ID DAPD_ALTMD Reviewed; 274 AA.
AC B4RVP7; F2GBY5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-APR-2013, entry version 40.
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=THP succinyltransferase;
DE Short=Tetrahydropicolinate succinylase;
GN Name=dapD; OrderedLocusNames=MADE_1004950;
OS Alteromonas macleodii (strain DSM 17117 / Deep ecotype).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas.
OX NCBI_TaxID=314275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17117 / Deep ecotype;
RX PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A.,
RA Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.;
RT "Comparative genomics of two ecotypes of the marine planktonic
RT copiotroph Alteromonas macleodii suggests alternative lifestyles
RT associated with different kinds of particulate organic matter.";
RL ISME J. 2:1194-1212(2008).
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 -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP001103; AEA97136.1; -; Genomic_DNA.
DR RefSeq; YP_004426134.1; NC_011138.2.
DR ProteinModelPortal; B4RVP7; -.
DR SMR; B4RVP7; 1-274.
DR STRING; 314275.MADE_03035; -.
DR PRIDE; B4RVP7; -.
DR EnsemblBacteria; AEA97136; AEA97136; MADE_1004950.
DR GeneID; 10556331; -.
DR KEGG; amc:MADE_1004950; -.
DR eggNOG; COG2171; -.
DR KO; K00674; -.
DR OMA; NQWAKKA; -.
DR BioCyc; AMAC314275:GHA7-1005-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_1000134027.
SQ SEQUENCE 274 AA; 29280 MW; BEE513784EFAED22 CRC64;
MNELKAIIED AFENRDSISP SSAPDEVRDA VAQAIDLLNS GKGRVAEKIA GEWVVHQWLK
KAVLLFFRLH NNDVIEGAES KFYDKVPLKY TNYTAEQFAA DGARIVPPAA VRTGTFVGKN
AVVMPSYVNI GAFVDEGTMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQANPTIIED
NCFIGARSEI VEGVIVEEGS VISMGVYIGQ STRIYDRETG EIHYGRVPAG SVVVAGNLPS
ADGKYSLYAA IIVKKVDAKT RAKVGINALL RGVE
//
