(data stored in ACNUC7421 zone)

HOGENOM: BURM1_2_PE1240

ID   BURM1_2_PE1240                       STANDARD;      PRT;   275 AA.
AC   BURM1_2_PE1240; A9AHT0;
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=THP succinyltransferase;
DE   Short=Tetrahydropicolinate succinylase; (BURM1_2.PE1240).
GN   Name=dapD; OrderedLocusNames=Bmul_1247, BMULJ_02000;
OS   BURKHOLDERIA MULTIVORANS ATCC 17616.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BURM1_2.PE1240.
CC       Burkholderia multivorans ATCC 17616 chromosome chromosome 1, complete
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:DAPD_BURM1
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   -!- GENE_FAMILY: HOG000003295 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A9AHT0; -.
DR   EMBL; CP000868; ABX14935.1; -; Genomic_DNA.
DR   EMBL; AP009385; BAG43917.1; -; Genomic_DNA.
DR   RefSeq; YP_001579432.1; NC_010084.1.
DR   RefSeq; YP_001946453.1; NC_010804.1.
DR   ProteinModelPortal; A9AHT0; -.
DR   SMR; A9AHT0; 3-273.
DR   STRING; A9AHT0; -.
DR   GeneID; 5766517; -.
DR   GeneID; 6359170; -.
DR   GenomeReviews; AP009385_GR; BMULJ_02000.
DR   GenomeReviews; CP000868_GR; Bmul_1247.
DR   KEGG; bmj:BMULJ_02000; -.
DR   KEGG; bmu:Bmul_1247; -.
DR   OMA; KAILLYF; -.
DR   ProtClustDB; PRK11830; -.
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; BURM1_2.PE1240; -.
KW   Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW   Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis; Repeat;
KW   Transferase.
SQ   SEQUENCE   275 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSQQLQQIID NAWENRAELS PKAAPAEVRE AVAHAIEQLD KGALRVAEKI DGNWTVHQWL
     KKAVLLSFRL EDNAPMPAGG YSQFYDKVPS KFANYTAEDF AAGGFRVVPP AIARRGSFIA
     KNVVLMPSYT NIGAYVDEGT MVDTWATVGS CAQIGKNVHL SGGVGIGGVL EPLQANPVII
     EDNCFIGARS EVVEGVIVEE NSVISMGVYL GQSTKIYDRE TGEISYGRIP AGSVVVAGNL
     PSKDGSHSLY CAVIVKKVDA KTRAKVGLNE LLRGD
//

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