DAPD_ECOLI
ID DAPD_ECOLI Reviewed; 274 AA.
AC P0A9D8; P03948;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase;
DE EC=2.3.1.117 {ECO:0000269|PubMed:6365916};
DE AltName: Full=Succinyl-CoA: tetrahydrodipicolinate N-succinyltransferase {ECO:0000303|PubMed:6365916};
DE AltName: Full=Tetrahydrodipicolinate N-succinyltransferase;
DE Short=THDP succinyltransferase;
DE Short=THP succinyltransferase;
DE Short=Tetrahydropicolinate succinylase {ECO:0000303|PubMed:6365916};
GN Name=dapD; OrderedLocusNames=b0166, JW0161;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6094577; DOI=10.1016/s0021-9258(17)42677-9;
RA Richaud C., Richaud F., Martin C., Haziza C., Patte J.-C.;
RT "Regulation of expression and nucleotide sequence of the Escherichia coli
RT dapD gene.";
RL J. Biol. Chem. 259:14824-14828(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8412694; DOI=10.1111/j.1365-2958.1993.tb01706.x;
RA van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.;
RT "The genes of the glutamine synthetase adenylylation cascade are not
RT regulated by nitrogen in Escherichia coli.";
RL Mol. Microbiol. 9:443-458(1993).
RN [7]
RP PROTEIN SEQUENCE OF 1-11.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBUNIT, AND PATHWAY.
RX PubMed=6365916; DOI=10.1016/s0021-9258(17)43207-8;
RA Simms S.A., Voige W.H., Gilvarg C.;
RT "Purification and characterization of succinyl-CoA: tetrahydrodipicolinate
RT N-succinyltransferase from Escherichia coli.";
RL J. Biol. Chem. 259:2734-2741(1984).
CC -!- FUNCTION: Catalyzes the formation of N-succinyl-2-amino-6-oxo-L-
CC pimelate from succinyl-CoA and tetrahydrodipicolinate, a key step in
CC lysine biosynthesis via diaminopimelate pathway.
CC {ECO:0000269|PubMed:6365916}.
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 Evidence={ECO:0000269|PubMed:6365916};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17326;
CC Evidence={ECO:0000305|PubMed:6365916};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide, p-
CC chloromercuriphenyl sulfonate, cobalt and copper ions.
CC {ECO:0000269|PubMed:6365916}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for succinyl-CoA (at pH 7.4) {ECO:0000269|PubMed:6365916};
CC KM=22 uM for tetrahydrodipicolinate (THDPA) (at pH 7.4)
CC {ECO:0000269|PubMed:6365916};
CC Note=kcat is 2600 min(-1). {ECO:0000269|PubMed:6365916};
CC pH dependence:
CC Optimum pH is 8.2. {ECO:0000269|PubMed:6365916};
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:0000305|PubMed:6365916}.
CC -!- SUBUNIT: Was originally thought to be a homodimer, but is rather a
CC homotrimer as shown in orthologs. {ECO:0000269|PubMed:6365916,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; K02970; AAA23667.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08595.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73277.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96742.1; -; Genomic_DNA.
DR EMBL; Z21842; CAA79888.1; -; Genomic_DNA.
DR PIR; F64740; XNECSD.
DR RefSeq; NP_414708.1; NC_000913.3.
DR RefSeq; WP_001186650.1; NZ_STEB01000032.1.
DR AlphaFoldDB; P0A9D8; -.
DR SMR; P0A9D8; -.
DR BioGRID; 4259746; 12.
DR BioGRID; 849262; 1.
DR DIP; DIP-31866N; -.
DR IntAct; P0A9D8; 5.
DR STRING; 511145.b0166; -.
DR SWISS-2DPAGE; P0A9D8; -.
DR jPOST; P0A9D8; -.
DR PaxDb; P0A9D8; -.
DR PRIDE; P0A9D8; -.
DR EnsemblBacteria; AAC73277; AAC73277; b0166.
DR EnsemblBacteria; BAB96742; BAB96742; BAB96742.
DR GeneID; 66671546; -.
DR GeneID; 944862; -.
DR KEGG; ecj:JW0161; -.
DR KEGG; eco:b0166; -.
DR PATRIC; fig|1411691.4.peg.2115; -.
DR EchoBASE; EB0203; -.
DR eggNOG; COG2171; Bacteria.
DR HOGENOM; CLU_050859_0_1_6; -.
DR InParanoid; P0A9D8; -.
DR OMA; YFPIQKM; -.
DR PhylomeDB; P0A9D8; -.
DR BioCyc; EcoCyc:MON0-2001; -.
DR BioCyc; MetaCyc:MON0-2001; -.
DR UniPathway; UPA00034; UER00019.
DR PRO; PR:P0A9D8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008666; F:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity; IDA:EcoCyc.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IMP:EcoCyc.
DR GO; GO:0009085; P:lysine biosynthetic process; IDA:EcoCyc.
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 Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Diaminopimelate biosynthesis; Direct protein sequencing;
KW Lysine biosynthesis; Reference proteome; Repeat; Transferase.
FT CHAIN 1..274
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase"
FT /id="PRO_0000196933"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 31
FT /note="V -> D (in Ref. 1; AAA23667)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="G -> R (in Ref. 1; AAA23667)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="I -> M (in Ref. 1; AAA23667)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="V -> L (in Ref. 1; AAA23667)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 29892 MW; 42D7A38610DD3AF6 CRC64;
MQQLQNIIET AFERRAEITP ANADTVTREA VNQVIALLDS GALRVAEKID GQWVTHQWLK
KAVLLSFRIN DNQVIEGAES RYFDKVPMKF ADYDEARFQK EGFRVVPPAA VRQGAFIARN
TVLMPSYVNI GAYVDEGTMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQANPTIIED
NCFIGARSEV VEGVIVEEGS VISMGVYIGQ STRIYDRETG EIHYGRVPAG SVVVSGNLPS
KDGKYSLYCA VIVKKVDAKT RGKVGINELL RTID
