ARGE_ERWT9
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 03-AUG-2022, entry version 83.
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=ETA_01340;
OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS 4357 / Et1/99).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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=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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01108};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-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;
CC Evidence={ECO:0000255|HAMAP-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}.
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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 EnsemblBacteria; CAO95180; CAO95180; ETA_01340.
DR KEGG; eta:ETA_01340; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_4_6; -.
DR OMA; CAHQPGE; -.
DR OrthoDB; 906744at2; -.
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:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR43808:SF1; PTHR43808:SF1; 1.
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; 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
