(data stored in ACNUC9543 zone)

SWISSPROT: DAPD_YERPA

ID   DAPD_YERPA              Reviewed;         274 AA.
AC   Q1CAN9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, entry version 83.
DE   RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE            EC=2.3.1.117 {ECO:0000255|HAMAP-Rule:MF_00811};
DE   AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE            Short=THDP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE            Short=THP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE            Short=Tetrahydropicolinate succinylase {ECO:0000255|HAMAP-Rule:MF_00811};
GN   Name=dapD {ECO:0000255|HAMAP-Rule:MF_00811};
GN   OrderedLocusNames=YPA_0515;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA =
CC         CoA + L-2-succinylamino-6-oxopimelate; Xref=Rhea:RHEA:17325,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15685, ChEBI:CHEBI:16845,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=2.3.1.117;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00811};
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. {ECO:0000255|HAMAP-Rule:MF_00811}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00811}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00811}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000255|HAMAP-Rule:MF_00811}.
DR   EMBL; CP000308; ABG12483.1; -; Genomic_DNA.
DR   RefSeq; WP_002212128.1; NZ_CP009906.1.
DR   SMR; Q1CAN9; -.
DR   PRIDE; Q1CAN9; -.
DR   EnsemblBacteria; ABG12483; ABG12483; YPA_0515.
DR   KEGG; ypa:YPA_0515; -.
DR   HOGENOM; HOG000003295; -.
DR   KO; K00674; -.
DR   OMA; YFPIQKM; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000001971; Chromosome.
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:UniProtKB-UniRule.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.166.10; -; 1.
DR   HAMAP; MF_00811; DapD; 1.
DR   InterPro; IPR005664; DapD_Trfase_Hexpep_rpt_fam.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR023180; THP_succinylTrfase_dom1.
DR   InterPro; IPR037133; THP_succinylTrfase_N_sf.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF14602; Hexapep_2; 1.
DR   Pfam; PF14805; THDPS_N_2; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR00965; dapD; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q1CAN9.
DR   SWISS-2DPAGE; Q1CAN9.
KW   Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW   Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis; Repeat;
KW   Transferase.
FT   CHAIN         1    274       2,3,4,5-tetrahydropyridine-2,6-
FT                                dicarboxylate N-succinyltransferase.
FT                                /FTId=PRO_1000047199.
FT   BINDING     104    104       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00811}.
FT   BINDING     141    141       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00811}.
SQ   SEQUENCE   274 AA;  29937 MW;  5BA5F77C11D66282 CRC64;
     MQQLQNVIET AFERRADITP ANVDTVTREA ITHVIDLLDT GALRVAEKID GQWVTHQWLK
     KAVLLSFRIN DNQVMEGAET RYYDKVPMKF AGYDEARFQR EGFRVVPPAT VRKGAFIARN
     TVLMPSYVNI GAFVDEGTMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQANPTIIED
     NCFVGARSEV VEGVIVEEGS VISMGVFIGQ STRIYDRETG EVHYGRVPAG SVVVSGNLPS
     KDGSYSLYCA VIVKKVDAKT RSKVGINELL RTID
//

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