ID   F3LFB1_9GAMM            Unreviewed;       388 AA.
AC   F3LFB1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:EGG94404.1};
GN   ORFNames=IMCC1989_2803 {ECO:0000313|EMBL:EGG94404.1};
OS   gamma proteobacterium IMCC1989.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX   NCBI_TaxID=937772 {ECO:0000313|EMBL:EGG94404.1, ECO:0000313|Proteomes:UP000010300};
RN   [1] {ECO:0000313|EMBL:EGG94404.1, ECO:0000313|Proteomes:UP000010300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC1989 {ECO:0000313|EMBL:EGG94404.1,
RC   ECO:0000313|Proteomes:UP000010300};
RX   PubMed=21602334; DOI=10.1128/JB.05202-11;
RA   Jang Y., Oh H.M., Kim H., Kang I., Cho J.C.;
RT   "Genome sequence of strain IMCC1989, a novel member of the marine
RT   gammaproteobacteria.";
RL   J. Bacteriol. 193:3672-3673(2011).
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:EGG94404.1}.
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DR   EMBL; AEVK01000085; EGG94404.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3LFB1; -.
DR   OrthoDB; 3665926at2; -.
DR   Proteomes; UP000010300; Unassembled WGS sequence.
DR   GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:InterPro.
DR   CDD; cd03894; M20_ArgE; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR010169; AcOrn-deacetyl.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01892; AcOrn-deacetyl; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF1; 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.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010300}.
FT   DOMAIN          183..294
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   388 AA;  42213 MW;  AF7E58836FC78465 CRC64;
     MAFNEKLFSE QLAQLVATPS VSCTNPKLDM GNRGVIDLLA NWLSDMGFAI DIQEVDGNPD
     KANLIATLGT ANPLHGKGGL VFSGHADTVP YDDKRWSHDP FTLHIENNRA YGLGATDMKG
     FFPAVFAAVQ PFLQSDLKEP IIIVATADEE TSMSGARALL NHPVPKARYG IVGEPTGMQP
     IRMHKGIGME AIKVRGQAGH SSNPALGNNA LDAMHDVITE LKQFRLGLQQ RYRNAGFVID
     VPTLNLGCIH GGDNPNRICG HCELEFDLRT LPGMGLDDLR QEIDILLANV ADKYHIHIER
     DSLFAGTEAF NQPIDSPLIE AVERLTKMNA DSVAFATEAP FLQKMGMDVV VMGPGSIDQA
     HQPDEYIDLA QVPVAVNVLQ GLIKQFCL
//