(data stored in ACNUC7421 zone)

HOGENOM: ACIAD_1_PE2358

ID   ACIAD_1_PE2358                       STANDARD;      PRT;   273 AA.
AC   ACIAD_1_PE2358; Q6F9A5;
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; Short=THDP succinyltransferase; Short=THP
DE   succinyltransferase; Short=Tetrahydropicolinate succinylase;
DE   (ACIAD_1.PE2358).
GN   Name=dapD; OrderedLocusNames=ACIAD2599;
OS   ACINETOBACTER SP. ADP1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIAD_1.PE2358.
CC       Acinetobacter sp. ADP1 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:DAPD_ACIAD
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; Q6F9A5; -.
DR   EMBL; CR543861; CAG69360.1; -; Genomic_DNA.
DR   RefSeq; YP_047182.1; NC_005966.1.
DR   ProteinModelPortal; Q6F9A5; -.
DR   SMR; Q6F9A5; 1-271.
DR   STRING; Q6F9A5; -.
DR   GeneID; 2878255; -.
DR   GenomeReviews; CR543861_GR; ACIAD2599.
DR   KEGG; aci:ACIAD2599; -.
DR   NMPDR; fig|62977.3.peg.2375; -.
DR   eggNOG; COG2171; -.
DR   OMA; KAILLYF; -.
DR   PhylomeDB; Q6F9A5; -.
DR   ProtClustDB; PRK11830; -.
DR   BioCyc; ASP62977:ACIAD2599-MON; -.
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:EC.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
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; ACIAD_1.PE2358; -.
KW   Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW   Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis; Repeat;
KW   Transferase.
SQ   SEQUENCE   273 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSQLSTIIEQ AFENRANFTA ADCPADIRQA VEEALSGLDN GTLRVAEKID GEWIVHQWLK
     KAVLLSFKLN DNKPIESGDL AFYDKVDTKF AGWTEEQFKE AGVRVVPPAV ARRGSYQAKN
     VVLMPSYVNI GAYVDENTMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQANPTIIED
     NCFIGARSEI VEGVIVEEGA VISMGVYIGQ STRIYDRETG EIHYGRVPAG SVVVPGSLPS
     KDGKYSLYAA IIVKKVDAQT RAKTSLNDLL RAD
//

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