ID A0A1J4NLG6_9ACTN Unreviewed; 329 AA.
AC A0A1J4NLG6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=WN71_035870 {ECO:0000313|EMBL:OIJ63139.1};
OS Streptomyces mangrovisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428628 {ECO:0000313|EMBL:OIJ63139.1, ECO:0000313|Proteomes:UP000034196};
RN [1] {ECO:0000313|EMBL:OIJ63139.1, ECO:0000313|Proteomes:UP000034196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC149T {ECO:0000313|Proteomes:UP000034196};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces mangrovisoli MUSC 149.";
RL Submitted (OCT-2016) 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:OIJ63139.1}.
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; LAVA02000115; OIJ63139.1; -; Genomic_DNA.
DR RefSeq; WP_046592076.1; NZ_LAVA02000115.1.
DR AlphaFoldDB; A0A1J4NLG6; -.
DR STRING; 1428628.WN71_035870; -.
DR OrthoDB; 9782799at2; -.
DR UniPathway; UPA00034; UER00019.
DR Proteomes; UP000034196; 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:UP000034196};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02122}.
FT DOMAIN 121..161
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase middle"
FT /evidence="ECO:0000259|Pfam:PF14789"
FT ACT_SITE 210
FT /note="Acyl-anhydride intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 177
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 194
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 212
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 227
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 230
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 253
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 268..269
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 276
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 288
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 301..304
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
SQ SEQUENCE 329 AA; 33940 MW; 915EFA7DB89E903E CRC64;
MTEKNAPRPT GAAAAGLATI AADGTVLDTW FPAPELVAEP GPSGTETLSA ERAVELLGEG
AAAAIGPDTR RNVEVVAVRT VIASIDEKPV DAHDVYLRLH LLSHRLVKPH GLSLDGQFGF
LANVAWTSLG PVAVDDLEKV RLNARAEGLH LQVTSVDKFP RMTDYVAPKG VRIADADRVR
LGAHLAEGTT VMHEGFVNFN AGTLGTSMVE GRISAGVVVG NGSDIGGGAS TMGTLSGGGN
VIISIGERCL IGAEAGVGIA LGDECVVEAG LYVTAGTRVS LPDGQIVKAR ELSGASNILF
RRNSVTGAVE ARPNNAVWGG LNEVLHSHN
//
