DAPD_BRUO2
ID DAPD_BRUO2 Reviewed; 284 AA.
AC A5VVT4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE EC=2.3.1.117 {ECO:0000255|HAMAP-Rule:MF_00811};
DE AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE Short=THDP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE Short=THP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE Short=Tetrahydropicolinate succinylase {ECO:0000255|HAMAP-Rule:MF_00811};
GN Name=dapD {ECO:0000255|HAMAP-Rule:MF_00811}; OrderedLocusNames=BOV_A0969;
OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=444178;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT range and tissue tropism.";
RL PLoS ONE 4:E5519-E5519(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-
CC 2-succinylamino-6-oxoheptanedioate + CoA; Xref=Rhea:RHEA:17325,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00811};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC (succinylase route): step 1/3. {ECO:0000255|HAMAP-Rule:MF_00811}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00811}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00811}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000255|HAMAP-Rule:MF_00811}.
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DR EMBL; CP000709; ABQ62359.1; -; Genomic_DNA.
DR RefSeq; WP_002965622.1; NC_009504.1.
DR AlphaFoldDB; A5VVT4; -.
DR SMR; A5VVT4; -.
DR EnsemblBacteria; ABQ62359; ABQ62359; BOV_A0969.
DR GeneID; 45126330; -.
DR GeneID; 55592652; -.
DR KEGG; bov:BOV_A0969; -.
DR HOGENOM; CLU_050859_0_1_5; -.
DR OMA; YFPIQKM; -.
DR PhylomeDB; A5VVT4; -.
DR UniPathway; UPA00034; UER00019.
DR Proteomes; UP000006383; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008666; F:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.166.10; -; 1.
DR HAMAP; MF_00811; DapD; 1.
DR InterPro; IPR005664; DapD_Trfase_Hexpep_rpt_fam.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR023180; THP_succinylTrfase_dom1.
DR InterPro; IPR037133; THP_succinylTrfase_N_sf.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF14602; Hexapep_2; 1.
DR Pfam; PF14805; THDPS_N_2; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR00965; dapD; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Diaminopimelate biosynthesis; Lysine biosynthesis; Repeat; Transferase.
FT CHAIN 1..284
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase"
FT /id="PRO_1000047123"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
SQ SEQUENCE 284 AA; 30753 MW; 9EF76F51038A6350 CRC64;
MTKPDLASLE KTIEKAFDER DGINTATRGE VREAVEQSLI LLDRGEVRVA EKQADGNWHV
NQWLKKAVLL SFRLNPMEVI KGGPGQSSWW DKVPSKFDGW TANEFEKAGF RAVPNCIVRH
SAYIAPNAIL MPSFVNLGAY VDKGAMIDTW ATVGSCAQIG KNVHLSGGVG IGGVLEPMQA
GPTIIEDNCF IGARSEVVEG CIVREGSVLG MGVFIGKSTK IVDRATGEVF YGEVPPYSVV
VAGTMPGKNV PGENWGPSLY CAVIVKRADE KTRSKTSINE LLRD