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 01-MAY-2013, entry version 38.
DE RecName: Full=Acetylornithine deacetylase;
DE Short=AO;
DE Short=Acetylornithinase;
DE EC=3.5.1.16;
DE AltName: Full=N-acetylornithinase;
DE Short=NAO;
GN Name=argE; OrderedLocusNames=ETA_01340;
OS Erwinia tasmaniensis (strain DSM 17950 / Et1/99).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Erwinia.
OX NCBI_TaxID=338565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17950 / 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 -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + H(2)O = acetate + L-
CC ornithine.
CC -!- COFACTOR: Binds 2 zinc or cobalt ions per subunit (By similarity).
CC -!- COFACTOR: Glutathione (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC ornithine from N(2)-acetyl-L-ornithine (linear): step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
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DR EMBL; CU468135; CAO95180.1; -; Genomic_DNA.
DR RefSeq; YP_001906090.1; NC_010694.1.
DR ProteinModelPortal; B2VGA3; -.
DR STRING; 465817.ETA_01340; -.
DR MEROPS; M20.974; -.
DR EnsemblBacteria; CAO95180; CAO95180; ETA_01340.
DR GeneID; 6299638; -.
DR KEGG; eta:ETA_01340; -.
DR PATRIC; 20425902; VBIErwTas9546_0177.
DR eggNOG; COG0624; -.
DR HOGENOM; HOG000243769; -.
DR KO; K01438; -.
DR OMA; CAHQPGE; -.
DR ProtClustDB; PRK05111; -.
DR BioCyc; ETAS465817:GI36-1684-MONOMER; -.
DR UniPathway; UPA00068; UER00110.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:HAMAP.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR HAMAP; MF_01108; ArgE; 1; -.
DR InterPro; IPR010169; AcOrn-deacetyl.
DR InterPro; IPR001261; ArgE/DapE_CS.
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; Peptidase_M20_dimer; 1.
DR TIGRFAMs; TIGR01892; AcOrn-deacetyl; 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;
KW Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1 383 Acetylornithine deacetylase.
FT /FTId=PRO_1000137069.
FT ACT_SITE 82 82 By similarity.
FT ACT_SITE 144 144 By similarity.
FT METAL 80 80 Cobalt or zinc 1 (By similarity).
FT METAL 112 112 Cobalt or zinc 1 (By similarity).
FT METAL 112 112 Cobalt or zinc 2 (By similarity).
FT METAL 145 145 Cobalt or zinc 2 (By similarity).
FT METAL 169 169 Cobalt or zinc 1 (By similarity).
FT METAL 355 355 Cobalt or zinc 2 (By similarity).
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
//
