(data stored in ACNUC7421 zone)

SWISSPROT: C6AZ63_RHILS

ID   C6AZ63_RHILS            Unreviewed;       397 AA.
AC   C6AZ63;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 59.
DE   RecName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000256|HAMAP-Rule:MF_01690, ECO:0000256|SAAS:SAAS00765884};
DE            Short=SDAP desuccinylase {ECO:0000256|HAMAP-Rule:MF_01690};
DE            EC=3.5.1.18 {ECO:0000256|HAMAP-Rule:MF_01690};
DE   AltName: Full=N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase {ECO:0000256|HAMAP-Rule:MF_01690};
GN   Name=dapE {ECO:0000256|HAMAP-Rule:MF_01690};
GN   OrderedLocusNames=Rleg_0078 {ECO:0000313|EMBL:ACS54389.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54389.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54389.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54389.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Catalyzes the hydrolysis of N-succinyl-L,L-
CC       diaminopimelic acid (SDAP), forming succinate and LL-2,6-
CC       diaminoheptanedioate (DAP), an intermediate involved in the
CC       bacterial biosynthesis of lysine and meso-diaminopimelic acid, an
CC       essential component of bacterial cell walls.
CC       {ECO:0000256|SAAS:SAAS00765822}.
CC   -!- CATALYTIC ACTIVITY: N-succinyl-LL-2,6-diaminoheptanedioate + H(2)O
CC       = succinate + LL-2,6-diaminoheptanedioate. {ECO:0000256|HAMAP-
CC       Rule:MF_01690, ECO:0000256|SAAS:SAAS00765871}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (succinylase route): step 3/3. {ECO:0000256|HAMAP-Rule:MF_01690,
CC       ECO:0000256|SAAS:SAAS00765795}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01690,
CC       ECO:0000256|SAAS:SAAS00765883}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. DapE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01690, ECO:0000256|SAAS:SAAS00765843}.
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DR   EMBL; CP001622; ACS54389.1; -; Genomic_DNA.
DR   RefSeq; WP_012755819.1; NC_012850.1.
DR   ProteinModelPortal; C6AZ63; -.
DR   EnsemblBacteria; ACS54389; ACS54389; Rleg_0078.
DR   KEGG; rlg:Rleg_0078; -.
DR   HOGENOM; HOG000243770; -.
DR   KO; K01439; -.
DR   OMA; LNSHHDT; -.
DR   OrthoDB; POG091H059V; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; 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   CDD; cd03891; M20_DapE_proteobac; 1.
DR   HAMAP; MF_01690; DapE; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR005941; DapE_proteobac.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01246; dapE_proteo; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6AZ63.
DR   SWISS-2DPAGE; C6AZ63.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01690,
KW   ECO:0000256|SAAS:SAAS00765856};
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_01690,
KW   ECO:0000256|SAAS:SAAS00765819};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_01690,
KW   ECO:0000256|SAAS:SAAS00765792};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01690,
KW   ECO:0000256|SAAS:SAAS00786827};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01690,
KW   ECO:0000256|SAAS:SAAS00765799};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01690,
KW   ECO:0000256|SAAS:SAAS00786925};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01690, ECO:0000256|SAAS:SAAS00765827}.
FT   DOMAIN      182    288       M20_dimer. {ECO:0000259|Pfam:PF07687}.
FT   ACT_SITE     75     75       {ECO:0000256|HAMAP-Rule:MF_01690}.
FT   ACT_SITE    140    140       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01690}.
FT   METAL        73     73       Cobalt or zinc 1. {ECO:0000256|HAMAP-
FT                                Rule:MF_01690}.
FT   METAL       106    106       Cobalt or zinc 1. {ECO:0000256|HAMAP-
FT                                Rule:MF_01690}.
FT   METAL       106    106       Cobalt or zinc 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_01690}.
FT   METAL       141    141       Cobalt or zinc 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_01690}.
FT   METAL       169    169       Cobalt or zinc 1. {ECO:0000256|HAMAP-
FT                                Rule:MF_01690}.
FT   METAL       366    366       Cobalt or zinc 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_01690}.
SQ   SEQUENCE   397 AA;  42259 MW;  D489F5463C72BDA3 CRC64;
     MTATDPVANL QTLIRCPSVT PAEGGALTAL EAMLAPLGFA LDRVKASEEG TPEIENLYAR
     LGKDGPHLMF AGHTDVVPVG DEAAWTHPPF EAQISKGELF GRGAVDMKGG IACFVAAVAR
     HIEKNGPPNG SISFLITGDE EGPAINGTIK LLQWAAERGE RWDACLVGEP TNPDRLGDMI
     KIGRRGSLSG KITVHGVQGH AAYPHLADNP VRGMLQLTQA LMDPPFDAGT GDFQPSNLEV
     TTVDVGNPAT NVIPAKASAS FNIRFNDSWT VETLRAEILR RLEAAAGNGA LRPGRDPVAY
     DIVWADRPSH VFLTRNNALI ASLSSAVESV AGQSPRLSTT GGTSDARFIK DYCPVVEFGL
     VGQTMHMVDE RVAVADLETL TAIYETFIAR WFANAGL
//

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