ID   Q21NV2_SACD2            Unreviewed;       387 AA.
AC   Q21NV2;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=Acetylornithine deacetylase ArgE. Metallo peptidase. MEROPS family M20A / acetylornithine deacetylase {ECO:0000313|EMBL:ABD79627.1};
DE            EC=3.5.1.16 {ECO:0000313|EMBL:ABD79627.1};
GN   OrderedLocusNames=Sde_0363 {ECO:0000313|EMBL:ABD79627.1};
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD79627.1, ECO:0000313|Proteomes:UP000001947};
RN   [1] {ECO:0000313|EMBL:ABD79627.1, ECO:0000313|Proteomes:UP000001947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024
RC   {ECO:0000313|Proteomes:UP000001947};
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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DR   EMBL; CP000282; ABD79627.1; -; Genomic_DNA.
DR   RefSeq; WP_011466851.1; NC_007912.1.
DR   AlphaFoldDB; Q21NV2; -.
DR   STRING; 203122.Sde_0363; -.
DR   KEGG; sde:Sde_0363; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_021802_2_4_6; -.
DR   OrthoDB; 3665926at2; -.
DR   Proteomes; UP000001947; Chromosome.
DR   GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:ABD79627.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001947}.
FT   DOMAIN          182..291
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   387 AA;  42190 MW;  36971E0EAD6025BE CRC64;
     MPNIAPSDVT VFKQRLQQLI ATPSISCTSA EYDMSNKSVV ELLAQWFEDL GFKIEILPVE
     GFAGKYNLLA TRGTGPGGLV LSGHTDTVPC DPNRWQQDPF QLTEKEQRFY GLGTTDMKGF
     FPVVLAALEG LDLNKLQQPV MILATADEES SMCGARALAA LGRPKARCAV IGEPTELKPI
     RMHKGIMMES VRVQGLAGHS SNPALGHNAL DTMTQVLNEL ILFRSELQSR YQHAGFDINV
     PTLNLGCIHG GDNPNRICGA CELHFDLRAL PGMSNHDLHA EIEKRLQAIG DKNHTPISLT
     PLFPGIASFE EQADSALVKA AERLSGYQAE SVAFATEAPF LQDLGMETIV MGPGTIDCAH
     QPNEYLAHDQ IQPGINIVRG LIEQFCF
//