ID   DAPD_ACTP2              Reviewed;         274 AA.
AC   A3N3F7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 102.
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};
GN   OrderedLocusNames=APL_1861;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN74943.1; -; Genomic_DNA.
DR   RefSeq; WP_005599515.1; NC_009053.1.
DR   AlphaFoldDB; A3N3F7; -.
DR   SMR; A3N3F7; -.
DR   STRING; 416269.APL_1861; -.
DR   EnsemblBacteria; ABN74943; ABN74943; APL_1861.
DR   KEGG; apl:APL_1861; -.
DR   eggNOG; COG2171; Bacteria.
DR   HOGENOM; CLU_050859_0_1_6; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000001432; Chromosome.
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   CDD; cd03350; LbH_THP_succinylT; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 1.10.166.10; Tetrahydrodipicolinate-N-succinyltransferase, N-terminal domain; 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   NCBIfam; TIGR00965; dapD; 1.
DR   PANTHER; PTHR19136:SF52; 2,3,4,5-TETRAHYDROPYRIDINE-2,6-DICARBOXYLATE N-SUCCINYLTRANSFERASE; 1.
DR   PANTHER; PTHR19136; MOLYBDENUM COFACTOR GUANYLYLTRANSFERASE; 1.
DR   Pfam; PF14602; Hexapep_2; 1.
DR   Pfam; PF14805; THDPS_N_2; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; Reference proteome;
KW   Repeat; Transferase.
FT   CHAIN           1..274
FT                   /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT                   succinyltransferase"
FT                   /id="PRO_1000047113"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
SQ   SEQUENCE   274 AA;  29692 MW;  91B1CB6831599E4D CRC64;
     MSLQAIIEAA FERRAEITPK TVDAETRAAI EEVIEGLDSG KYRVAEKIDG EWVTHQWLKK
     AVLLSFRIND NQIIDGAETK YYDKVALKFA DYTEERFAQE GFRVVPSATV RKGAYISKNC
     VLMPSYVNIG AYVGEGTMVD TWATVGSCAQ IGKNVHLSGG VGIGGVLEPL QANPTIIGDN
     CFIGARSEVV EGVIVEDGCV ISMGVFIGQS TRIYDRETGE IHYGRVPAGS VVVSGSLPSK
     CGKYSLYCAV IVKKVDAKTL GKVGINELLR TIEE
//