ID   DAPD_ROSDO              Reviewed;         275 AA.
AC   Q16DM5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=RD1_0189;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG29918.1; -; Genomic_DNA.
DR   RefSeq; WP_011566540.1; NZ_FOOO01000015.1.
DR   AlphaFoldDB; Q16DM5; -.
DR   SMR; Q16DM5; -.
DR   STRING; 375451.RD1_0189; -.
DR   EnsemblBacteria; ABG29918; ABG29918; RD1_0189.
DR   KEGG; rde:RD1_0189; -.
DR   eggNOG; COG2171; Bacteria.
DR   HOGENOM; CLU_050859_0_1_5; -.
DR   OMA; YFPIQKM; -.
DR   OrthoDB; 752123at2; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000007029; 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   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; Reference proteome;
KW   Repeat; Transferase.
FT   CHAIN           1..275
FT                   /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT                   succinyltransferase"
FT                   /id="PRO_1000047179"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
SQ   SEQUENCE   275 AA;  29028 MW;  12EACD7988235A44 CRC64;
     MSNAELETAI EAAWEARDSI SPATKGAERD AIEATLAALD GGGLRVAERQ ADGNWHVNQW
     AKKAVLLGFR IKDMEMQSGG AQGGGWWDKV DSKFAGWGEA DWKDAGFRAV PNCVVRKSAY
     IAPGVVLMPS FVNLGAYVDE GTMVDTWATV GSCAQIGKNV HLSGGVGIGG VLEPMQAGPT
     IIEDNCFIGA RSEVVEGCIV REGSVLGMGV FIGKSTKIVD RETGEFTYGE VPAGSVVVAG
     SMPSKNGVNL YCAVIVKKVD AQTRSKTSIN ELLRD