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Entry: A0A1H1CZ30_9ACTN
LinkDB: A0A1H1CZ30_9ACTN
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ID   A0A1H1CZ30_9ACTN        Unreviewed;       345 AA.
AC   A0A1H1CZ30;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN04489765_1453 {ECO:0000313|EMBL:SDQ69410.1};
OS   Tsukamurella pulmonis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=47312 {ECO:0000313|EMBL:SDQ69410.1, ECO:0000313|Proteomes:UP000183053};
RN   [1] {ECO:0000313|Proteomes:UP000183053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44142 {ECO:0000313|Proteomes:UP000183053};
RA   Varghese 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; FNLF01000002; SDQ69410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1CZ30; -.
DR   STRING; 47312.SAMN04489765_1453; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000183053; 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};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   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          139..178
FT                   /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT                   succinyltransferase middle"
FT                   /evidence="ECO:0000259|Pfam:PF14789"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        227
FT                   /note="Acyl-anhydride intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT   BINDING         194
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         211
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         229
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT   BINDING         244
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT   BINDING         247
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT   BINDING         270
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT   BINDING         285..286
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT   BINDING         293
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT   BINDING         305
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT   BINDING         318..321
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
SQ   SEQUENCE   345 AA;  35549 MW;  013C4B43A6CECEA6 CRC64;
     MHGIRIRDVR SASTAGAPGP ARPPGTLSDV TNRGAKAYGL ATLTDDGTVL DTWFPAPELT
     EGGGTAGSVQ DPAGAPAELT ALAGADADRK VRTVVVETTI ADLSAAPVDA HDVYLRLHLL
     SHRLVQPHGL SLEGQFGLLA NVVWTNFGPC SPAGFELVRA ALRKRGTVTV LAVDKFPRMV
     DYVLPTGVRI GDPDRVRLGA HLADGTTVMH EGFVNFNAGT LGTAMVEGRI SAGVVIGDHS
     DVGGGASTMG TLSGGGKEII ALGERCLLGA NSGLGIPLGD DCVLEAGLYL TAGTKVTGPD
     GQTIKARELA GKSNLLFRRN SMTGAVEVVP WKSDGVELNA ALHKN
//
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