DAPD_MYCTO
ID DAPD_MYCTO Reviewed; 317 AA.
AC P9WP20; L0T666; O05302; Q7D8M6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
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 AltName: Full=Tetrahydropicolinate succinylase;
GN Name=dapD; OrderedLocusNames=MT1239;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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:0000250}.
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 type 2 tetrahydrodipicolinate N-
CC succinyltransferase family. {ECO:0000305}.
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DR EMBL; AE000516; AAK45496.1; -; Genomic_DNA.
DR PIR; G70608; G70608.
DR RefSeq; WP_003898768.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WP20; -.
DR SMR; P9WP20; -.
DR EnsemblBacteria; AAK45496; AAK45496; MT1239.
DR KEGG; mtc:MT1239; -.
DR PATRIC; fig|83331.31.peg.1338; -.
DR HOGENOM; CLU_057490_1_0_11; -.
DR UniPathway; UPA00034; UER00019.
DR Proteomes; UP000001020; 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:0000287; F:magnesium ion binding; 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; IPR019875; DapD_actinobacteria.
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.
DR TIGRFAMs; TIGR03535; DapD_actino; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Diaminopimelate biosynthesis; Lysine biosynthesis; Magnesium;
KW Metal-binding; Transferase.
FT CHAIN 1..317
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase"
FT /id="PRO_0000427028"
FT ACT_SITE 199
FT /note="Acyl-anhydride intermediate"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="ligand shared between trimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared between trimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000250"
FT BINDING 257..258
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000250"
FT BINDING 290..293
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000250"
SQ SEQUENCE 317 AA; 32642 MW; EF204F46B90ADFF3 CRC64;
MSTVTGAAGI GLATLAADGS VLDTWFPAPE LTESGTSATS RLAVSDVPVE LAALIGRDDD
RRTETIAVRT VIGSLDDVAA DPYDAYLRLH LLSHRLVAPH GLNAGGLFGV LTNVVWTNHG
PCAIDGFEAV RARLRRRGPV TVYGVDKFPR MVDYVVPTGV RIADADRVRL GAHLAPGTTV
MHEGFVNYNA GTLGASMVEG RISAGVVVGD GSDVGGGASI MGTLSGGGTH VISIGKRCLL
GANSGLGISL GDDCVVEAGL YVTAGTRVTM PDSNSVKARE LSGSSNLLFR RNSVSGAVEV
LARDGQGIAL NEDLHAN
