(data stored in SCRATCH zone)

SWISSPROT: C8U1N4_ECO10

ID   C8U1N4_ECO10            Unreviewed;       274 AA.
AC   C8U1N4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-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: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:BAI29042.1};
GN   OrderedLocusNames=ECO103_0164 {ECO:0000313|EMBL:BAI29042.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29042.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29042.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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: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; AP010958; BAI29042.1; -; Genomic_DNA.
DR   RefSeq; WP_001186650.1; NC_013353.1.
DR   SMR; C8U1N4; -.
DR   EnsemblBacteria; BAI29042; BAI29042; ECO103_0164.
DR   KEGG; eoh:ECO103_0164; -.
DR   HOGENOM; HOG000003295; -.
DR   KO; K00674; -.
DR   OMA; YFPIQKM; -.
DR   BioCyc; ECOL585395:ECO103_RS00840-MONOMER; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000000959; 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; C8U1N4.
DR   SWISS-2DPAGE; C8U1N4.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00811,
KW   ECO:0000256|SAAS:SAAS00681961};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00811,
KW   ECO:0000256|SAAS:SAAS00681960};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
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:BAI29042.1}.
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;  29892 MW;  42D7A38610DD3AF6 CRC64;
     MQQLQNIIET AFERRAEITP ANADTVTREA VNQVIALLDS GALRVAEKID GQWVTHQWLK
     KAVLLSFRIN DNQVIEGAES RYFDKVPMKF ADYDEARFQK EGFRVVPPAA VRQGAFIARN
     TVLMPSYVNI GAYVDEGTMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQANPTIIED
     NCFIGARSEV VEGVIVEEGS VISMGVYIGQ STRIYDRETG EIHYGRVPAG SVVVSGNLPS
     KDGKYSLYCA VIVKKVDAKT RGKVGINELL RTID
//

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