ID   DAPE_MYCTO              Reviewed;         354 AA.
AC   P9WHS8; L0T8Y4; Q79FR1; Q7D8M5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Putative succinyl-diaminopimelate desuccinylase DapE;
DE            Short=SDAP desuccinylase;
DE            EC=3.5.1.18;
GN   Name=dapE; OrderedLocusNames=MT1240;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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. {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000250};
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.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45497.1; -; Genomic_DNA.
DR   PIR; H70608; H70608.
DR   RefSeq; WP_003406235.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHS8; -.
DR   SMR; P9WHS8; -.
DR   EnsemblBacteria; AAK45497; AAK45497; MT1240.
DR   KEGG; mtc:MT1240; -.
DR   PATRIC; fig|83331.31.peg.1339; -.
DR   HOGENOM; CLU_021802_1_0_11; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR010174; Succinyl-DAP_deSuclase_DapE.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01900; dapE-gram_pos; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cobalt; Diaminopimelate biosynthesis; Hydrolase;
KW   Lysine biosynthesis; Metal-binding; Zinc.
FT   CHAIN           1..354
FT                   /note="Putative succinyl-diaminopimelate desuccinylase
FT                   DapE"
FT                   /id="PRO_0000428130"
FT   ACT_SITE        71
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        125
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  37273 MW;  F8DA6ABA0E1CA6DB CRC64;
     MLDLRGDPIE LTAALIDIPS ESRKEARIAD EVEAALRAQA SGFEIIRNGN AVLARTKLNR
     SSRVLLAGHL DTVPVAGNLP SRRENDQLHG CGAADMKSGD AVFLHLAATL AEPTHDLTLV
     FYDCEEIDSA ANGLGRIQRE LPDWLSADVA ILGEPTAGCI EAGCQGTLRV VLSVTGTRAH
     SARSWLGDNA IHKLGAVLDR LAVYRARSVD IDGCTYREGL SAVRVAGGVA GNVIPDAASV
     TINYRFAPDR SVAAALQHVH DVFDGLDVQI EQTDAAAGAL PGLSEPAAKA LVEAAGGQVR
     AKYGWTDVSR FAALGIPAVN YGPGDPNLAH CRDERVPVGN ITAAVDLLRR YLGG