DAPD_CAMJE
ID DAPD_CAMJE Reviewed; 386 AA.
AC Q0P823;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE EC=2.3.1.117 {ECO:0000255|HAMAP-Rule:MF_02122};
DE AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE Short=THDP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE Short=THP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE AltName: Full=Tetrahydropicolinate succinylase {ECO:0000255|HAMAP-Rule:MF_02122};
GN Name=dapD {ECO:0000255|HAMAP-Rule:MF_02122}; OrderedLocusNames=Cj1605c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of putative 2,3,4,5-tetrahydropyridine-2-carboxylate N-
RT succinyltransferase (NP_282733.1) from Campylobacter jejuni at 1.90 A
RT resolution.";
RL Submitted (MAR-2011) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of the cyclic tetrahydrodipicolinate
CC (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using
CC succinyl-CoA. {ECO:0000255|HAMAP-Rule:MF_02122}.
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:0000255|HAMAP-Rule:MF_02122};
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_02122}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_02122}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02122}.
CC -!- SIMILARITY: Belongs to the type 2 tetrahydrodipicolinate N-
CC succinyltransferase family. {ECO:0000255|HAMAP-Rule:MF_02122}.
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DR EMBL; AL111168; CAL35702.1; -; Genomic_DNA.
DR PIR; C81256; C81256.
DR RefSeq; WP_002851311.1; NC_002163.1.
DR RefSeq; YP_002344974.1; NC_002163.1.
DR PDB; 2RIJ; X-ray; 1.90 A; A=1-386.
DR PDBsum; 2RIJ; -.
DR AlphaFoldDB; Q0P823; -.
DR SMR; Q0P823; -.
DR IntAct; Q0P823; 3.
DR STRING; 192222.Cj1605c; -.
DR PaxDb; Q0P823; -.
DR PRIDE; Q0P823; -.
DR EnsemblBacteria; CAL35702; CAL35702; Cj1605c.
DR GeneID; 905872; -.
DR KEGG; cje:Cj1605c; -.
DR PATRIC; fig|192222.6.peg.1581; -.
DR eggNOG; COG2171; Bacteria.
DR HOGENOM; CLU_057490_1_0_7; -.
DR OMA; TVLDTWF; -.
DR UniPathway; UPA00034; UER00019.
DR EvolutionaryTrace; Q0P823; -.
DR Proteomes; UP000000799; 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; 3.30.60.70; -; 1.
DR HAMAP; MF_02122; DapD_type2; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR032784; THDPS_M.
DR InterPro; IPR038361; THDPS_M_sf.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR InterPro; IPR026586; Type2_DapD.
DR Pfam; PF14602; Hexapep_2; 1.
DR Pfam; PF14789; THDPS_M; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Diaminopimelate biosynthesis; Lysine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..386
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase"
FT /id="PRO_0000412257"
FT ACT_SITE 257
FT /note="Acyl-anhydride intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 259
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 274
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 277
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 300
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 315..316
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 323
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 349
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT BINDING 362..365
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT HELIX 5..16
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 25..34
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2RIJ"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:2RIJ"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:2RIJ"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2RIJ"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:2RIJ"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:2RIJ"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:2RIJ"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:2RIJ"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:2RIJ"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:2RIJ"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:2RIJ"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:2RIJ"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:2RIJ"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:2RIJ"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:2RIJ"
SQ SEQUENCE 386 AA; 42361 MW; 2C750BCE3CA97BA3 CRC64;
MINTKEDFLL LIKQIEQKSG YKKPKAFGIA RLDRGQLNKN KILQASFALI NYEQNFGSAA
IMLEAFMQRG VEIDFNASEF VQTLKLEDID FALSCFKPFL EEDGHQNIDL LKIIKDKFKD
DEFSFVCLFE DKEPLSVESI YLKLYLLSTK KVPLRSINLN GAFGLLSNVA WSDDKPIELE
YLRANEMRLK MSNQYPKIDF VDKFPRFLAH IIPEDNTRIL ESSKVRMGAS LAAGTTIMPG
ASYVNFNAGT TGACMVEGRI SSSAIVGEGS DVGGGASILG VLSGTSGNAI SVGKACLLGA
NSVTGIPLGD NCIVDAGIAV LEGTKFLLKD AEELAKLNPY FNFDKEIYKG LELKGLNGLH
FRQDSISGAM IVALNKKAVK LNEALH
