ID   DAPD_BRUMB              Reviewed;         284 AA.
AC   C0RMG8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 74.
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=BMEA_B1014;
OS   Brucella melitensis biotype 2 (strain ATCC 23457).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=546272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23457;
RA   Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA   Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA   Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA   Han C., Detter J.C., Bruce D., Brettin T.S.;
RT   "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001489; ACO02801.1; -; Genomic_DNA.
DR   RefSeq; WP_004685944.1; NC_012442.1.
DR   AlphaFoldDB; C0RMG8; -.
DR   SMR; C0RMG8; -.
DR   KEGG; bmi:BMEA_B1014; -.
DR   HOGENOM; CLU_050859_0_1_5; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000001748; 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   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; Repeat; Transferase.
FT   CHAIN           1..284
FT                   /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT                   succinyltransferase"
FT                   /id="PRO_1000148582"
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;  30726 MW;  48231A894992DA4B CRC64;
     MTKPDLASLE KTIEKAFDER DGINTATRGE VREAVEQSLI LLDRGEVRVA EKQADGNWHV
     NQWLKKAVLL SFRLNPMEVI KGGPGQSSWW DKVPSKFDGW TANEFEKAGF RAVPSCIVRH
     SAYIAPNAIL MPSFVNLGAY VDKGAMIDTW ATVGSCAQIG KNVHLSGGVG IGGVLEPMQA
     GPTIIEDNCF IGARSEVVEG CIVREGSVLG MGVFIGKSTK IVDRATGEVF YGEVPPYSVV
     VAGTMPGKNV PGENWGPSLY CAVIVKRADE KTRSKTSINE LLRD
//