ID DAPD_ACIET Reviewed; 274 AA.
AC B9MJK9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 37.
DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase;
DE EC=2.3.1.117;
DE AltName: Full=Tetrahydrodipicolinate N-succinyltransferase;
DE Short=THDP succinyltransferase;
DE Short=THP succinyltransferase;
DE Short=Tetrahydropicolinate succinylase;
GN Name=dapD; OrderedLocusNames=Dtpsy_1890;
OS Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=535289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TPSY;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Coates J.D.;
RT "Complete sequence of Diaphorobacter sp. TPSY.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-
CC 2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6-
CC oxoheptanedioate.
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.
CC -!- SUBUNIT: Homotrimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
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DR EMBL; CP001392; ACM33347.1; -; Genomic_DNA.
DR RefSeq; YP_002553347.1; NC_011992.1.
DR ProteinModelPortal; B9MJK9; -.
DR STRING; 535289.Dtpsy_1890; -.
DR PRIDE; B9MJK9; -.
DR EnsemblBacteria; ACM33347; ACM33347; Dtpsy_1890.
DR GeneID; 7382251; -.
DR KEGG; dia:Dtpsy_1890; -.
DR PATRIC; 21780885; VBIDiaSp55748_1929.
DR eggNOG; COG2171; -.
DR HOGENOM; HOG000003295; -.
DR KO; K00674; -.
DR OMA; IMPSFIN; -.
DR ProtClustDB; PRK11830; -.
DR BioCyc; AEBR535289:GHOO-1921-MONOMER; -.
DR UniPathway; UPA00034; UER00019.
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:HAMAP.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:HAMAP.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:HAMAP.
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_transf.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR023180; THP_succinylTrfase_dom1.
DR InterPro; IPR011004; Trimer_LpxA-like.
DR PANTHER; PTHR19136:SF52; PTHR19136:SF52; 1.
DR Pfam; PF00132; Hexapep; 2.
DR SUPFAM; SSF51161; Trimer_LpxA_like; 1.
DR TIGRFAMs; TIGR00965; dapD; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis; Repeat;
KW Transferase.
FT CHAIN 1 274 2,3,4,5-tetrahydropyridine-2,6-
FT dicarboxylate N-succinyltransferase.
FT /FTId=PRO_1000148583.
FT BINDING 106 106 Substrate (By similarity).
FT BINDING 143 143 Substrate (By similarity).
SQ SEQUENCE 274 AA; 29318 MW; DEE6C06B520E2892 CRC64;
MTQQLQTLID NAWDNRASLS PSAAPKEVVD AVEHVIAELN NGRLRVATRE GVGQWTVHQW
IKKAVLLSFR LKDNELMKAG DLGFFDKVPT KFAHLSADEM AATGVRVVPP AVARRGSFIA
KGAILMPSYV NIGAYVDEGT MVDTWATVGS CAQVGKNVHL SGGVGLGGVL EPLQANPTII
EDNCFIGARS EVVEGVIVEE NSVISMGVYI GQSTPIYDRT TGETTYGRVP AGSVVVSGNL
PKDGGRYSMY AAIIVKKVDA KTRSTTSLND LLRD
//
