DAPD_ROTMD
ID DAPD_ROTMD Reviewed; 321 AA.
AC D2NS11;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE EC=2.3.1.117 {ECO:0000255|HAMAP-Rule:MF_02122};
DE AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE Short=THDP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE Short=THP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE AltName: Full=Tetrahydropicolinate succinylase {ECO:0000255|HAMAP-Rule:MF_02122};
GN Name=dapD {ECO:0000255|HAMAP-Rule:MF_02122};
GN OrderedLocusNames=RMDY18_06050;
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Rothia.
OX NCBI_TaxID=680646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18;
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of the cyclic tetrahydrodipicolinate
CC (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using
CC succinyl-CoA. {ECO:0000255|HAMAP-Rule:MF_02122}.
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_02122};
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_02122}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_02122}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02122}.
CC -!- SIMILARITY: Belongs to the type 2 tetrahydrodipicolinate N-
CC succinyltransferase family. {ECO:0000255|HAMAP-Rule:MF_02122}.
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DR EMBL; AP011540; BAI64437.1; -; Genomic_DNA.
DR RefSeq; WP_012903150.1; NC_013715.1.
DR AlphaFoldDB; D2NS11; -.
DR SMR; D2NS11; -.
DR STRING; 680646.RMDY18_06050; -.
DR EnsemblBacteria; BAI64437; BAI64437; RMDY18_06050.
DR KEGG; rmu:RMDY18_06050; -.
DR eggNOG; COG2171; Bacteria.
DR HOGENOM; CLU_057490_1_0_11; -.
DR OMA; TVLDTWF; -.
DR OrthoDB; 1251912at2; -.
DR UniPathway; UPA00034; UER00019.
DR Proteomes; UP000001883; 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:0000287; F:magnesium ion binding; 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; 3.30.60.70; -; 1.
DR HAMAP; MF_02122; DapD_type2; 1.
DR InterPro; IPR019875; DapD_actinobacteria.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR032784; THDPS_M.
DR InterPro; IPR038361; THDPS_M_sf.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR InterPro; IPR026586; Type2_DapD.
DR Pfam; PF14602; Hexapep_2; 1.
DR Pfam; PF14789; THDPS_M; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR03535; DapD_actino; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Diaminopimelate biosynthesis; Lysine biosynthesis; Magnesium;
KW Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..321
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase"
FT /id="PRO_0000412267"
FT ACT_SITE 199
FT /note="Acyl-anhydride intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="ligand shared between trimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared between trimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 201
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 216
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 219
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 242
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 257..258
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 265
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 281
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 294..297
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
SQ SEQUENCE 321 AA; 33502 MW; 32EE7C5915DD59D8 CRC64;
MGGMSENTPR YASGVALVNV VISGEHAGTV LDAWFPAPSL TQTPDLSIAD ELEDLAVEHP
ARNARTEVRS ASINLDEAPE DAVDAYLRLH LLSHTLVRPN ELNLDGLFGT LANVAWTNHG
PVLAAEFQKL AIGLRKLGHL SVSHIDKFPR LVDYVVPAGV RIGDGDRLRL GAHLASGTTV
MHEGFVNFNA GTLGTSMVEG RISQGVVVGD GSDVGGGAST MGTLSGGGKK RVSIGERSLL
GAESGIGIAL GDDCVVEAGL YVTAGSRVSV LLPGQEARVV KAAELSGVSN LLFRRNSLSG
AIEVLPRAKN TVELNEALHL N
