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Database: UniProt
Entry: A0A1I1SC66_9BACI
LinkDB: A0A1I1SC66_9BACI
Original site: A0A1I1SC66_9BACI 
ID   A0A1I1SC66_9BACI        Unreviewed;       398 AA.
AC   A0A1I1SC66;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=4-acetamidobutyryl-CoA deacetylase {ECO:0000313|EMBL:SFD44017.1};
GN   ORFNames=SAMN05216238_101347 {ECO:0000313|EMBL:SFD44017.1};
OS   Lentibacillus persicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX   NCBI_TaxID=640948 {ECO:0000313|EMBL:SFD44017.1, ECO:0000313|Proteomes:UP000199474};
RN   [1] {ECO:0000313|EMBL:SFD44017.1, ECO:0000313|Proteomes:UP000199474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22530 {ECO:0000313|EMBL:SFD44017.1,
RC   ECO:0000313|Proteomes:UP000199474};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; FOMR01000001; SFD44017.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1SC66; -.
DR   STRING; 640948.SAMN05216238_101347; -.
DR   Proteomes; UP000199474; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR010182; ArgE/DapE.
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   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.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          178..290
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   398 AA;  43629 MW;  6F84EF8D1A5E44DF CRC64;
     MIRQPSTAGN EKGVQQLVSE KLTQLGLEVD IWEPDVKALS KSKFFNSSRS DFDNSPNVVG
     VLAGTGGGHS IILNGHVDVV PPGDLNTWDE DPYSGRVKDG KVYGRGATDM KGGNAALLIA
     LETIVDMDVQ LKGDVIFQSV IEEESGGSGT LSVIEERGYK GDVALLPEPS EMKIFPKQQG
     SVWFKVKVKG ISAHGGTRYE GVSAIDKGIK VYHKLLELEK IRNDRLNDPL YAENPIPIPL
     NIGQFNGGYF PSAVPDDVEI EGRYGIAPAE SIEEAQREFE ETLKHLAEDD EWFKEHPVTV
     EWFGLRLPPG GCDLDHPFLE VLKNSYQSVK NEEPTLAGST WGTDGGLLTQ AGNIPSLIFG
     PGTTRMAHFS NEYVELDKIF DTAEIITEAI LEWCNRSK
//
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