ID ARGE_BUCAI Reviewed; 381 AA. AC P57155; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 28-JAN-2026, entry version 146. 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}; OrderedLocusNames=BU047; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). 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, ECO:0000305}. 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; BA000003; BAB12770.1; -; Genomic_DNA. DR RefSeq; WP_010895917.1; NC_002528.1. DR AlphaFoldDB; P57155; -. DR SMR; P57155; -. DR STRING; 563178.BUAP5A_046; -. DR EnsemblBacteria; BAB12770; BAB12770; BAB12770. DR KEGG; buc:BU047; -. DR PATRIC; fig|107806.10.peg.56; -. DR eggNOG; COG0624; Bacteria. DR HOGENOM; CLU_021802_2_4_6; -. DR UniPathway; UPA00068; UER00110. DR Proteomes; UP000001806; 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..381 FT /note="Acetylornithine deacetylase" FT /id="PRO_0000185238" FT ACT_SITE 81 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT ACT_SITE 143 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT BINDING 79 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT BINDING 111 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT BINDING 111 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT BINDING 144 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT BINDING 168 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" FT BINDING 354 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108" SQ SEQUENCE 381 AA; 43045 MW; A837B49131A1E0ED CRC64; MIRKIPSFIE VYKSLIQIPT ISSNNKLLDQ SNKNFIDLLS NYFSDLNFSV KNYQIPHTDK YNMLACVGSG NGGLLLSGHS DTVDFDEKKW TKDPFKLTET NNKFYGLGAV DMKGFFALIL EVISSINIKK INKPIYILAT ANEETDMSGA RNFIQSTIIK PDCIIIGEPT SLKLINAHKG HMSYSIKVIG DTGHSSNPDH GVNSIEIMHD VIRSLLILKK YFKEEYQHPN FSIPYPTMNL SSIHGGSAIN RICPLCILNF EIRPIPGLTL TQIEIVIKEK LETIMKKWSH RIFIKKLFSS VPAYECPHNS GTIKIVEKLC QLNSAAVNYC TEAPFLQRIA PTLILGPGSI EQAHQPDEYL EHYFIQPTKN IITKLINKFC Y //