(data stored in ACNUC7421 zone)

SWISSPROT: DAPD_SINFN

ID   DAPD_SINFN              Reviewed;         285 AA.
AC   C3MF35;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   08-MAY-2019, entry version 65.
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};
GN   OrderedLocusNames=NGR_c00680;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA =
CC         CoA + L-2-succinylamino-6-oxopimelate; 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}.
DR   EMBL; CP001389; ACP23872.1; -; Genomic_DNA.
DR   RefSeq; WP_012706657.1; NC_012587.1.
DR   RefSeq; YP_002824625.1; NC_012587.1.
DR   SMR; C3MF35; -.
DR   STRING; 394.NGR_c00680; -.
DR   EnsemblBacteria; ACP23872; ACP23872; NGR_c00680.
DR   GeneID; 7790647; -.
DR   KEGG; rhi:NGR_c00680; -.
DR   PATRIC; fig|394.7.peg.2861; -.
DR   eggNOG; ENOG4105DMJ; Bacteria.
DR   eggNOG; COG2171; LUCA.
DR   HOGENOM; HOG000003295; -.
DR   KO; K00674; -.
DR   OMA; YFPIQKM; -.
DR   OrthoDB; 752123at2; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000001054; 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   3: Inferred from homology;
DR   PRODOM; C3MF35.
DR   SWISS-2DPAGE; C3MF35.
KW   Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW   Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN         1    285       2,3,4,5-tetrahydropyridine-2,6-
FT                                dicarboxylate N-succinyltransferase.
FT                                /FTId=PRO_1000148587.
FT   BINDING     111    111       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00811}.
FT   BINDING     148    148       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00811}.
SQ   SEQUENCE   285 AA;  30314 MW;  B8D84D35EB14D855 CRC64;
     MTNHDLASLS QTIETAFEDR EAVSTSTRGA IRDAVEAALN LLDSGKVRVA ERGADGTWTV
     NQWLKKAVLL SFRLNPMELV KGGPGESVWW DKVASKFDGW SVNEFEKAGF RAVPNCVVRR
     SAYIAPNAIL MPSFVNLGAY VGEGTMVDTW ATVGSCAQIG KNVHLSGGVG IGGVLEPMQA
     GPTIIEDNCF IGARSEVVEG CIVREGSVLG MGVFIGKSTK IVDRATGEVT YGEVPPYSVV
     VAGSMPSGST MANGQPAPNL YCAVIVKRVD EKTRSKTGIN ELLRD
//

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