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2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (EC 2.3.1.117) (Tetrahydrodipicolinate N-succinyltransferase) (THDP succinyltransferase) (THP succinyltransferase) (Tetrahydropicolinate succinylase)

 DAPD_GEOOG              Reviewed;         324 AA.
D2S9Y8;
21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
02-MAR-2010, sequence version 1.
28-MAR-2018, entry version 46.
RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
EC=2.3.1.117 {ECO:0000255|HAMAP-Rule:MF_02122};
AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
Short=THDP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
Short=THP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
AltName: Full=Tetrahydropicolinate succinylase {ECO:0000255|HAMAP-Rule:MF_02122};
Name=dapD {ECO:0000255|HAMAP-Rule:MF_02122};
OrderedLocusNames=Gobs_1092;
Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 /
G-20).
Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae;
Geodermatophilus.
NCBI_TaxID=526225;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / G-20;
US DOE Joint Genome Institute (JGI-PGF);
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
Ivanova N., Munk A.C., Brettin T., Detter J.C., Han C., Larimer F.,
Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
Woyke T., Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.;
"The complete genome of Geodermatophilus obscurus DSM 43160.";
Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the conversion of the cyclic
tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-
amino-6-oxopimelate using succinyl-CoA. {ECO:0000255|HAMAP-
Rule:MF_02122}.
-!- CATALYTIC ACTIVITY: Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-
2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6-
oxoheptanedioate. {ECO:0000255|HAMAP-Rule:MF_02122}.
-!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
(succinylase route): step 1/3. {ECO:0000255|HAMAP-Rule:MF_02122}.
-!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_02122}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02122}.
-!- SIMILARITY: Belongs to the type 2 tetrahydrodipicolinate N-
succinyltransferase family. {ECO:0000255|HAMAP-Rule:MF_02122}.
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EMBL; CP001867; ADB73851.1; -; Genomic_DNA.
RefSeq; WP_012947292.1; NC_013757.1.
ProteinModelPortal; D2S9Y8; -.
SMR; D2S9Y8; -.
STRING; 526225.Gobs_1092; -.
PRIDE; D2S9Y8; -.
EnsemblBacteria; ADB73851; ADB73851; Gobs_1092.
KEGG; gob:Gobs_1092; -.
eggNOG; ENOG4105EJ3; Bacteria.
eggNOG; COG2171; LUCA.
HOGENOM; HOG000248194; -.
KO; K00674; -.
OMA; TVLDTWF; -.
OrthoDB; POG091H05ZG; -.
BioCyc; GOBS526225:G1GH8-1103-MONOMER; -.
UniPathway; UPA00034; UER00019.
Proteomes; UP000001382; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008666; F:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
Gene3D; 3.30.60.70; -; 1.
HAMAP; MF_02122; DapD_type2; 1.
InterPro; IPR019875; DapD_actinobacteria.
InterPro; IPR001451; Hexapep.
InterPro; IPR032784; THDPS_M.
InterPro; IPR038361; THDPS_M_sf.
InterPro; IPR011004; Trimer_LpxA-like_sf.
InterPro; IPR026586; Type2_DapD.
Pfam; PF14602; Hexapep_2; 1.
Pfam; PF14789; THDPS_M; 1.
SUPFAM; SSF51161; SSF51161; 1.
TIGRFAMs; TIGR03535; DapD_actino; 1.
3: Inferred from homology;
Acyltransferase; Amino-acid biosynthesis; Complete proteome;
Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis;
Magnesium; Metal-binding; Reference proteome; Transferase.
CHAIN 1 324 2,3,4,5-tetrahydropyridine-2,6-
dicarboxylate N-succinyltransferase.
/FTId=PRO_0000412259.
REGION 264 265 Succinyl-CoA binding. {ECO:0000255|HAMAP-
Rule:MF_02122}.
REGION 297 300 Succinyl-CoA binding. {ECO:0000255|HAMAP-
Rule:MF_02122}.
ACT_SITE 206 206 Acyl-anhydride intermediate.
{ECO:0000255|HAMAP-Rule:MF_02122}.
METAL 173 173 Magnesium 1; shared with trimeric
partners. {ECO:0000255|HAMAP-
Rule:MF_02122}.
METAL 190 190 Magnesium 2; shared with trimeric
partners. {ECO:0000255|HAMAP-
Rule:MF_02122}.
BINDING 208 208 Succinyl-CoA. {ECO:0000255|HAMAP-
Rule:MF_02122}.
BINDING 223 223 Succinyl-CoA; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_02122}.
BINDING 226 226 Succinyl-CoA. {ECO:0000255|HAMAP-
Rule:MF_02122}.
BINDING 249 249 Succinyl-CoA; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_02122}.
BINDING 272 272 Succinyl-CoA; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_02122}.
BINDING 284 284 Succinyl-CoA. {ECO:0000255|HAMAP-
Rule:MF_02122}.
SEQUENCE 324 AA; 33209 MW; 52E09516CF8FC91D CRC64;
MTDSAPHSAV AAGLATVTPA GTVLDTWYPE PRLGVPAGAR PGTTRLGALE ISGELGPDYG
GLVRRDESRG VEVIAVRTVI PDLAAAPVDT HDVWLRLHLL SHRLVSPRSI SMDGVFGLLT
NVAWTSAGPV EAATFNVHRL RAALGHVTVF GVDKFPRMVD YVIPSGVRVA DGDRVRLGAH
LAEGTTVMHE GFVNYNAGTL GPSMVEGRIS AGVVVGPNSD IGGGASIMGT LSGGGKQVVS
IGSGCLLGAN AGIGISLGDN CVVEAGCYVT AGSRVTLPDG SVVKAAELSG RDGLLFRRNS
VSGALEALPR TGTWGELNAQ LHAN


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