ID A0A0G3HFU0_9CORY Unreviewed; 323 AA.
AC A0A0G3HFU0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000256|HAMAP-Rule:MF_02122};
DE EC=2.3.1.117 {ECO:0000256|HAMAP-Rule:MF_02122};
DE AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000256|HAMAP-Rule:MF_02122};
DE Short=THDP succinyltransferase {ECO:0000256|HAMAP-Rule:MF_02122};
DE Short=THP succinyltransferase {ECO:0000256|HAMAP-Rule:MF_02122};
DE AltName: Full=Tetrahydropicolinate succinylase {ECO:0000256|HAMAP-Rule:MF_02122};
GN Name=dapD {ECO:0000256|HAMAP-Rule:MF_02122};
GN ORFNames=CUTER_04085 {ECO:0000313|EMBL:AKK10823.1};
OS Corynebacterium uterequi.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1072256 {ECO:0000313|EMBL:AKK10823.1, ECO:0000313|Proteomes:UP000035548};
RN [1] {ECO:0000313|EMBL:AKK10823.1, ECO:0000313|Proteomes:UP000035548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45634 {ECO:0000313|EMBL:AKK10823.1,
RC ECO:0000313|Proteomes:UP000035548};
RX PubMed=26227590;
RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT "Virulence Factor Genes Detected in the Complete Genome Sequence of
RT Corynebacterium uterequi DSM 45634, Isolated from the Uterus of a Maiden
RT Mare.";
RL Genome Announc. 3:e00783-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45634 {ECO:0000313|Proteomes:UP000035548};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium uterequi DSM 45634, isolated
RT from the uterus of a maiden mare.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_02122}.
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:0000256|HAMAP-Rule:MF_02122};
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:0000256|HAMAP-Rule:MF_02122}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_02122}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02122}.
CC -!- SIMILARITY: Belongs to the type 2 tetrahydrodipicolinate N-
CC succinyltransferase family. {ECO:0000256|HAMAP-Rule:MF_02122}.
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DR EMBL; CP011546; AKK10823.1; -; Genomic_DNA.
DR RefSeq; WP_047259326.1; NZ_CP011546.1.
DR AlphaFoldDB; A0A0G3HFU0; -.
DR STRING; 1072256.CUTER_04085; -.
DR KEGG; cut:CUTER_04085; -.
DR PATRIC; fig|1072256.5.peg.810; -.
DR OrthoDB; 9782799at2; -.
DR UniPathway; UPA00034; UER00019.
DR Proteomes; UP000035548; 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 CDD; cd04649; LbH_THP_succinylT_putative; 1.
DR Gene3D; 3.30.70.2010; -; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 3.30.60.70; Trimeric LpxA-like enzymes; 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 NCBIfam; TIGR03535; DapD_actino; 1.
DR Pfam; PF14602; Hexapep_2; 1.
DR Pfam; PF14789; THDPS_M; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_02122}; Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02122};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02122};
KW Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_02122};
KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02122};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02122};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02122};
KW Reference proteome {ECO:0000313|Proteomes:UP000035548};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02122}.
FT DOMAIN 107..146
FT /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT succinyltransferase middle"
FT /evidence="ECO:0000259|Pfam:PF14789"
FT ACT_SITE 195
FT /note="Acyl-anhydride intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 162
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:0000256|HAMAP-Rule:MF_02122"
FT BINDING 179
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:0000256|HAMAP-Rule:MF_02122"
FT BINDING 197
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 212
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 215
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 238
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 253..254
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 261
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 283
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
FT BINDING 296..299
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02122"
SQ SEQUENCE 323 AA; 33439 MW; B994EAFFB2AAF260 CRC64;
MTTAYARGLA TVTHNGTVLD VWYPSPALNA SVSETGTVRL DEAPQQFAEL VGPDEERGVA
RIAVETSIAD LDAAPVDTYD AYLRLHLLSH RLVRPHGQNL EGIFGLLANV VWTNYGPCAV
ADFQMTRGRL ASRGPVIVYS VDKFPRMVDY VVPTGVRIGD ADRVRLGAHL AEGTTVMHEG
FVNFNAGTLG HSMVEGRISA GVIVDDGTDV GGGASIMGTL SGGGKETISL GKRCLLGANS
GVGISLGDDC VVEAGLYVTA GTKVTVLGVV AEAAGVSHGD TIKAAALSGA SGVLYRRNSV
SGAVEATPWK AEAVTLNAAL HAN
//
