(data stored in ACNUC7421 zone)

SWISSPROT: D4YXA9_SPHJU

ID   D4YXA9_SPHJU            Unreviewed;       279 AA.
AC   D4YXA9;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 52.
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:BAI94991.1};
GN   OrderedLocusNames=SJA_C1-01570 {ECO:0000313|EMBL:BAI94991.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI94991.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI94991.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- CATALYTIC ACTIVITY: Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-
CC       2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6-
CC       oxoheptanedioate. {ECO:0000256|HAMAP-Rule:MF_00811,
CC       ECO:0000256|SAAS:SAAS00681964}.
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; AP010803; BAI94991.1; -; Genomic_DNA.
DR   RefSeq; WP_007685477.1; NC_014006.1.
DR   ProteinModelPortal; D4YXA9; -.
DR   STRING; 452662.SJA_C1-01570; -.
DR   EnsemblBacteria; BAI94991; BAI94991; SJA_C1-01570.
DR   GeneID; 29271865; -.
DR   KEGG; sjp:SJA_C1-01570; -.
DR   eggNOG; ENOG4105DMJ; Bacteria.
DR   eggNOG; COG2171; LUCA.
DR   HOGENOM; HOG000003295; -.
DR   KO; K00674; -.
DR   OMA; QVPCALI; -.
DR   OrthoDB; POG091H0G02; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000007753; Chromosome 1.
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-HAMAP.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP.
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; IPR011004; Trimer_LpxA-like.
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; D4YXA9.
DR   SWISS-2DPAGE; D4YXA9.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00811,
KW   ECO:0000256|SAAS:SAAS00681961, ECO:0000313|EMBL:BAI94991.1};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00811,
KW   ECO:0000256|SAAS:SAAS00681960};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
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:UP000007753};
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:BAI94991.1}.
FT   DOMAIN        5     69       THDPS_N_2. {ECO:0000259|Pfam:PF14805}.
FT   BINDING     106    106       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00811}.
FT   BINDING     143    143       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00811}.
SQ   SEQUENCE   279 AA;  29485 MW;  946A5F61E94315BA CRC64;
     MSNELIATID AAWEDRANVS LSTQGAVRQA VDKALAMLDS GELRVAEPTA EGWRVNQWAK
     KAVLLSFRLN DNVMIDNGPG AGHWWDKVPS KFAGWDEAAF RAAGFRAVPG SFARAGAHIA
     KNVILMPSFV NIGAFVDEGT MVDTWVTVGS CAQIGKNVHL SGGVGIGGVL EPLQADPVII
     EDDCFIGARS EVVEGVRVGK GSVLSMGVFI GQSTKIVDRA TGEVFMGEVP PYSVVVPGSL
     PGKPLPDGTP GPSLYCAVIV KRVDAQTRSK TGINELLRD
//

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