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DAPE_RICB8
ID   DAPE_RICB8              Reviewed;         391 AA.
AC   A8GYC8;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=A1I_07900;
OS   Rickettsia bellii (strain OSU 85-389).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=391896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OSU 85-389;
RA   Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.;
RT   "Complete genome sequencing of Rickettsia bellii.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000849; ABV79878.1; -; Genomic_DNA.
DR   RefSeq; WP_012152314.1; NC_009883.1.
DR   AlphaFoldDB; A8GYC8; -.
DR   SMR; A8GYC8; -.
DR   KEGG; rbo:A1I_07900; -.
DR   HOGENOM; CLU_021802_4_0_5; -.
DR   OMA; LNSHHDT; -.
DR   UniPathway; UPA00034; UER00021.
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; Zinc.
FT   CHAIN           1..391
FT                   /note="Succinyl-diaminopimelate desuccinylase"
FT                   /id="PRO_0000375698"
FT   ACT_SITE        69
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         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01690"
FT   BINDING         101
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   391 AA;  43734 MW;  05520BE007E01CD4 CRC64;
     MHTTYLKNLI GFESLTPQSN GAIEYIDDLL KEHGFKTEVK IFGETEQVTN LYAVYGNSKP
     NICFVGHVDV VPAGDPNLWH NSNPFKAHEQ EGKIYGRGTV DMKGSIACFL AASLDFIKNN
     TDFVGSISFL LTSDEEGKAK HGTKEMLQYI YNQGHEIDFA IVGEPTCEKE IGDTIKIGRR
     GSINFKLAVK GLGGHVAYPQ KANNPLPCLI RILNELTNIK LDKGTEFFQN SNLEVTNIDV
     DNNTTNVIPE TATVHFNIRF NNLHSAETLA KQVEEIIKQH CQKHKLDYTL EYNSSADSFI
     QNPNDKIKEF ATIVEKTLNI KPNFSTSGGT SDARFVKNYC PLVEFGLLSD TAHKINEYTK
     ISDLQKLYDV YYNFLMETLN VTGSPPLLGM T
 
 
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