ID A0A0F2TDW6_STRR3 Unreviewed; 330 AA.
AC A0A0F2TDW6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=VM95_15545 {ECO:0000313|EMBL:KJS61408.1};
OS Streptomyces rubellomurinus (strain ATCC 31215).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=359131 {ECO:0000313|EMBL:KJS61408.1, ECO:0000313|Proteomes:UP000033699};
RN [1] {ECO:0000313|EMBL:KJS61408.1, ECO:0000313|Proteomes:UP000033699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31215 {ECO:0000313|EMBL:KJS61408.1,
RC ECO:0000313|Proteomes:UP000033699};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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:KJS61408.1}.
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DR EMBL; JZKH01000027; KJS61408.1; -; Genomic_DNA.
DR RefSeq; WP_045696900.1; NZ_JZKH01000027.1.
DR AlphaFoldDB; A0A0F2TDW6; -.
DR PATRIC; fig|359131.3.peg.3447; -.
DR UniPathway; UPA00034; UER00019.
DR Proteomes; UP000033699; 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:UP000033699};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02122}.
FT DOMAIN 122..162
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase middle"
FT /evidence="ECO:0000259|Pfam:PF14789"
FT ACT_SITE 211
FT /note="Acyl-anhydride intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 178
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 195
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 213
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 228
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 254
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 269..270
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 277
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 289
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 302..305
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
SQ SEQUENCE 330 AA; 33827 MW; DD5E4C91268128F4 CRC64;
MTAESTTPRP NGAVATGLAT IAADGTVLDT WYPAPALADE PGPAGTVRLT AEQAEAELGA
GAAEALRTDA RRGVEVVAVR TTIASLDEKP LDTHDVYLRL HLLSHRLVQP HGQNLDGIFG
LLANVAWTSI GPVPVDQVEQ ARLAVRAQGG QLAVYGVDKF PRMTDYVAPG GVRIAHADRV
RLGAHLAAGT TVMHEGFVNF NAGTLGTSMV EGRISAGVVV GDHSDIGGGA SIMGTLSGGG
KQVVSVGQRC LLGANAGIGI SLGNDCVVEA GLYVTAGTRV TTPDGTVAKA VELSGQDNLL
FRRNSQTGAV EVIARSGSWG GLNADLHAHN
//
