(data stored in SCRATCH zone)

SWISSPROT: D3UWF6_XENBS

ID   D3UWF6_XENBS            Unreviewed;       274 AA.
AC   D3UWF6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 62.
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:CBJ79730.1};
GN   OrderedLocusNames=XBJ1_0586 {ECO:0000313|EMBL:CBJ79730.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79730.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79730.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79730.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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}.
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; FN667741; CBJ79730.1; -; Genomic_DNA.
DR   RefSeq; WP_012987184.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0586; -.
DR   EnsemblBacteria; CBJ79730; CBJ79730; XBJ1_0586.
DR   GeneID; 8830208; -.
DR   KEGG; xbo:XBJ1_0586; -.
DR   PATRIC; fig|406818.4.peg.539; -.
DR   eggNOG; ENOG4105DMJ; Bacteria.
DR   eggNOG; COG2171; LUCA.
DR   HOGENOM; HOG000003295; -.
DR   KO; K00674; -.
DR   OMA; YFPIQKM; -.
DR   BioCyc; XBOV406818:XBJ1_RS02540-MONOMER; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000002045; 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; D3UWF6.
DR   SWISS-2DPAGE; D3UWF6.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00811,
KW   ECO:0000256|SAAS:SAAS00681961, ECO:0000313|EMBL:CBJ79730.1};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00811,
KW   ECO:0000256|SAAS:SAAS00681960};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
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   Reference proteome {ECO:0000313|Proteomes:UP000002045};
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:CBJ79730.1}.
FT   DOMAIN        3     69       THDPS_N_2. {ECO:0000259|Pfam:PF14805}.
FT   BINDING     104    104       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00811}.
FT   BINDING     141    141       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00811}.
SQ   SEQUENCE   274 AA;  29828 MW;  50BFD6922C1C6E21 CRC64;
     MQQLQSIIDN AFENRTNITP GTVDEATRSA VNQVIQMLDS GKLRVAEKIA GQWVTHQWLK
     KAVLLSFRIN DNQVIEGAES RYFDKVPMKF ADYDQARFEK EGFRVVPPAA VRQGAYIARN
     SVLMPSYVNI GAYVDEGTMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQANPTIIED
     NCFIGARSEI VEGVIVEEGA VISMGVYIGQ STKIYDRETG EIHYGRVPAG SVVVSGNLPS
     KDGSYSLYCA VIVKKVDAKT RGKVGLNELL RNID
//

If you have problems or comments...

PBIL Back to PBIL home page