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Entry: A0A0B9AG81_9SPHN
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ID   A0A0B9AG81_9SPHN        Unreviewed;       278 AA.
AC   A0A0B9AG81;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000256|HAMAP-Rule:MF_00811};
DE            EC=2.3.1.117 {ECO:0000256|HAMAP-Rule:MF_00811};
DE   AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000256|HAMAP-Rule:MF_00811};
DE            Short=THDP succinyltransferase {ECO:0000256|HAMAP-Rule:MF_00811};
DE            Short=THP succinyltransferase {ECO:0000256|HAMAP-Rule:MF_00811};
DE            Short=Tetrahydropicolinate succinylase {ECO:0000256|HAMAP-Rule:MF_00811};
GN   Name=dapD {ECO:0000256|HAMAP-Rule:MF_00811,
GN   ECO:0000313|EMBL:KHS48348.1};
GN   ORFNames=NJ75_01015 {ECO:0000313|EMBL:KHS48348.1};
OS   Novosphingobium subterraneum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=48936 {ECO:0000313|EMBL:KHS48348.1, ECO:0000313|Proteomes:UP000031338};
RN   [1] {ECO:0000313|EMBL:KHS48348.1, ECO:0000313|Proteomes:UP000031338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12447 {ECO:0000313|EMBL:KHS48348.1,
RC   ECO:0000313|Proteomes:UP000031338};
RA   Gan H.M., Gan H.Y., Savka M.A.;
RT   "Draft genome sequence of Novosphingobium subterraneum DSM 12447.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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_00811};
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_00811}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00811}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00811}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000256|ARBA:ARBA00007274, ECO:0000256|HAMAP-Rule:MF_00811}.
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:KHS48348.1}.
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DR   EMBL; JRVC01000004; KHS48348.1; -; Genomic_DNA.
DR   RefSeq; WP_039332075.1; NZ_JRVC01000004.1.
DR   AlphaFoldDB; A0A0B9AG81; -.
DR   STRING; 48936.NJ75_01015; -.
DR   PATRIC; fig|48936.3.peg.1028; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000031338; 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:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   CDD; cd03350; LbH_THP_succinylT; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 1.10.166.10; Tetrahydrodipicolinate-N-succinyltransferase, N-terminal domain; 1.
DR   HAMAP; MF_00811; DapD; 1.
DR   InterPro; IPR005664; DapD_Trfase_Hexpep_rpt_fam.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR023180; THP_succinylTrfase_dom1.
DR   InterPro; IPR037133; THP_succinylTrfase_N_sf.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   NCBIfam; TIGR00965; dapD; 1.
DR   PANTHER; PTHR19136:SF52; 2,3,4,5-TETRAHYDROPYRIDINE-2,6-DICARBOXYLATE N-SUCCINYLTRANSFERASE; 1.
DR   PANTHER; PTHR19136; MOLYBDENUM COFACTOR GUANYLYLTRANSFERASE; 1.
DR   Pfam; PF14602; Hexapep_2; 1.
DR   Pfam; PF14805; THDPS_N_2; 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_00811};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00811}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00811};
KW   Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915,
KW   ECO:0000256|HAMAP-Rule:MF_00811};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW   Rule:MF_00811};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00811};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000313|EMBL:KHS48348.1}.
FT   DOMAIN          4..68
FT                   /note="Tetrahydrodipicolinate-N-succinyltransferase chain
FT                   A"
FT                   /evidence="ECO:0000259|Pfam:PF14805"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00811"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00811"
SQ   SEQUENCE   278 AA;  28849 MW;  61343AACF793887E CRC64;
     MTDQLQAAIE AAWEDRANVT PASDAVREVV EAALELLDSG KARAAEKVDG EWRVNQWLKK
     AVLLSFRLND NAVIEAGSGG APAFDKVPSK FAGWGENRFR EAGFRVVPGA VARKGAHIAK
     GVVLMPSFVN IGAFVDEGTM VDTWATVGSC AQIGKNVHIS GGAGIGGVLE PLQAGPVIIE
     DGAFIGARSE VAEGVIVGEG AVLSMGVYLG ASTKIVDRAT GEVHIGRVPP YAVVVPGAMP
     GKPLPDGTPG PSLYCAVIVK TVDAQTRSKT GINELLRD
//
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