ID B6A0A0_RHILW Unreviewed; 305 AA.
AC B6A0A0;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Dihydrodipicolinate synthetase {ECO:0000313|EMBL:ACI58034.1};
GN OrderedLocusNames=Rleg2_4793 {ECO:0000313|EMBL:ACI58034.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OG Plasmid pRLG201 {ECO:0000313|EMBL:ACI58034.1,
OG ECO:0000313|Proteomes:UP000008330}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI58034.1, ECO:0000313|Proteomes:UP000008330};
RN [1] {ECO:0000313|EMBL:ACI58034.1, ECO:0000313|Proteomes:UP000008330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304 {ECO:0000313|EMBL:ACI58034.1,
RC ECO:0000313|Proteomes:UP000008330};
RC PLASMID=pRLG201 {ECO:0000313|EMBL:ACI58034.1};
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; CP001192; ACI58034.1; -; Genomic_DNA.
DR RefSeq; WP_012555768.1; NC_011368.1.
DR AlphaFoldDB; B6A0A0; -.
DR KEGG; rlt:Rleg2_4793; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_5_1_5; -.
DR Proteomes; UP000008330; Plasmid pRLG201.
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 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:ACI58034.1};
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 207
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 305 AA; 33001 MW; DEED827875B8ACD3 CRC64;
MTKFKGVVPP VVTPLNPDFT VDYPSYTRVL DHLIDAGCHG VFVLGSTSEV IFHDEKTRRE
IIEHSAKVVN GRVPLIVGVI DPTTDRVIAH SKVAKAAGAD AVVVTAPFYT VTSQSEILDH
FRYVRDAVDV PLVAYDIPVC VHVKLQRQTV VTLAKEGSII GLKDSSGDDG NFRYALLDLA
EHKDVFLMTG SEIVVDNALL MGAHGVVPGI ANVDPHGYIR LWDAAQRGDW AAAKKEQERL
CRLFEIVWVA QGRVSGGASG IGAFKAAMQS LGIIDSAVMP RPRASLNDAE TARIDEILRA
TGLLN
//
