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Database: UniProt
Entry: A0A117RYT4_9ACTN
LinkDB: A0A117RYT4_9ACTN
Original site: A0A117RYT4_9ACTN 
ID   A0A117RYT4_9ACTN        Unreviewed;       359 AA.
AC   A0A117RYT4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:KUO17107.1};
DE            EC=3.5.1.18 {ECO:0000313|EMBL:KUO17107.1};
GN   ORFNames=AQJ91_32875 {ECO:0000313|EMBL:KUO17107.1};
OS   Streptomyces dysideae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO17107.1, ECO:0000313|Proteomes:UP000053260};
RN   [1] {ECO:0000313|EMBL:KUO17107.1, ECO:0000313|Proteomes:UP000053260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RV15 {ECO:0000313|EMBL:KUO17107.1,
RC   ECO:0000313|Proteomes:UP000053260};
RA   Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA   Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT   sponge.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KUO17107.1}.
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DR   EMBL; LMXB01000081; KUO17107.1; -; Genomic_DNA.
DR   RefSeq; WP_067028932.1; NZ_KQ949100.1.
DR   AlphaFoldDB; A0A117RYT4; -.
DR   STRING; 909626.AQJ91_32875; -.
DR   OrthoDB; 9809784at2; -.
DR   Proteomes; UP000053260; 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:InterPro.
DR   CDD; cd05647; M20_DapE_actinobac; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
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   NCBIfam; TIGR01900; dapE-gram_pos; 1.
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.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KUO17107.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053260}.
FT   DOMAIN          170..268
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   359 AA;  38319 MW;  AD56A483835EBCE9 CRC64;
     MADTPLDLTL DAARLTAQLV DFPSESGTEK PLADAIETAL RALPHLTVDR YGNNVVARTN
     LGRPERVILA GHIDTVPIAD NVPSRLDEDG VLWGCGTCDM KAGVAVQLRI AETVPAPNRD
     LTFVFYDNEE VAADLNGLKH VSEAHPEWLE GDFAVLLEPS DGQVEGGCQG TLRVLLKTEG
     ERAHSARSWM GSNAIHAAAP ILAKLAAYEP RYPVIDGLEY REGLSAVGIT GGVAGNVIPD
     ACVVTVNFRY APDRSEEEAL AHVREVFADC GVAEFVVDDH SGAALPGLSH PAAAAFIKAV
     GGTPQPKYGW TDVSRFSSLG VPAVNYGPGN PHLAHKRDER VDTAKILAGE ERLRTWLTA
//
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