ID   A0A0T6ASA6_9BACT        Unreviewed;       397 AA.
AC   A0A0T6ASA6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN   ORFNames=XU14_C0003G0047 {ECO:0000313|EMBL:KRT77953.1};
OS   Armatimonadetes bacterium CSP1-3.
OC   Bacteria; Armatimonadota.
OX   NCBI_TaxID=1640515 {ECO:0000313|EMBL:KRT77953.1, ECO:0000313|Proteomes:UP000051026};
RN   [1] {ECO:0000313|EMBL:KRT77953.1, ECO:0000313|Proteomes:UP000051026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-3 {ECO:0000313|EMBL:KRT77953.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRT77953.1}.
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DR   EMBL; LDXQ01000003; KRT77953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6ASA6; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000051026; Unassembled WGS sequence.
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:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   CDD; cd08659; M20_ArgE_DapE-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR010182; ArgE/DapE.
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   NCBIfam; TIGR01910; DapE-ArgE; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KRT77953.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          185..290
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   397 AA;  42477 MW;  73D1DCDE9E405061 CRC64;
     MPIDAPALAD EIERQRPSLV GLLASLVRTD TTNPPGDTRR AVDLIGARFR KLGVDFQILA
     DDPKKPNLLL RLGSGRPELL FNTHMDTVPP GDRTTWRHDP LGAQIEGTRL FGRGAADPKG
     CVAAMVVAVE TLVRLRVSLG GSLLLTLVSD EEVGGAKGTE MLVQRGLLRP DQVIIGEVTH
     NRIAIAEKGL LWVRLVTRGR TAHGSTPWKG VNAVRSMVKV LAALEAEIGA RLRQQTHPLT
     PPPSLSIGTI TGGIATNVVP DHCEATIDRR TLPHEHPADA LAEIDRVVAR LRDEDPDLDV
     TVESVQQGPP IETAADAPLV RAAREVAAAL GLDSAPAGYQ QASDGRFFAA RGIDTMLFGP
     GIPDLAHSPD EYVDLDEVTV AAKFYAQVAA RLLRSGP
//