DAPD_BRUSU
ID DAPD_BRUSU Reviewed; 284 AA.
AC Q8FV25; G0KE34;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE EC=2.3.1.117 {ECO:0000255|HAMAP-Rule:MF_00811};
DE AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE Short=THDP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE Short=THP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811};
DE Short=Tetrahydropicolinate succinylase {ECO:0000255|HAMAP-Rule:MF_00811};
GN Name=dapD {ECO:0000255|HAMAP-Rule:MF_00811};
GN OrderedLocusNames=BRA1028, BS1330_II1020;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS).
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of 2,3,4,5-tetrahydropyridine-2-carboxylate n-
RT succinyltransferase from Brucella melitensis biovar abortus 2308.";
RL Submitted (SEP-2008) to the PDB data bank.
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_00811};
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_00811}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00811}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00811}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000255|HAMAP-Rule:MF_00811}.
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DR EMBL; AE014292; AAN34196.1; -; Genomic_DNA.
DR EMBL; CP002998; AEM20472.1; -; Genomic_DNA.
DR PIR; AD3543; AD3543.
DR RefSeq; WP_002965622.1; NZ_KN046805.1.
DR PDB; 3EG4; X-ray; 1.87 A; A=1-284.
DR PDBsum; 3EG4; -.
DR AlphaFoldDB; Q8FV25; -.
DR SMR; Q8FV25; -.
DR EnsemblBacteria; AEM20472; AEM20472; BS1330_II1020.
DR GeneID; 45126330; -.
DR GeneID; 55592652; -.
DR KEGG; bms:BRA1028; -.
DR KEGG; bsi:BS1330_II1020; -.
DR PATRIC; fig|204722.21.peg.1090; -.
DR HOGENOM; CLU_050859_0_1_5; -.
DR OMA; YFPIQKM; -.
DR PhylomeDB; Q8FV25; -.
DR UniPathway; UPA00034; UER00019.
DR EvolutionaryTrace; Q8FV25; -.
DR Proteomes; UP000007104; Chromosome II.
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; Repeat; Transferase.
FT CHAIN 1..284
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase"
FT /id="PRO_0000196922"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:3EG4"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:3EG4"
FT HELIX 29..43
FT /evidence="ECO:0007829|PDB:3EG4"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3EG4"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3EG4"
FT HELIX 62..74
FT /evidence="ECO:0007829|PDB:3EG4"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:3EG4"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:3EG4"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:3EG4"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:3EG4"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:3EG4"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:3EG4"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:3EG4"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3EG4"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3EG4"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:3EG4"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:3EG4"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:3EG4"
FT STRAND 258..267
FT /evidence="ECO:0007829|PDB:3EG4"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:3EG4"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:3EG4"
SQ SEQUENCE 284 AA; 30753 MW; 9EF76F51038A6350 CRC64;
MTKPDLASLE KTIEKAFDER DGINTATRGE VREAVEQSLI LLDRGEVRVA EKQADGNWHV
NQWLKKAVLL SFRLNPMEVI KGGPGQSSWW DKVPSKFDGW TANEFEKAGF RAVPNCIVRH
SAYIAPNAIL MPSFVNLGAY VDKGAMIDTW ATVGSCAQIG KNVHLSGGVG IGGVLEPMQA
GPTIIEDNCF IGARSEVVEG CIVREGSVLG MGVFIGKSTK IVDRATGEVF YGEVPPYSVV
VAGTMPGKNV PGENWGPSLY CAVIVKRADE KTRSKTSINE LLRD
