(data stored in ACNUC7421 zone)

SWISSPROT: DAPD_ECO57

ID   DAPD_ECO57              Reviewed;         274 AA.
AC   Q8X8Y7; Q7AHM1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAY-2019, entry version 116.
DE   RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase;
DE            EC=2.3.1.117;
DE   AltName: Full=Tetrahydrodipicolinate N-succinyltransferase;
DE            Short=THDP succinyltransferase;
DE            Short=THP succinyltransferase;
DE            Short=Tetrahydropicolinate succinylase;
GN   Name=dapD; OrderedLocusNames=Z0176, ECs0168;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=18242192; DOI=10.1016/j.febslet.2008.01.032;
RA   Nguyen L., Kozlov G., Gehring K.;
RT   "Structure of Escherichia coli tetrahydrodipicolinate N-
RT   succinyltransferase reveals the role of a conserved C-terminal helix
RT   in cooperative substrate binding.";
RL   FEBS Lett. 582:623-626(2008).
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   -!- 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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
DR   EMBL; AE005174; AAG54468.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33591.1; -; Genomic_DNA.
DR   PIR; H85500; H85500.
DR   PIR; H90649; H90649.
DR   RefSeq; NP_308195.1; NC_002695.1.
DR   RefSeq; WP_001186649.1; NZ_SDVX01000001.1.
DR   PDB; 3BXY; X-ray; 2.00 A; A=2-274.
DR   PDBsum; 3BXY; -.
DR   SMR; Q8X8Y7; -.
DR   STRING; 155864.EDL933_0169; -.
DR   EnsemblBacteria; AAG54468; AAG54468; Z0176.
DR   EnsemblBacteria; BAB33591; BAB33591; BAB33591.
DR   GeneID; 913832; -.
DR   KEGG; ece:Z0176; -.
DR   KEGG; ecs:ECs0168; -.
DR   PATRIC; fig|386585.9.peg.269; -.
DR   eggNOG; ENOG4105DMJ; Bacteria.
DR   eggNOG; COG2171; LUCA.
DR   HOGENOM; HOG000003295; -.
DR   KO; K00674; -.
DR   BioCyc; ECOO157:DAPD-MONOMER; -.
DR   BRENDA; 2.3.1.117; 2026.
DR   UniPathway; UPA00034; UER00019.
DR   EvolutionaryTrace; Q8X8Y7; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   1: Evidence at protein level;
DR   PRODOM; Q8X8Y7.
DR   SWISS-2DPAGE; Q8X8Y7.
KW   3D-structure; Acyltransferase; Amino-acid biosynthesis;
KW   Complete proteome; Cytoplasm; Diaminopimelate biosynthesis;
KW   Lysine biosynthesis; Reference proteome; Repeat; Transferase.
FT   CHAIN         1    274       2,3,4,5-tetrahydropyridine-2,6-
FT                                dicarboxylate N-succinyltransferase.
FT                                /FTId=PRO_0000196934.
FT   BINDING     104    104       Substrate. {ECO:0000250}.
FT   BINDING     141    141       Substrate. {ECO:0000250}.
FT   HELIX         2     13       {ECO:0000244|PDB:3BXY}.
FT   HELIX        14     17       {ECO:0000244|PDB:3BXY}.
FT   TURN         20     22       {ECO:0000244|PDB:3BXY}.
FT   HELIX        25     39       {ECO:0000244|PDB:3BXY}.
FT   STRAND       45     49       {ECO:0000244|PDB:3BXY}.
FT   STRAND       52     55       {ECO:0000244|PDB:3BXY}.
FT   HELIX        57     69       {ECO:0000244|PDB:3BXY}.
FT   STRAND       73     76       {ECO:0000244|PDB:3BXY}.
FT   STRAND       81     86       {ECO:0000244|PDB:3BXY}.
FT   TURN         89     92       {ECO:0000244|PDB:3BXY}.
FT   HELIX        95    101       {ECO:0000244|PDB:3BXY}.
FT   STRAND      110    112       {ECO:0000244|PDB:3BXY}.
FT   STRAND      125    128       {ECO:0000244|PDB:3BXY}.
FT   STRAND      144    146       {ECO:0000244|PDB:3BXY}.
FT   STRAND      214    216       {ECO:0000244|PDB:3BXY}.
FT   TURN        217    219       {ECO:0000244|PDB:3BXY}.
FT   STRAND      225    227       {ECO:0000244|PDB:3BXY}.
FT   STRAND      231    239       {ECO:0000244|PDB:3BXY}.
FT   STRAND      241    244       {ECO:0000244|PDB:3BXY}.
FT   STRAND      246    255       {ECO:0000244|PDB:3BXY}.
FT   HELIX       258    260       {ECO:0000244|PDB:3BXY}.
FT   HELIX       266    271       {ECO:0000244|PDB:3BXY}.
SQ   SEQUENCE   274 AA;  29878 MW;  13D6A38610DCFC2D CRC64;
     MQQLQNIIET AFERRAEITP ANADTVTREA VNQVIALLDS GALRVAEKID GQWVTHQWLK
     KAVLLSFRIN DNQVIEGAES RYFDKVPMKF ADYDEARFQK EGFRVVPPAA VRQGAFIARN
     TVLMPSYVNI GAYVDEGTMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQANPTIIED
     NCFIGARSEV VEGVIVEEGS VISMGVYIGQ STRIYDRETG DIHYGRVPAG SVVVSGNLPS
     KDGKYSLYCA VIVKKVDAKT RGKVGINELL RTID
//

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