位置:首页 > 蛋白库 > DAPD_CUTAK
DAPD_CUTAK
ID   DAPD_CUTAK              Reviewed;         320 AA.
AC   Q6AA30;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE            EC=2.3.1.117 {ECO:0000255|HAMAP-Rule:MF_02122};
DE   AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE            Short=THDP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE            Short=THP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_02122};
DE   AltName: Full=Tetrahydropicolinate succinylase {ECO:0000255|HAMAP-Rule:MF_02122};
GN   Name=dapD {ECO:0000255|HAMAP-Rule:MF_02122}; OrderedLocusNames=PPA0630;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
CC   -!- FUNCTION: Catalyzes the conversion of the cyclic tetrahydrodipicolinate
CC       (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using
CC       succinyl-CoA. {ECO:0000255|HAMAP-Rule:MF_02122}.
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_02122};
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_02122}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_02122}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02122}.
CC   -!- SIMILARITY: Belongs to the type 2 tetrahydrodipicolinate N-
CC       succinyltransferase family. {ECO:0000255|HAMAP-Rule:MF_02122}.
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; AE017283; AAT82386.1; -; Genomic_DNA.
DR   RefSeq; WP_002515195.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6AA30; -.
DR   SMR; Q6AA30; -.
DR   STRING; 267747.PPA0630; -.
DR   EnsemblBacteria; AAT82386; AAT82386; PPA0630.
DR   GeneID; 66621483; -.
DR   KEGG; pac:PPA0630; -.
DR   eggNOG; COG2171; Bacteria.
DR   HOGENOM; CLU_057490_1_0_11; -.
DR   OMA; TVLDTWF; -.
DR   UniPathway; UPA00034; UER00019.
DR   Proteomes; UP000000603; 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:0000287; F:magnesium ion binding; 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; 3.30.60.70; -; 1.
DR   HAMAP; MF_02122; DapD_type2; 1.
DR   InterPro; IPR019875; DapD_actinobacteria.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR032784; THDPS_M.
DR   InterPro; IPR038361; THDPS_M_sf.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   InterPro; IPR026586; Type2_DapD.
DR   Pfam; PF14602; Hexapep_2; 1.
DR   Pfam; PF14789; THDPS_M; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR03535; DapD_actino; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; Magnesium;
KW   Metal-binding; Transferase.
FT   CHAIN           1..320
FT                   /note="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-
FT                   succinyltransferase"
FT                   /id="PRO_0000412264"
FT   ACT_SITE        202
FT                   /note="Acyl-anhydride intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT   BINDING         169
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between trimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared between trimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT   BINDING         204
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT   BINDING         219
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT   BINDING         222
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT   BINDING         245
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT   BINDING         260..261
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT   BINDING         268
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
FT   BINDING         280
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02122"
SQ   SEQUENCE   320 AA;  33769 MW;  E08C629F739A2EDB CRC64;
     MTQTTTSQTA SADRRAWGWG LATVHEDGGV LDTWYPEPQL GCPDDSSAPA DLHRVTEAGR
     DAIRNVHTEV VHTVIDLDAA PVDVSDAYLR LHLLSSRLAI PRTINLDGIF GVLPNNAWTT
     IGPIRMADLE KARMEARIAH APFTVLLIDK FPRMVDFVVP TGVRIGDADR VRLGAHLAVG
     TTVMHEGFVN FNAGTLGHSM VEGRISQGVI VGDGTDIGGG ASIMGTLSGG GKERVTIGRG
     CLLGAEAGIG ISLGDNCVVE AGLYVTAGTK VTLPNGKVVK ASELSGASDI LYIRDSTTGI
     VKARGRGNHK IELNSDLHQN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024