ID ARGE_ERWT9 Reviewed; 383 AA. AC B2VGA3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 18-JUN-2025, entry version 94. 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=ETA_01340; OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB OS 4357 / Et1/99). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Erwiniaceae; Erwinia. OX NCBI_TaxID=465817; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99; RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x; RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R., RA Geider K.; RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic RT bacterium in the genus Erwinia."; RL Environ. Microbiol. 10:2211-2222(2008). 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; CU468135; CAO95180.1; -; Genomic_DNA. DR RefSeq; WP_012439904.1; NC_010694.1. DR AlphaFoldDB; B2VGA3; -. DR SMR; B2VGA3; -. DR STRING; 465817.ETA_01340; -. DR MEROPS; M20.974; -. DR KEGG; eta:ETA_01340; -. DR eggNOG; COG0624; Bacteria. DR HOGENOM; CLU_021802_2_4_6; -. DR OrthoDB; 3665926at2; -. DR UniPathway; UPA00068; UER00110. DR Proteomes; UP000001726; Chromosome. 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; Reference proteome; Zinc. FT CHAIN 1..383 FT /note="Acetylornithine deacetylase" FT /id="PRO_1000137069" 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; 42132 MW; D5B1ABD10DFB05C9 CRC64; MKTKLPNFIE IYRQLIATPS ISATDSALDQ SNETLINLLG GWFRDLGFTV EVQPVPGTRN KFNMLAKSGS GAGGLLLAGH TDTVPFDDGR WTRDPFTLTE HDNKLYGLGT ADMKGFFAFI LDTLRDVELS TLKKPLYILA TADEETTMAG AKYFSESTAL RPDCAIIGEP TSLKPVRAHK GHISNAIRIQ GQSGHSSDPG RGVNAIELMH ESITQLMALR NTLKERYRHA GFAIPYPTMN FGHIHGGDAA NRICACCELH MDIRPLPGLT LSDLDGLLNE ALAPVSARWP GRLTVGELHP PIPGYECPRE HQLVQVVEKL LGRETEVVNY CTEAPFIQQV CPTLVLGPGS IEQAHQPDEF IDTAFIKPTR DLIAQVVHHF CHH //