ID C6ARM9_RHILS Unreviewed; 308 AA.
AC C6ARM9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Dihydrodipicolinate synthetase {ECO:0000313|EMBL:ACS57054.1};
GN OrderedLocusNames=Rleg_2793 {ECO:0000313|EMBL:ACS57054.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS57054.1, ECO:0000313|Proteomes:UP000002256};
RN [1] {ECO:0000313|EMBL:ACS57054.1, ECO:0000313|Proteomes:UP000002256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1325 {ECO:0000313|EMBL:ACS57054.1,
RC ECO:0000313|Proteomes:UP000002256};
RX PubMed=21304718;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Copeland A., Nolan M., Han C., Brettin T., Land M., Ovchinikova G.,
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 WSM1325, an effective microsymbiont of annual Mediterranean clovers.";
RL Stand. Genomic Sci. 2:347-356(2010).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; CP001622; ACS57054.1; -; Genomic_DNA.
DR RefSeq; WP_012758228.1; NC_012850.1.
DR AlphaFoldDB; C6ARM9; -.
DR KEGG; rlg:Rleg_2793; -.
DR HOGENOM; CLU_049343_5_0_5; -.
DR OrthoDB; 9778880at2; -.
DR Proteomes; UP000002256; Chromosome.
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 PANTHER; PTHR12128:SF73; 4-HYDROXY-TETRAHYDRODIPICOLINATE SYNTHASE; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 166
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 50
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 308 AA; 32927 MW; B7D7927109316998 CRC64;
MSVTSPFHGL SAFPPTPANR EGRVDTEALG RLLERLCDAG VASIGLLGST GIYAFLTREE
RRRAVEAAVE CVRGRIPLVV GVGALRTDHA RSLARDAEAA GADALLLAPV SYTPLTQDEA
YEHFLAVTEA ANLPLCIYNN PGTTHFTFGR DLLQRLSDIE TIRAVKMPLP ADGDFAGELA
ALREKTRLAI GYSGDWGAAE ALLSGADAWY SVIGGLLPRV ALALTKAAIA GKGGEAHRLD
GLLEPLWKTF KAFGSLRVVY TLVDLLSLAG AELPRPLLPL GPMDRQRVLD AVEPLIALES
ELKRQSLL
//
