(data stored in ACNUC7421 zone)

HOGENOM: ACIAC_1_PE2441

ID   ACIAC_1_PE2441                       STANDARD;      PRT;   274 AA.
AC   ACIAC_1_PE2441; A1TQ21;
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   (ACIAC_1.PE2441).
GN   Name=dapD; OrderedLocusNames=Aave_2484;
OS   ACIDOVORAX CITRULLI AAC00-1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIAC_1.PE2441.
CC       Acidovorax avenae subsp. citrulli AAC00-1, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:DAPD_ACIAC
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; A1TQ21; -.
DR   EMBL; CP000512; ABM33059.1; -; Genomic_DNA.
DR   RefSeq; YP_970833.1; NC_008752.1.
DR   ProteinModelPortal; A1TQ21; -.
DR   SMR; A1TQ21; 2-273.
DR   STRING; A1TQ21; -.
DR   GeneID; 4665125; -.
DR   GenomeReviews; CP000512_GR; Aave_2484.
DR   KEGG; aav:Aave_2484; -.
DR   NMPDR; fig|397945.5.peg.2127; -.
DR   eggNOG; COG2171; -.
DR   OMA; KAILLYF; -.
DR   PhylomeDB; A1TQ21; -.
DR   ProtClustDB; PRK11830; -.
DR   BioCyc; AAVE397945:AAVE_2484-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; ACIAC_1.PE2441; -.
KW   Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW   Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis; Repeat;
KW   Transferase.
SQ   SEQUENCE   274 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTQQLQNIID TAWENRASLS PSAAPREVQD AVEHVIAELD AGKLRVATRE GVGQWTVHQW
     IKKAVLLSFR LKDNELIEAG SLGFYDKVPT KFAGRSAAEM AATGVRVVPP AVARRGSFIA
     KGAILMPSYV NIGAYVDEGT MVDTWATVGS CAQVGKHVHL SGGVGLGGVL EPLQANPTII
     EDNCFIGARS EIVEGVIVEE NSVISMGVYI GQSTPIYDRA TDTVSYGRVP AGSVVVSGSL
     PKGDGKYSMY AAIIVKKVDA KTRSTTSLND LLRD
//

If you have problems or comments...

PBIL Back to PBIL home page