGRFVM NGADPLVPYA LYAGCDGLIW GGANFAPKTS VALVEAASQR KWDEVRDLWK
     ILEPAMGLIW EGDYVQSVYA AADMVGYGAG VPRKPLRALA AEKLPALRHS LEALMEREAI
//