ID A0A2U9TWT8_9HYPH Unreviewed; 389 AA. AC A0A2U9TWT8; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 29-SEP-2021, entry version 19. DE RecName: Full=Acetylornithine deacetylase {ECO:0000256|ARBA:ARBA00014177}; DE EC=3.5.1.16 {ECO:0000256|ARBA:ARBA00011916}; DE AltName: Full=N-acetylornithinase {ECO:0000256|ARBA:ARBA00020618}; GN ORFNames=A3862_19215 {ECO:0000313|EMBL:AWV17362.1}; OS Methylobacterium sp. XJLW. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=739141 {ECO:0000313|EMBL:AWV17362.1, ECO:0000313|Proteomes:UP000249508}; RN [1] {ECO:0000313|EMBL:AWV17362.1, ECO:0000313|Proteomes:UP000249508} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XJLM {ECO:0000313|Proteomes:UP000249508}; RA Shao Y., Zhong W.; RT "Methylobacterium sp. XJLM Genome sequencing and research."; RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00001551}; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000256|ARBA:ARBA00001941}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- COFACTOR: CC Name=glutathione; Xref=ChEBI:CHEBI:57925; CC Evidence={ECO:0000256|ARBA:ARBA00001955}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine CC from N(2)-acetyl-L-ornithine (linear): step 1/1. CC {ECO:0000256|ARBA:ARBA00004867}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily. CC {ECO:0000256|ARBA:ARBA00005691}. 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; CP016429; AWV17362.1; -; Genomic_DNA. DR RefSeq; WP_043384180.1; NZ_CP016429.1. DR EnsemblBacteria; AWV17362; AWV17362; A3862_19215. DR KEGG; metx:A3862_19215; -. DR UniPathway; UPA00068; UER00110. DR Proteomes; UP000249508; Chromosome. DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway. 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 Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR SUPFAM; SSF55031; SSF55031; 1. DR TIGRFAMs; TIGR01892; AcOrn-deacetyl; 1. DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571}; KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}. FT DOMAIN 177..287 FT /note="M20_dimer" FT /evidence="ECO:0000259|Pfam:PF07687" SQ SEQUENCE 389 AA; 41290 MW; F0D5631A3EAB80B7 CRC64; MSATGERLSP LDMLARLVSF DTESDKSNLP LIEAVCDYLG GWNVPYLHLP NPGGDKAAVL ATIGPMVDGG VVLSGHTDVV PVTGQAWTSD PFTLRLADGR AYGRGAVDMK GFDALALALV PDMLAAGLKR PIHILLSYDE ETTCLGSMDG IARFGADLPR PAAVIVGEPT GMEVADAHKS IVTCLTTVHG HEAHSARPAL GANAVSAACD LVAGLNRIAD LMIERGDPSG RFDPASTTVH VGTIQGGTAR NILAKECRFL WEYRGLPDLD PAEIPRLFAQ EVDRVTRERL NRYGAYGRIE TLEEVDIPGL APEPGSEAER LCLRLAGRNH TVAVPYATEA GRFQAAGLPT VVCGPGDIAQ AHQPDEFITL DALGQGERFL RNLIEACAS //