(data stored in ACNUC7421 zone)

HOGENOM: BAQUI1_1_PE60

ID   BAQUI1_1_PE60                        STANDARD;      PRT;   282 AA.
AC   BAQUI1_1_PE60; Q6G1F4;
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   (BAQUI1_1.PE60).
GN   Name=dapD; OrderedLocusNames=BQ00650;
OS   BARTONELLA QUINTANA STR. TOULOUSE.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283165;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BAQUI1_1.PE60.
CC       Bartonella quintana str. Toulouse, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:DAPD_BARQU
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; Q6G1F4; -.
DR   EMBL; BX897700; CAF25572.1; -; Genomic_DNA.
DR   RefSeq; YP_031790.1; NC_005955.1.
DR   ProteinModelPortal; Q6G1F4; -.
DR   SMR; Q6G1F4; 6-281.
DR   GeneID; 2867249; -.
DR   GenomeReviews; BX897700_GR; BQ00650.
DR   KEGG; bqu:BQ00650; -.
DR   NMPDR; fig|283165.1.peg.60; -.
DR   OMA; KAILLYF; -.
DR   PhylomeDB; Q6G1F4; -.
DR   ProtClustDB; PRK11830; -.
DR   BioCyc; BQUI283165:BQ00650-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; BAQUI1_1.PE60; -.
KW   Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW   Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis; Repeat;
KW   Transferase.
SQ   SEQUENCE   282 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTNLTQLEMI IEKAFDDRDS IKTTTKGEIR ESVEHALNLL DKGEIRVAER QKNGQWHVHQ
     WLKKAVLLFF RLNPMQIIAG GVNGTYWWDK VPSKFSNWQE TDFKKANFRS VPGTIVRHSA
     YIAPNVILMP SFVNLGAFID EGTMVDTWAT VGSCAQIGKH VHLSGGVGLG GVLEPLQANP
     TIIEDHCFIG ARSEVVEGCI IREGAVLGMG VFIGKSTKII DRTTGEVFIG EVPAYSVVVP
     GSLPGKPLPN GEVGPNLYCA VIVKRVDQKT REKTSINDLL RD
//

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