DAPD_BARHE
ID DAPD_BARHE Reviewed; 282 AA.
AC Q6G549;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, 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}; OrderedLocusNames=BH00720;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(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; BX897699; CAF26888.1; -; Genomic_DNA.
DR RefSeq; WP_011180033.1; NZ_LRIJ02000001.1.
DR PDB; 6WQM; X-ray; 2.15 A; A/B/C/D/E/F=1-282.
DR PDBsum; 6WQM; -.
DR AlphaFoldDB; Q6G549; -.
DR SMR; Q6G549; -.
DR STRING; 283166.BH00720; -.
DR PaxDb; Q6G549; -.
DR PRIDE; Q6G549; -.
DR EnsemblBacteria; CAF26888; CAF26888; BH00720.
DR GeneID; 64156378; -.
DR KEGG; bhe:BH00720; -.
DR eggNOG; COG2171; Bacteria.
DR OMA; YFPIQKM; -.
DR UniPathway; UPA00034; UER00019.
DR Proteomes; UP000000421; 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; 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..282
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase"
FT /id="PRO_0000196913"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:6WQM"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:6WQM"
FT HELIX 27..41
FT /evidence="ECO:0007829|PDB:6WQM"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:6WQM"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6WQM"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:6WQM"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6WQM"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6WQM"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6WQM"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:6WQM"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:6WQM"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:6WQM"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6WQM"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6WQM"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:6WQM"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:6WQM"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:6WQM"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:6WQM"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:6WQM"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:6WQM"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:6WQM"
SQ SEQUENCE 282 AA; 30939 MW; 7595A2A929274E64 CRC64;
MTDLTQLEMI IEKAFDDRNS INTTTKGEIL ESVEHALNLL DKGEVRVVKR QKNGKWHVHQ
WLKKAVLLSF RLNPMQIMTG GVNGTSWWDK VPSKFSHWQE ADFKKADFRS VPGAIVRHSA
YIAPNVILMP SFVNLGAFVD EGTMVDTWAT VGSCAQIGKH VHLSGGVGIG GVLEPLQANP
TIIEDHCFIG ARSEVVEGCI IREGSVLGMG VFIGKSTKII DRTTGEIFIG EVPPYSVVVP
GSLPGKPLPN GEIGPNLYCA VIVKRVDQKT REKTSINDLL RD
