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Database: UniProt
Entry: A0A429FZ66_9ACTN
LinkDB: A0A429FZ66_9ACTN
Original site: A0A429FZ66_9ACTN 
ID   A0A429FZ66_9ACTN        Unreviewed;       371 AA.
AC   A0A429FZ66;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:RSN66860.1};
GN   ORFNames=DMH08_15350 {ECO:0000313|EMBL:RSN66860.1};
OS   Actinomadura sp. WAC 06369.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=2203193 {ECO:0000313|EMBL:RSN66860.1, ECO:0000313|Proteomes:UP000288610};
RN   [1] {ECO:0000313|EMBL:RSN66860.1, ECO:0000313|Proteomes:UP000288610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC 06369 {ECO:0000313|EMBL:RSN66860.1,
RC   ECO:0000313|Proteomes:UP000288610};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
RL   Submitted (MAY-2018) 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:RSN66860.1}.
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DR   EMBL; QHJN01000047; RSN66860.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A429FZ66; -.
DR   Proteomes; UP000288610; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd08659; M20_ArgE_DapE-like; 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   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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288610}.
FT   DOMAIN          170..269
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   371 AA;  38157 MW;  37CC52577C3C613E CRC64;
     MDTAGPTIDA LDLARRLVRT DTRAGGERAA ADLVAGVLDG AGFDVRVDEP EAGRANVVAR
     RGPAAPRVPV TLTGHLDTVP ADPSGWSFDP LCGEVRDGRL LGRGSSDMKA GVACQIAAAA
     DAGRDRPLQL VFTFGEETGC DGAARLDPAS LVPTDLLVVA EPTANRTVLG HKGTLWLRAT
     AHGVSAHGSR PELGRNALAA LAAAATRVHG HRGWPVSPTH GPVTVNVGTF HAGVQPNLVP
     DRAEMRLDVR TVPGFGSDAA VAAIAELCGP EVGLERLVDL PGVATDPASP DVARVLELLA
     PGASAREPEY ATYFTDASVL TGMLGGPDVV VYGPGDPEQA HVTDESCSVH RIGEAAAAFR
     RLLDASPPVT A
//
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