ID DAPE_CROS8 Reviewed; 375 AA. AC A7ML10; DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 92. 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}; GN OrderedLocusNames=ESA_00778; OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=290339; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-894; RX PubMed=20221447; DOI=10.1371/journal.pone.0009556; RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., RA McClelland M., Forsythe S.J.; RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic RT hybridization analysis with other Cronobacter species."; RL PLoS ONE 5:E9556-E9556(2010). 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 = CC (2S,6S)-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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01690}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000783; ABU76055.1; -; Genomic_DNA. DR RefSeq; WP_012124066.1; NC_009778.1. DR AlphaFoldDB; A7ML10; -. DR SMR; A7ML10; -. DR MEROPS; M20.010; -. DR GeneID; 56729663; -. DR KEGG; esa:ESA_00778; -. DR PATRIC; fig|290339.8.peg.690; -. DR HOGENOM; CLU_021802_4_0_6; -. DR UniPathway; UPA00034; UER00021. DR Proteomes; UP000000260; 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 CDD; cd03891; M20_DapE_proteobac; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 2. 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 NCBIfam; TIGR01246; dapE_proteo; 1. DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1. DR PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 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; PS00758; ARGE_DAPE_CPG2_1; 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..375 FT /note="Succinyl-diaminopimelate desuccinylase" FT /id="PRO_0000375548" FT ACT_SITE 68 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690" FT ACT_SITE 133 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690" FT BINDING 66 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690" FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690" FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690" FT BINDING 134 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690" FT BINDING 162 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690" FT BINDING 348 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01690" SQ SEQUENCE 375 AA; 41244 MW; 5F4EB07003167BEF CRC64; MSCPVIELTQ QLIRRPSLSP DDAGCQALLI ERLQAVGFTV EPMNIGDTQN FWAWRGTGET LAFAGHTDVV PAGDVERWIN PPFEPTIRDG MLFGRGAADM KGSLAAMVVA AERFVAQHPH HRGRLAFLIT SDEEASATNG TVKVVEALMA RGERLDYCLV GEPSSSEVVG DVVKNGRRGS LTCNLTIHGV QGHVAYPHLA DNPVHRAAPM LNELVGIEWD RGNEFFPPTS MQIANIQAGT GSNNVIPGDL HVQFNFRFST ELTDEMIKQR VVALLEKYQL RYTLDWWLSG QPFLTARGKL VDAVVNAVHH YNEIKPQLLT TGGTSDGRFI ARMGAQVVEL GPVNATIHKI NECVKASDLQ LLARMYQRIM EQLVA //