位置:首页 > 蛋白库 > DAPD_GLUOX
DAPD_GLUOX
ID   DAPD_GLUOX              Reviewed;         276 AA.
AC   Q5FPX6;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 99.
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}; OrderedLocusNames=GOX1831;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + succinyl-CoA = (S)-
CC         2-succinylamino-6-oxoheptanedioate + CoA; 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW61570.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; CP000009; AAW61570.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011253351.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FPX6; -.
DR   SMR; Q5FPX6; -.
DR   STRING; 290633.GOX1831; -.
DR   EnsemblBacteria; AAW61570; AAW61570; GOX1831.
DR   GeneID; 56906168; -.
DR   KEGG; gox:GOX1831; -.
DR   eggNOG; COG2171; Bacteria.
DR   HOGENOM; CLU_050859_0_1_5; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000006375; 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; 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.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; Reference proteome;
KW   Repeat; Transferase.
FT   CHAIN           1..276
FT                   /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT                   succinyltransferase"
FT                   /id="PRO_0000196938"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00811"
SQ   SEQUENCE   276 AA;  29566 MW;  44A57BEDA31F8161 CRC64;
     MPNAPLRTAI EALWERRATL SARTEGEDRD VVEKVLSALD AGTLRVAEPF ADGWTVHEWL
     KKAVLLSFRL NDSRVMERGC GGEPAFDKVP LKFDGWDQFR FAEAGFRAVP GAIVRRSAFI
     APNVVLMPSF VNVGARVDSG TMIDTWATVG SCAQIGKNCH ISGGAGIGGV LEPLQAAPVI
     IEDDCFIGAR SEVAEGVIVE KGSVLSMGVF LGASTKIVDR ATGEIFMGRV PAYSVVVPGT
     LPPKEPGMPS LACAVIVKRV DERTRSKTSI NDLLRD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024