DAPD_LEGPH
ID DAPD_LEGPH Reviewed; 276 AA.
AC Q5ZX45;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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}; OrderedLocusNames=lpg0888;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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; AE017354; AAU26975.1; -; Genomic_DNA.
DR RefSeq; WP_010946623.1; NC_002942.5.
DR RefSeq; YP_094922.1; NC_002942.5.
DR PDB; 6CKT; X-ray; 1.80 A; A=1-276.
DR PDBsum; 6CKT; -.
DR AlphaFoldDB; Q5ZX45; -.
DR SMR; Q5ZX45; -.
DR STRING; 272624.lpg0888; -.
DR PaxDb; Q5ZX45; -.
DR EnsemblBacteria; AAU26975; AAU26975; lpg0888.
DR GeneID; 66490069; -.
DR KEGG; lpn:lpg0888; -.
DR PATRIC; fig|272624.6.peg.919; -.
DR eggNOG; COG2171; Bacteria.
DR HOGENOM; CLU_050859_0_1_6; -.
DR OMA; YFPIQKM; -.
DR UniPathway; UPA00034; UER00019.
DR Proteomes; UP000000609; 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; 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.
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..276
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase"
FT /id="PRO_0000196945"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
FT HELIX 1..13
FT /evidence="ECO:0007829|PDB:6CKT"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:6CKT"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6CKT"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:6CKT"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:6CKT"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6CKT"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:6CKT"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6CKT"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:6CKT"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:6CKT"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:6CKT"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6CKT"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:6CKT"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:6CKT"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6CKT"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:6CKT"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:6CKT"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:6CKT"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:6CKT"
SQ SEQUENCE 276 AA; 30078 MW; 0A2A05B59986C6E0 CRC64;
MNSLQDLIEQ AFENRQNLSL DTASSDLINA INEVLSGLDN GQFRVAEKIN GEWTVHQWLK
KAVLLSFKLF PNQIIDAGFC KFYDKIPLKY TDCSNEQFQQ SGVRVVPHAM VRRGAYIAKN
TVLMPSYVNI GAYIDEGVMV DTWATVGSCA QIGKNVHISG GAGIGGVLEP LQANPTIIED
NCFIGARSEI VEGVIVEKNS VISMGVFLGQ STKIYNRITG EVSYGRIPAG SVVVAGNLPS
HDGSHSLYCA VIVKQVDEKT RAKVSINDLL RANQDD
