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Database: UniProt
Entry: B9MJK9
LinkDB: B9MJK9
Original site: B9MJK9 
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   29-OCT-2014, entry version 44.
DE   RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE            EC=2.3.1.117 {ECO:0000255|HAMAP-Rule:MF_00811};
DE   AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE            Short=THDP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE            Short=THP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE            Short=Tetrahydropicolinate succinylase {ECO:0000255|HAMAP-Rule:MF_00811};
GN   Name=dapD {ECO:0000255|HAMAP-Rule:MF_00811};
GN   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. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00811}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00811}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00811}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000255|HAMAP-Rule:MF_00811}.
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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; SCAQVGA; -.
DR   OrthoDB; EOG68H8BV; -.
DR   BioCyc; AEBR535289:GHOO-1921-MONOMER; -.
DR   UniPathway; UPA00034; UER00019.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008666; F:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-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; 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; 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. {ECO:0000255|HAMAP-
FT                                Rule:MF_00811}.
FT   BINDING     143    143       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00811}.
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
//
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