ID ARGE_SHIDS Reviewed; 383 AA. AC Q32AB8; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 104. 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=SDY_3792; OS Shigella dysenteriae serotype 1 (strain Sd197). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300267; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sd197; RX PubMed=16275786; DOI=10.1093/nar/gki954; RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., RA Jin Q.; RT "Genome dynamics and diversity of Shigella species, the etiologic agents of RT bacillary dysentery."; RL Nucleic Acids Res. 33:6445-6458(2005). 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=H2O + N(2)-acetyl-L-ornithine = acetate + L-ornithine; 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; CP000034; ABB63737.1; -; Genomic_DNA. DR RefSeq; WP_005015828.1; NC_007606.1. DR RefSeq; YP_405228.1; NC_007606.1. DR AlphaFoldDB; Q32AB8; -. DR SMR; Q32AB8; -. DR STRING; 300267.SDY_3792; -. DR MEROPS; M20.974; -. DR EnsemblBacteria; ABB63737; ABB63737; SDY_3792. DR KEGG; sdy:SDY_3792; -. DR PATRIC; fig|300267.13.peg.4481; -. DR HOGENOM; CLU_021802_2_4_6; -. DR UniPathway; UPA00068; UER00110. DR Proteomes; UP000002716; 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:arginine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd03894; M20_ArgE; 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 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. 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_1000065062" 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; 42307 MW; D306D4FEAB322410 CRC64; MKNKLPPFIE IYRALIATPS ISATEEALDQ SNADLITLLA DWFKNLGFNV EVQPVPGTRN KFNMLASTGQ GAGGLLLAGH TDTVPFDDGR WTRDPFTLTE HDGKLYGLGT ADMKGFFAFI LDALRDVDVT KLKKPLYILA TADEETSMAG ARYFAETTAL RPDCAIIGEP TSLQPVRAHK GHISNAIRIQ GQSGHSSDPA RGVNAIELMH DAIGHILQLR DSLKERYHYE AFTVPYPTLN LGHIHGGDAS NRICACCELH MDIRPLPGMT LNELNGLLND ALAPVSERWP GRLTVDELHP PIPGYECPPN HQLVEVVEKL LGAKTEVVNY CTEAPFIQTL CPTLVLGPGS INQAHQPDEY LETRFIKPTR ELITQVIHHF CWH //