DAPD_ACIBA
ID DAPD_ACIBA Reviewed; 273 AA.
AC Q5DL43;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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};
OS Acinetobacter baumannii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=470;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ab244;
RX PubMed=15793123; DOI=10.1128/aac.49.4.1432-1440.2005;
RA Mussi M.A., Limansky A.S., Viale A.M.;
RT "Acquisition of resistance to carbapenems in multidrug-resistant clinical
RT strains of Acinetobacter baumannii: natural insertional inactivation of a
RT gene encoding a member of a novel family of beta-barrel outer membrane
RT proteins.";
RL Antimicrob. Agents Chemother. 49:1432-1440(2005).
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; AY684798; AAV80242.1; -; Genomic_DNA.
DR RefSeq; WP_000080867.1; NZ_WYAT01000009.1.
DR PDB; 6AMY; X-ray; 2.85 A; A/B/C=1-273.
DR PDB; 6AMZ; X-ray; 2.05 A; A=1-273.
DR PDBsum; 6AMY; -.
DR PDBsum; 6AMZ; -.
DR AlphaFoldDB; Q5DL43; -.
DR SMR; Q5DL43; -.
DR STRING; 470.IX87_09360; -.
DR GeneID; 66396290; -.
DR eggNOG; COG2171; Bacteria.
DR OMA; YFPIQKM; -.
DR OrthoDB; 752123at2; -.
DR UniPathway; UPA00034; UER00019.
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..273
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase"
FT /id="PRO_0000196909"
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 4..13
FT /evidence="ECO:0007829|PDB:6AMZ"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:6AMZ"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6AMZ"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:6AMZ"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:6AMZ"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6AMZ"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:6AMZ"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6AMY"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6AMZ"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:6AMY"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:6AMZ"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:6AMZ"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6AMZ"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:6AMZ"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:6AMZ"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:6AMZ"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:6AMZ"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6AMZ"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:6AMZ"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:6AMY"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:6AMZ"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:6AMY"
SQ SEQUENCE 273 AA; 29552 MW; 787ACFB4AC14E131 CRC64;
MSQLSTIIEQ AFEDRANFTA ADCPSEIRQA VEEAIAGLDN GTLRVAEKIN GEWVVHQWLK
KAVLLSFKLN DNKPIESCDL RFYDKVETKF SGWTEEQFKA AGVRVVPPAV ARRGSFQAKN
VVLMPSYVNI GAYVDEGTMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQANPTIIED
NCFIGARSEI VEGVIVEEGS VISMGVYIGQ STRIYDRETG EIHYGRVPAG SVVVPGNLPS
ADGKYSLYAA IIVKKVDAQT RAKTSLNDLL RAD
