(data stored in ACNUC7421 zone)

HOGENOM: ECOKI_1_PE165

ID   ECOKI_1_PE165                        STANDARD;      PRT;   274 AA.
AC   ECOKI_1_PE165; D5CV98;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate
DE   N-succinyltransferase; EC=2.3.1 117;AltName: Full=Tetrahydrodipicolinate
DE   N-succinyltransferase; (ECOKI_1.PE165).
GN   Name=dapD; OrderedLocusNames=ECOK1_0167;
OS   ESCHERICHIA COLI IHE3034.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=714962;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOKI_1.PE165.
CC       Escherichia coli O18:K1:H7 (strain IHE3034 / ExPEC) chromosome, complet
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D5CV98_ECOKI
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.
CC   -!- GENE_FAMILY: HOG000003295 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D5CV98; -.
DR   EMBL; CP001969; ADE92429.1; -; Genomic_DNA.
DR   ProteinModelPortal; D5CV98; -.
DR   SMR; D5CV98; 2-274.
DR   EnsemblBacteria; EBESCT00000228196; EBESCP00000213747; EBESCG00000227054.
DR   GenomeReviews; CP001969_GR; ECOK1_0167.
DR   GeneTree; EBGT00050000010899; -.
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   HAMAP; MF_00811; DapD; 1; -.
DR   InterPro; IPR005664; DapD.
DR   InterPro; IPR001451; Hexapep_transf.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR023180; THP_succinylTrfase_dom1.
DR   InterPro; IPR011004; Trimer_LpxA-like.
DR   Gene3D; G3DSA:1.10.166.10; THP_succinylTrfase_dom1; 1.
DR   Pfam; PF00132; Hexapep; 2.
DR   SUPFAM; SSF51161; Trimer_LpxA_like; 1.
DR   TIGRFAMs; TIGR00965; DapD; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
DR   HOGENOMDNA; ECOKI_1.PE165; -.
KW   ADE92429.1000068575old_1320000031;
KW   Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW   Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis; Repeat;
KW   Transferase.
SQ   SEQUENCE   274 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQQLQNIIET AFERRAEITP ANADTVTREA VNQVIALLDS GALRVAEKID GQWVTHQWLK
     KAVLLSFRIN DNQVIEGAES RYFDKVPMKF ANYDEARFQK EGFRVVPPAA VRQGAFIARN
     TVLMPSYVNI GAYVDEGTMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQANPTIIED
     NCFIGARSEV VEGVIVEEGS VISMGVYIGQ STRIYDRETG EIHYGRVPAG SVVVSGNLPS
     KDGKYSLYCA VIVKKVDAKT RGKVGINELL RTID
//

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