ID A0A1R1SH20_9ACTN Unreviewed; 333 AA.
AC A0A1R1SH20;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000256|HAMAP-Rule:MF_02122};
DE EC=2.3.1.117 {ECO:0000256|HAMAP-Rule:MF_02122};
DE AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000256|HAMAP-Rule:MF_02122};
DE Short=THDP succinyltransferase {ECO:0000256|HAMAP-Rule:MF_02122};
DE Short=THP succinyltransferase {ECO:0000256|HAMAP-Rule:MF_02122};
DE AltName: Full=Tetrahydropicolinate succinylase {ECO:0000256|HAMAP-Rule:MF_02122};
GN Name=dapD {ECO:0000256|HAMAP-Rule:MF_02122};
GN ORFNames=SPAR_20615 {ECO:0000313|EMBL:OMI37552.1};
OS Streptomyces sparsogenes DSM 40356.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI37552.1, ECO:0000313|Proteomes:UP000186168};
RN [1] {ECO:0000313|EMBL:OMI37552.1, ECO:0000313|Proteomes:UP000186168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI37552.1,
RC ECO:0000313|Proteomes:UP000186168};
RA Coyne S., Seebeck F.P.;
RT "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL Submitted (MAY-2013) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_02122}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_02122}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02122}.
CC -!- SIMILARITY: Belongs to the type 2 tetrahydrodipicolinate N-
CC succinyltransferase family. {ECO:0000256|HAMAP-Rule:MF_02122}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMI37552.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASQP01000287; OMI37552.1; -; Genomic_DNA.
DR RefSeq; WP_065958389.1; NZ_ASQP01000287.1.
DR AlphaFoldDB; A0A1R1SH20; -.
DR STRING; 67365.GCA_001704635_01352; -.
DR UniPathway; UPA00034; UER00019.
DR Proteomes; UP000186168; Unassembled WGS sequence.
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 CDD; cd04649; LbH_THP_succinylT_putative; 1.
DR Gene3D; 3.30.70.2010; -; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 3.30.60.70; Trimeric LpxA-like enzymes; 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 NCBIfam; TIGR03535; DapD_actino; 1.
DR Pfam; PF14602; Hexapep_2; 1.
DR Pfam; PF14789; THDPS_M; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_02122}; Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02122};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02122};
KW Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_02122};
KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02122};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02122};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02122};
KW Reference proteome {ECO:0000313|Proteomes:UP000186168};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02122}.
FT DOMAIN 125..165
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase middle"
FT /evidence="ECO:0000259|Pfam:PF14789"
FT ACT_SITE 214
FT /note="Acyl-anhydride intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 181
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:0000256|HAMAP-Rule:MF_02122"
FT BINDING 198
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:0000256|HAMAP-Rule:MF_02122"
FT BINDING 216
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 231
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 234
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 257
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 272..273
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 280
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 292
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 305..308
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
SQ SEQUENCE 333 AA; 34201 MW; F9B7C5F6D3F2201C CRC64;
MTDAAITTST TSTTGAAAAG LATLAEDGTV LDTWFPAPEL VAEPGPAGTE RLSDERAAEL
LGATVLKAVG PDPRRGVEVV AVRTVIGSLE DKPLDAHDVY LRLHLLSHRL VKPHGLSLDG
QFGLLANVAW TSLGPVPVDQ VERARLAARA EGLQLSVTSV DKFPRMTDYV IPAGVRIGDA
DRVRLGAHLA SGTTVMHEGF VNFNAGTLGT SMVEGRISAG VVVGDGSDIG GGASIMGTLS
GGGKQTISLG ERCLLGAEAG IGISLGDDCI VEAGLYVTAG TRVTLPDGTI TKALELSGVN
NLLFRRNSTT GTVEALPRSG SWGGLNEALH SHN
//
