ID A0A372UT13_9BACE Unreviewed; 355 AA. AC A0A372UT13; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 29-MAY-2024, entry version 16. DE RecName: Full=succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00011921}; DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921}; GN ORFNames=DW640_10245 {ECO:0000313|EMBL:RGC85278.1}; OS Bacteroides sp. AM23-12. OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=2292942 {ECO:0000313|EMBL:RGC85278.1, ECO:0000313|Proteomes:UP000264414}; RN [1] {ECO:0000313|EMBL:RGC85278.1, ECO:0000313|Proteomes:UP000264414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM23-12 {ECO:0000313|EMBL:RGC85278.1, RC ECO:0000313|Proteomes:UP000264414}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. 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; CC Evidence={ECO:0000256|ARBA:ARBA00001246}; 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; L-lysine biosynthesis via DAP CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate CC (succinylase route): step 3/3. {ECO:0000256|ARBA:ARBA00005130}. 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:RGC85278.1}. 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; QTLF01000008; RGC85278.1; -; Genomic_DNA. DR AlphaFoldDB; A0A372UT13; -. DR Proteomes; UP000264414; Unassembled WGS sequence. DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:TreeGrafter. DR CDD; cd05651; M20_ArgE_DapE-like; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 2. 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 PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1. DR PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 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. PE 4: Predicted; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RGC85278.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 169..268 FT /note="Peptidase M20 dimerisation" FT /evidence="ECO:0000259|Pfam:PF07687" SQ SEQUENCE 355 AA; 39204 MW; C3FD86854B46EABF CRC64; MKYDIPTMTA EAVSLLKSLI SIPSISREET QAADFLQNYI EAEGMQTGRK GNNVWCLSPM FDLKKPTILL NSHIDTVKPV NGWRKDPFTP REENGKLYGL GSNDAGASVV SLLQVFLQLC RTSQNYNLIY LASCEEEVSG KDGIESVLPG LPPVSFAIVG EPTEMQPAIA EKGLMVLDVT ATGKAGHAAR DEGDNAIYKV LNDIAWFRDY RFEKESPLLG PVKMSVTVIN AGTQHNVVPD KCTFVVDIRS NELYSNEDLF AEIRKHIACD AKARSFRLNS SRIDEKHPFV QKAVKMGRIP FGSPTLSDQA LMSFASVKIG PGRSSRSHTA EEYIMLKEIE EAIGIYLDLL DGLKL //