ID A0A1I0VD15_9ACTN Unreviewed; 313 AA.
AC A0A1I0VD15;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN05192575_101140 {ECO:0000313|EMBL:SFA74255.1};
OS Nocardioides alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=748909 {ECO:0000313|EMBL:SFA74255.1, ECO:0000313|Proteomes:UP000199113};
RN [1] {ECO:0000313|EMBL:SFA74255.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10697 {ECO:0000313|EMBL:SFA74255.1};
RA de Groot N.N.;
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}.
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DR EMBL; FOKC01000001; SFA74255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0VD15; -.
DR STRING; 748909.SAMN05192575_101140; -.
DR OrthoDB; 9782799at2; -.
DR UniPathway; UPA00034; UER00019.
DR Proteomes; UP000199113; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02122}.
FT DOMAIN 98..138
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase middle"
FT /evidence="ECO:0000259|Pfam:PF14789"
FT ACT_SITE 187
FT /note="Acyl-anhydride intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 154
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 171
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 189
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 204
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 207
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 245..246
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 269
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 282..285
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
SQ SEQUENCE 313 AA; 32003 MW; 5497967FBEAD892A CRC64;
MTAASGFGLA TLSGDTVLDV WFPSPVLGAT AGDAPAELTA LEGRDDARDV RSEVRLVEIA
DLADAPASTE DVWLRLHLLS TRLVQPHGMS MDGVFGLLTN VVWTSAGPCA VEGFEATRAR
LRATGQHVTV FGVDKFPRLV DYVMPSGVRI ADADRVRLGA HLAEGTTVMH EGFVNFNAGT
LGTSMVEGRI SAGVVVGDGS DVGGGSSIMG TLSGGGKEVI SVGQRCLLGA NAGIGISLGD
DCVVEAGCYV TAGTKVTVKD MDGKPQVVKA ASLSGVDNIL FRRNSVSGAI EAVPWKGGSD
GAGIALNAAL HAN
//
