ID ARGE_ECOL5 Reviewed; 383 AA.
AC Q0TAA3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 108.
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=ECP_4170;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG72126.1; -; Genomic_DNA.
DR RefSeq; WP_001298411.1; NC_008253.1.
DR AlphaFoldDB; Q0TAA3; -.
DR SMR; Q0TAA3; -.
DR MEROPS; M20.974; -.
DR KEGG; ecp:ECP_4170; -.
DR HOGENOM; CLU_021802_2_4_6; -.
DR UniPathway; UPA00068; UER00110.
DR Proteomes; UP000009182; 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; Zinc.
FT CHAIN 1..383
FT /note="Acetylornithine deacetylase"
FT /id="PRO_1000065056"
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; 42266 MW; DDD84477F025524E CRC64;
MKNKLPPFIE IYRALIATPS ISATEEALDQ SNADLITLLA DWFKDLGFNV EVQPVPGTRN
KFNMLASCGQ GAGGLLLAGH TDTVPFDDGR WTRDPFTLTE HDGKLYGLGT ADMKGFFAFI
LDALRDVDVT KLAKPLYILA TADEETSMAG ARYFAETTAL RPDCAIIGEP TSLQPVRAHK
GHISNAIRIQ GQSGHSSDPA RGVNAIELMH DAIGHILQLR DNLKERYHYD AFTVPYPTLN
LGHIHGGDAS NRICACCELH MDIRPLPGMT LNELNGLLND ALAPVSERWP GRLTVDELHP
PIPGYECPPN HQLVEVVEKL LGAKTEVVNY CTEAPFIQTL CPTLVLGPGS INQAHQPDEY
LETRFIKPTR ELITQVIHHF CWH
//
