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 03-AUG-2022, entry version 127.
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., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA 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., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT 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-succinyltransferase
RT reveals the role of a conserved C-terminal helix in cooperative substrate
RT binding.";
RL FEBS Lett. 582:623-626(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-
CC 2-succinylamino-6-oxoheptanedioate + CoA; 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}.
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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_SWKA01000005.1.
DR PDB; 3BXY; X-ray; 2.00 A; A=2-274.
DR PDBsum; 3BXY; -.
DR AlphaFoldDB; Q8X8Y7; -.
DR SMR; Q8X8Y7; -.
DR STRING; 155864.EDL933_0169; -.
DR EnsemblBacteria; AAG54468; AAG54468; Z0176.
DR EnsemblBacteria; BAB33591; BAB33591; ECs_0168.
DR GeneID; 913832; -.
DR KEGG; ece:Z0176; -.
DR KEGG; ecs:ECs_0168; -.
DR PATRIC; fig|386585.9.peg.269; -.
DR eggNOG; COG2171; Bacteria.
DR HOGENOM; CLU_050859_0_1_6; -.
DR OMA; YFPIQKM; -.
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;
KW 3D-structure; Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Diaminopimelate biosynthesis; Lysine biosynthesis; Reference proteome;
KW Repeat; Transferase.
FT CHAIN 1..274
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase"
FT /id="PRO_0000196934"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:3BXY"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:3BXY"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:3BXY"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:3BXY"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:3BXY"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:3BXY"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:3BXY"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3BXY"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3BXY"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:3BXY"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:3BXY"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3BXY"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3BXY"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3BXY"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:3BXY"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:3BXY"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:3BXY"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:3BXY"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:3BXY"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:3BXY"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3BXY"
FT HELIX 266..271
FT /evidence="ECO:0007829|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
