ID A0A1H8EXK2_9BURK Unreviewed; 275 AA.
AC A0A1H8EXK2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN05428959_101827 {ECO:0000313|EMBL:SEN24212.1};
OS Duganella sp. CF517.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1881038 {ECO:0000313|EMBL:SEN24212.1, ECO:0000313|Proteomes:UP000198691};
RN [1] {ECO:0000313|Proteomes:UP000198691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF517 {ECO:0000313|Proteomes:UP000198691};
RA Varghese N., Submissions S.;
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; FODC01000001; SEN24212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8EXK2; -.
DR STRING; 1881038.SAMN05428959_101827; -.
DR OrthoDB; 9775362at2; -.
DR UniPathway; UPA00034; UER00019.
DR Proteomes; UP000198691; 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; IPR018357; Hexapep_transf_CS.
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.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000198691};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00811};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00811}.
FT DOMAIN 4..70
FT /note="Tetrahydrodipicolinate-N-succinyltransferase chain
FT A"
FT /evidence="ECO:0000259|Pfam:PF14805"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00811"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00811"
SQ SEQUENCE 275 AA; 29542 MW; 171464D65AF72B4C CRC64;
MTQQLQQIID QAWEDRANIN PANGAAELRD AVSHVIAGLD AGTIRVAEKT TGDWVVNQWV
KKAVLLSFRL ENNVVMPSDG TMQFYDKVPT KFANYTPEDF AKGGFRVVPP AVARRGSFIA
KNVVLMPSYV NIGAYVDEGA MVDTWATVGS CAQIGKNVHL SGGVGIGGVL EPMQANPTII
EDNCFIGARS EIVEGVIVEE NSVISMGVYI GQSTKIYDRA TGEVTYGRVP AGSVVVSGNL
PSEDGKYSLY CAVIVKRVDA KTRAKTGINE LLRGI
//
