ID A0A4Y7B6L1_9BURK Unreviewed; 274 AA. AC A0A4Y7B6L1; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 26-FEB-2020, entry version 5. 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:ROZ68579.1}; GN ORFNames=EEB15_25175 {ECO:0000313|EMBL:ROZ68579.1}; OS Ramlibacter sp. WS9. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Ramlibacter; unclassified Ramlibacter. OX NCBI_TaxID=1882741 {ECO:0000313|EMBL:ROZ68579.1, ECO:0000313|Proteomes:UP000317475}; RN [1] {ECO:0000313|EMBL:ROZ68579.1, ECO:0000313|Proteomes:UP000317475} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WS9 {ECO:0000313|EMBL:ROZ68579.1, RC ECO:0000313|Proteomes:UP000317475}; RA Larke-Mejia N.L., Murrell J.C.; RT "Identification of active isoprene-degradading bacteria from willow soil RT using DNA-Stable Isotope Probing (SIP)."; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = CoA CC + L-2-succinylamino-6-oxopimelate; 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 ECO:0000256|SAAS:SAAS01124328}; 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 ECO:0000256|SAAS:SAAS00681956}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00811}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00811, CC ECO:0000256|SAAS:SAAS00681965}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. CC {ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS00672410}. 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:ROZ68579.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; RKMB01000022; ROZ68579.1; -; Genomic_DNA. DR UniPathway; UPA00034; UER00019. DR Proteomes; UP000317475; 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 Gene3D; 1.10.166.10; -; 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 Pfam; PF14602; Hexapep_2; 1. DR Pfam; PF14805; THDPS_N_2; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR00965; dapD; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00811, KW ECO:0000256|SAAS:SAAS00681961, ECO:0000313|EMBL:ROZ68579.1}; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00811, KW ECO:0000256|SAAS:SAAS00681960}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS00681955}; KW Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00811, KW ECO:0000256|SAAS:SAAS00681957}; KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00811, KW ECO:0000256|SAAS:SAAS00681953}; KW Reference proteome {ECO:0000313|Proteomes:UP000317475}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS00681954}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00811, KW ECO:0000256|SAAS:SAAS00681963, ECO:0000313|EMBL:ROZ68579.1}. FT DOMAIN 4..71 FT /note="THDPS_N_2" FT /evidence="ECO:0000259|Pfam:PF14805" FT BINDING 106 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00811" FT BINDING 143 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00811" SQ SEQUENCE 274 AA; 29454 MW; BA12D2B8997F95CA CRC64; MTQQLQQIID NAWENRAGIS VKTVSKEVSE AVEHVIAELN NGHLRVATRE SVGQWTVHQW IKKAVLLSFR LRDNEIVRAG DLGFYDKVPT KFAHLTPEEM AATGVRVVPP AVARRGSFIA KGAILMPSYV NIGAYVDEAT MVDTWATVGS CAQIGKNVHL SGGVGIGGVL EPVQAGPTII EDNCFIGARS EVVEGVIVEE NSVISMGVYI GQSTKIYDRA TGTVTYGRIP AGSVVVSGNL PSADGKYSLY CAVIVKRVDA QTRAKTSLND LLRD //