ID H0PTZ2_9RHOO Unreviewed; 273 AA.
AC H0PTZ2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000256|HAMAP-Rule:MF_00811};
DE EC=2.3.1.117 {ECO:0000256|HAMAP-Rule:MF_00811};
DE AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000256|HAMAP-Rule:MF_00811};
DE Short=THDP succinyltransferase {ECO:0000256|HAMAP-Rule:MF_00811};
DE Short=THP succinyltransferase {ECO:0000256|HAMAP-Rule:MF_00811};
DE Short=Tetrahydropicolinate succinylase {ECO:0000256|HAMAP-Rule:MF_00811};
GN Name=dapD {ECO:0000256|HAMAP-Rule:MF_00811,
GN ECO:0000313|EMBL:BAL25110.1};
GN ORFNames=AZKH_2804 {ECO:0000313|EMBL:BAL25110.1};
OS Azoarcus sp. KH32C.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL25110.1, ECO:0000313|Proteomes:UP000007106};
RN [1] {ECO:0000313|EMBL:BAL25110.1, ECO:0000313|Proteomes:UP000007106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH32C {ECO:0000313|EMBL:BAL25110.1,
RC ECO:0000313|Proteomes:UP000007106};
RA Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S.,
RA Senoo K.;
RT "Complete genome sequence of Azoarcus sp. KH32C.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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_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:0000256|HAMAP-Rule:MF_00811}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00811}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00811}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000256|ARBA:ARBA00007274, ECO:0000256|HAMAP-Rule:MF_00811}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP012304; BAL25110.1; -; Genomic_DNA.
DR RefSeq; WP_015436415.1; NC_020516.1.
DR AlphaFoldDB; H0PTZ2; -.
DR STRING; 748247.AZKH_2804; -.
DR KEGG; aza:AZKH_2804; -.
DR PATRIC; fig|748247.4.peg.2775; -.
DR eggNOG; COG2171; Bacteria.
DR HOGENOM; CLU_050859_0_1_4; -.
DR OrthoDB; 9775362at2; -.
DR UniPathway; UPA00034; UER00019.
DR Proteomes; UP000007106; 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 CDD; cd03350; LbH_THP_succinylT; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 1.10.166.10; Tetrahydrodipicolinate-N-succinyltransferase, N-terminal domain; 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 NCBIfam; TIGR00965; dapD; 1.
DR PANTHER; PTHR19136:SF52; 2,3,4,5-TETRAHYDROPYRIDINE-2,6-DICARBOXYLATE N-SUCCINYLTRANSFERASE; 1.
DR PANTHER; PTHR19136; MOLYBDENUM COFACTOR GUANYLYLTRANSFERASE; 1.
DR Pfam; PF14602; Hexapep_2; 1.
DR Pfam; PF14805; THDPS_N_2; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_00811};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00811};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00811};
KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915,
KW ECO:0000256|HAMAP-Rule:MF_00811};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW Rule:MF_00811}; Reference proteome {ECO:0000313|Proteomes:UP000007106};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00811};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00811}.
FT DOMAIN 3..69
FT /note="Tetrahydrodipicolinate-N-succinyltransferase chain
FT A"
FT /evidence="ECO:0000259|Pfam:PF14805"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00811"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00811"
SQ SEQUENCE 273 AA; 29298 MW; 8B6A8A78427F71CC CRC64;
MQELQKIIDD AFENRSSLSP SSAPAVIRDA VAEVINGLDS GRLRVAEKVD GNWTVNQWIK
KAVLISFRLR DNEVQSAGAL NFYDKVPTKF GDYTPEQFRE GGFRVVPPAV ARKGSYIAKN
VVLMPSYVNI GAYVDEGTMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP VQAGPVIIED
NVFVGARSEV VEGVIIEENA VLSMGVYIGQ STKIYDRETG EIFYGRVPSG AVVVPGSLPS
ADGKYSLYCA VIVKRVDAQT RAKTGINELL RGA
//