ID A0A0N0TL12_9ACTN Unreviewed; 414 AA.
AC A0A0N0TL12;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN ORFNames=ADK66_07280 {ECO:0000313|EMBL:KOX11004.1};
OS Micromonospora sp. NRRL B-16802.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1415541 {ECO:0000313|EMBL:KOX11004.1, ECO:0000313|Proteomes:UP000037709};
RN [1] {ECO:0000313|EMBL:KOX11004.1, ECO:0000313|Proteomes:UP000037709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16802 {ECO:0000313|EMBL:KOX11004.1,
RC ECO:0000313|Proteomes:UP000037709};
RA Noorani M.;
RL Submitted (JUL-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:KOX11004.1}.
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DR EMBL; LGEB01000046; KOX11004.1; -; Genomic_DNA.
DR RefSeq; WP_053653148.1; NZ_LGEB01000046.1.
DR AlphaFoldDB; A0A0N0TL12; -.
DR STRING; 1415541.ADK66_07280; -.
DR PATRIC; fig|1415541.3.peg.1542; -.
DR OrthoDB; 7055905at2; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000037709; 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; 3.40.630.10; 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; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 193..298
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 414 AA; 43448 MW; ECED5D7279CC530D CRC64;
MTSDTHAALR AGHLVDEQAV VALTQELVRI PSTWDPARER SEQPAAERVA EVMRGFGWQP
EVVEVAPGRP NVVAVVDGGL PGPTLMFEGH TDVVTEGSRD EWTVDPFGGD IVDGRLYGRG
SADMKAGVAA MIHATRAVEL AGPFPGRIVV AALVDEEGQM LGAKHFTTTS LAAEVDAAIV
CEPEAEEICA VAKGAVRLLV TCTGRMAHGA MPQHGRNPIP AVAELVQALN RFQAELQVVP
GEHEHLGLTY LTPTVLDAGS ADQINVIPGR AVLGVDCRTV PGVDHAALAE RVRSDAAAIG
ARHGVTFAVD VVDDRPCAVT PEDHPIALAV ARAHRDVTGV EPAFGGVPGA TDGTILWRDS
GIPNVVYGPG PKWIAHQPDE YVEVDDVVRK TRVYAEAALV FLTGATVAEA GGAL
//
