ID ARGE_SALDC Reviewed; 383 AA. AC B5FPX2; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2008, sequence version 1. DT 10-JUN-2026, entry version 91. DE RecName: Full=Acetylornithine deacetylase {ECO:0000255|HAMAP-Rule:MF_01108}; DE Short=AO {ECO:0000255|HAMAP-Rule:MF_01108}; DE Short=Acetylornithinase {ECO:0000255|HAMAP-Rule:MF_01108}; DE EC=3.5.1.16 {ECO:0000255|HAMAP-Rule:MF_01108}; DE AltName: Full=N-acetylornithinase {ECO:0000255|HAMAP-Rule:MF_01108}; DE Short=NAO {ECO:0000255|HAMAP-Rule:MF_01108}; GN Name=argE {ECO:0000255|HAMAP-Rule:MF_01108}; GN OrderedLocusNames=SeD_A4525; OS Salmonella dublin (strain CT_02021853). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=439851; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT_02021853; RX PubMed=21602358; DOI=10.1128/jb.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). CC -!- FUNCTION: Catalyzes the hydrolysis of the amide bond of N(2)-acetylated CC L-amino acids. Cleaves the acetyl group from N-acetyl-L-ornithine to CC form L-ornithine, an intermediate in L-arginine biosynthesis pathway, CC and a branchpoint in the synthesis of polyamines. {ECO:0000255|HAMAP- CC Rule:MF_01108}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(2)-acetyl-L-ornithine + H2O = L-ornithine + acetate; CC Xref=Rhea:RHEA:15941, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=3.5.1.16; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01108}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01108}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01108}; CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01108}; CC -!- COFACTOR: CC Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01108}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine CC from N(2)-acetyl-L-ornithine (linear): step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01108}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01108}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01108}. CC -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01108}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001144; ACH77352.1; -; Genomic_DNA. DR RefSeq; WP_000800208.1; NC_011205.1. DR AlphaFoldDB; B5FPX2; -. DR SMR; B5FPX2; -. DR MEROPS; M20.974; -. DR KEGG; sed:SeD_A4525; -. DR HOGENOM; CLU_021802_2_4_6; -. DR UniPathway; UPA00068; UER00110. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd03894; M20_ArgE; 1. DR FunFam; 3.30.70.360:FF:000003; Acetylornithine deacetylase; 1. DR Gene3D; 3.30.70.360; -; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR HAMAP; MF_01108; ArgE; 1. DR InterPro; IPR010169; AcOrn-deacetyl. DR InterPro; IPR001261; ArgE/DapE_CS. DR InterPro; IPR036264; Bact_exopeptidase_dim_dom. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR InterPro; IPR050072; Peptidase_M20A. DR NCBIfam; TIGR01892; AcOrn-deacetyl; 1. DR NCBIfam; NF003474; PRK05111.1; 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. DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1. DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Cobalt; Cytoplasm; KW Hydrolase; Metal-binding; Zinc. FT CHAIN 1..383 FT /note="Acetylornithine deacetylase" FT /id="PRO_1000137074" FT ACT_SITE 82 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT ACT_SITE 144 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT BINDING 80 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT BINDING 112 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT BINDING 112 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT BINDING 169 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT BINDING 355 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" SQ SEQUENCE 383 AA; 42202 MW; A56BDB11FBDE6475 CRC64; MKNVLPPFIE IYRALIATPS ISATEESLDQ SNASLITLLA GWFSDLGFNV EVQPVPGTRN KFNMLASTGH GAGGLLLTGH TDTVPFDDGR WTRDPFTLTE HDNKLYGLGT ADMKGFFAFI LDALRDVDVT KLKKPLYILA TADEETSMAG ARYFSETTAL RPDCAIIGEP TSLQPIRAHK GHISNVVRVL GQSGHSSDPA RGVNAIELMH DAIGHIMQLR DSLKARYHYE AFTVPYPTLN LGHIHGGDAS NRICACCELH MDIRPLPGMT LNDLNGLLND ALAPVSERWP GRLTVAELHP PIPGYECPPD HQLVEVVEKL LGTKTDVVNY CTEAPFMQTL CPTLVLGPGS INQAHQPDEY LETRFIKPTR ELITQVVHHF CWH //