ID A6UH42_SINMW Unreviewed; 296 AA.
AC A6UH42;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Dihydrodipicolinate synthetase {ECO:0000313|EMBL:ABR62972.1};
GN OrderedLocusNames=Smed_4167 {ECO:0000313|EMBL:ABR62972.1};
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OG Plasmid pSMED01 {ECO:0000313|EMBL:ABR62972.1,
OG ECO:0000313|Proteomes:UP000001108}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394 {ECO:0000313|EMBL:ABR62972.1, ECO:0000313|Proteomes:UP000001108};
RN [1] {ECO:0000313|Proteomes:UP000001108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419 {ECO:0000313|Proteomes:UP000001108};
RC PLASMID=Plasmid pSMED01 {ECO:0000313|Proteomes:UP000001108};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABR62972.1, ECO:0000313|Proteomes:UP000001108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419 {ECO:0000313|EMBL:ABR62972.1,
RC ECO:0000313|Proteomes:UP000001108};
RC PLASMID=Plasmid pSMED01 {ECO:0000313|Proteomes:UP000001108};
RX PubMed=21304680; DOI=10.4056/sigs.43526;
RA Reeve W., Chain P., O'Hara G., Ardley J., Nandesena K., Brau L., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Hauser L., Chang Y.J., Ivanova N., Mavromatis K., Markowitz V.,
RA Kyrpides N., Gollagher M., Yates R., Dilworth M., Howieson J.;
RT "Complete genome sequence of the Medicago microsymbiont Ensifer
RT (Sinorhizobium) medicae strain WSM419.";
RL Stand. Genomic Sci. 2:77-86(2010).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; CP000739; ABR62972.1; -; Genomic_DNA.
DR RefSeq; WP_011969794.1; NC_009620.1.
DR RefSeq; YP_001312905.1; NC_009620.1.
DR AlphaFoldDB; A6UH42; -.
DR KEGG; smd:Smed_4167; -.
DR PATRIC; fig|366394.8.peg.624; -.
DR HOGENOM; CLU_049343_5_0_5; -.
DR OrthoDB; 9778880at2; -.
DR Proteomes; UP000001108; Plasmid pSMED01.
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: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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Plasmid {ECO:0000313|EMBL:ABR62972.1}.
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"
SQ SEQUENCE 296 AA; 31323 MW; ADD7A9B828D1A5D9 CRC64;
MTLFAGLAAF SITPADASGH VDTAALARLL ERICAAGAES IGLLGSTGGY AFLSRRERQR
AVEAAIECVD GRIPVIVGVG ALRTDEAQAL ARDARKAGAS GLLLAPMSYT PLTDEEVLQH
ISAVAEAGQL PLCIYNNPST TRFTFTDDLI VRLARLPNIA AVKMPLPAQG DVAGELARMR
SRIPEGFSIG YSGDWGAADA LLAGCDAWYS VVAGLMPAEA VALTRAARAG DVAEARRLDR
AFQPLWNLFK EFGSFRVMYA MADLLGLVGV DPPRPILPLG KTDMARVKDA LTRIAL
//
