(data stored in ACNUC7421 zone)

SWISSPROT: C6AZ64_RHILS

ID   C6AZ64_RHILS            Unreviewed;       286 AA.
AC   C6AZ64;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
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   OrderedLocusNames=Rleg_0079 {ECO:0000313|EMBL:ACS54390.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54390.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54390.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54390.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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:0000256|HAMAP-Rule:MF_00811,
CC         ECO:0000256|SAAS:SAAS01124328};
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       ECO:0000256|SAAS:SAAS00681956}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00811}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00811,
CC       ECO:0000256|SAAS:SAAS00681965}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000256|HAMAP-Rule:MF_00811, ECO:0000256|SAAS:SAAS00672410}.
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DR   EMBL; CP001622; ACS54390.1; -; Genomic_DNA.
DR   RefSeq; WP_012755820.1; NC_012850.1.
DR   EnsemblBacteria; ACS54390; ACS54390; Rleg_0079.
DR   KEGG; rlg:Rleg_0079; -.
DR   HOGENOM; HOG000003295; -.
DR   KO; K00674; -.
DR   OMA; YFPIQKM; -.
DR   OrthoDB; 752123at2; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000002256; 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; C6AZ64.
DR   SWISS-2DPAGE; C6AZ64.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00811,
KW   ECO:0000256|SAAS:SAAS00681961, ECO:0000313|EMBL:ACS54390.1};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00811,
KW   ECO:0000256|SAAS:SAAS00681960};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00811,
KW   ECO:0000256|SAAS:SAAS00681955};
KW   Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00811,
KW   ECO:0000256|SAAS:SAAS00681957};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00811,
KW   ECO:0000256|SAAS:SAAS00681953};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00811,
KW   ECO:0000256|SAAS:SAAS00681954};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00811,
KW   ECO:0000256|SAAS:SAAS00681963, ECO:0000313|EMBL:ACS54390.1}.
FT   DOMAIN        8     74       THDPS_N_2. {ECO:0000259|Pfam:PF14805}.
FT   BINDING     111    111       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00811}.
FT   BINDING     148    148       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00811}.
SQ   SEQUENCE   286 AA;  30448 MW;  19CF5D5A2D4A5EDA CRC64;
     MSATDLASLE KIIESAFDNR DNVNTSTKGE VRDAVEAALD LLDAGKARVA ERSADGAWTV
     NQWLKKAVLL SFRLNDMDVV EGGSGNSTWW DKVPSKFENW GENHFRAAGF RAVPNCVVRR
     SAYIAPNAIL MPSFVNLGAY VGEGTMVDTW ATVGSCAQIG KHVHLSGGVG IGGVLEPMQA
     GPTIIEDNCF IGARSEVVEG CIIREGSVLG MGVFIGKSTK IVDRATGEVS YGEVPPYSVV
     VAGSMPSGNA TMGNGQPAPH LYCAVIVKRV DEKTRSKTGI NELLRD
//

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