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Database: UniProt
Entry: A0A1I3TXM6_9RHOB
LinkDB: A0A1I3TXM6_9RHOB
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ID   A0A1I3TXM6_9RHOB        Unreviewed;       275 AA.
AC   A0A1I3TXM6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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   ORFNames=SAMN04488138_109133 {ECO:0000313|EMBL:SFJ75223.1};
OS   Celeribacter halophilus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=576117 {ECO:0000313|EMBL:SFJ75223.1, ECO:0000313|Proteomes:UP000183299};
RN   [1] {ECO:0000313|EMBL:SFJ75223.1, ECO:0000313|Proteomes:UP000183299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.8891 {ECO:0000313|EMBL:SFJ75223.1,
RC   ECO:0000313|Proteomes:UP000183299};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FORY01000009; SFJ75223.1; -; Genomic_DNA.
DR   RefSeq; WP_066601243.1; NZ_QKZJ01000009.1.
DR   AlphaFoldDB; A0A1I3TXM6; -.
DR   STRING; 576117.SAMN04488138_109133; -.
DR   OrthoDB; 9775362at2; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000183299; 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}; Reference proteome {ECO:0000313|Proteomes:UP000183299};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00811};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000313|EMBL:SFJ75223.1}.
FT   DOMAIN          5..71
FT                   /note="Tetrahydrodipicolinate-N-succinyltransferase chain
FT                   A"
FT                   /evidence="ECO:0000259|Pfam:PF14805"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00811"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00811"
SQ   SEQUENCE   275 AA;  29241 MW;  BBFED49431A4B487 CRC64;
     MSNAQLEAAI EAAWDARDTI TPATGGETRE AIEATLNALD HGEIRVAEKQ EDGNWSVNQW
     AKKAVLLGFR IKDMELHDGG PQGSGWWDKV DSKFKGWGTA EFTEAGFRAV PNAVVRKSAY
     IAPGVVLMPS FVNLGAYVDS GTMVDTWATV GSCAQIGKNV HLSGGAGIGG VLEPLQAGPV
     IIEDNCFIGA RAEVAEGVIV REGSVLGMGV YLGQSTKIVD RETGEVFYGE VPPYSVVVAG
     TMPSRNGVNL YCAVIVKRVD AKTRSKTGIN ELLRD
//
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