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DAPE_RUEPO
ID   DAPE_RUEPO              Reviewed;         380 AA.
AC   Q5LN80;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000255|HAMAP-Rule:MF_01690};
DE            Short=SDAP desuccinylase {ECO:0000255|HAMAP-Rule:MF_01690};
DE            EC=3.5.1.18 {ECO:0000255|HAMAP-Rule:MF_01690};
DE   AltName: Full=N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase {ECO:0000255|HAMAP-Rule:MF_01690};
GN   Name=dapE {ECO:0000255|HAMAP-Rule:MF_01690}; OrderedLocusNames=SPO3332;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic
CC       acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP),
CC       an intermediate involved in the bacterial biosynthesis of lysine and
CC       meso-diaminopimelic acid, an essential component of bacterial cell
CC       walls. {ECO:0000255|HAMAP-Rule:MF_01690}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-
CC         2,6-diaminoheptanedioate + succinate; Xref=Rhea:RHEA:22608,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30031, ChEBI:CHEBI:57609,
CC         ChEBI:CHEBI:58087; EC=3.5.1.18; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01690};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01690};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01690};
CC       Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01690};
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:0000255|HAMAP-Rule:MF_01690}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01690}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. DapE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01690}.
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DR   EMBL; CP000031; AAV96559.1; -; Genomic_DNA.
DR   RefSeq; WP_011049015.1; NC_003911.12.
DR   AlphaFoldDB; Q5LN80; -.
DR   SMR; Q5LN80; -.
DR   STRING; 246200.SPO3332; -.
DR   EnsemblBacteria; AAV96559; AAV96559; SPO3332.
DR   KEGG; sil:SPO3332; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_021802_4_0_5; -.
DR   OMA; LNSHHDT; -.
DR   OrthoDB; 275025at2; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc 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   HAMAP; MF_01690; DapE; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
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; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cobalt; Diaminopimelate biosynthesis; Hydrolase;
KW   Lysine biosynthesis; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..380
FT                   /note="Succinyl-diaminopimelate desuccinylase"
FT                   /id="PRO_0000375750"
FT   ACT_SITE        71
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   ACT_SITE        135
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   BINDING         136
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
SQ   SEQUENCE   380 AA;  40185 MW;  A74EED6C67D4F0A1 CRC64;
     MTLDAARLTA DLIRCASVTP ADDGALDVLE RVLSQAGFSC TRVDRGGICN LFARWGDKGH
     ARSFGFNGHT DVVPVGDAAA WTVAPFGAEE KDGFLYGRGA TDMKSGVAAF VAAAVDLVTT
     TPPEGAVIVT ITGDEEGDAL DGTKALLDYM AASGERMSVC LVGEPTCPDR MGEMIKIGRR
     GSMTAWFTVT GVQGHSAYPH RAKNPLPAMA RLMDRLASHG LDQGTDHFDP STLAVVTIDT
     GNTATNVIPA QCRGAVNIRF NDLHSGASLT GWMQGEADRV AEEFGVAVEM KVKISGESFL
     TPPGELSDLV AAAVEAETGV TPVLSTSGGT SDARFVKDHC PVVEFGLVGR TMHQVDERVE
     IAQIHQLKAI YGRILRDFFA
 
 
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