ARGE_ECOLI
ID ARGE_ECOLI Reviewed; 383 AA.
AC P23908; Q2M8Q2;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Acetylornithine deacetylase;
DE Short=AO;
DE Short=Acetylornithinase;
DE EC=3.5.1.16 {ECO:0000269|PubMed:10684608, ECO:0000269|PubMed:1551850};
DE AltName: Full=N-acetylornithinase;
DE Short=NAO;
GN Name=argE {ECO:0000303|PubMed:1551850}; OrderedLocusNames=b3957, JW3929;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND PATHWAY.
RC STRAIN=K12;
RX PubMed=1551850; DOI=10.1128/jb.174.7.2323-2331.1992;
RA Meinnel T., Schmitt E., Mechulam Y., Blanquet S.;
RT "Structural and biochemical characterization of the Escherichia coli argE
RT gene product.";
RL J. Bacteriol. 174:2323-2331(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1628835; DOI=10.1016/0378-1119(92)90621-u;
RA Boyen A., Charlier D.R.M., Sakanyan V., Mett I., Glansdorff N.;
RT "Acetylornithine deacetylase, succinyldiaminopimelate desuccinylase and
RT carboxypeptidase G2 are evolutionarily related.";
RL Gene 116:1-6(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / DH5-alpha, and
RC K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
RA Xiao X.G., Cao K.H.;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RC STRAIN=K12;
RX PubMed=6761650; DOI=10.1093/nar/10.24.8031;
RA Piette J., Cunin R., Boyen A., Charlier D.R.M., Crabeel M., van Vliet F.,
RA Glansdorff N., Squires C., Squires C.L.;
RT "The regulatory region of the divergent argECBH operon in Escherichia coli
RT K-12.";
RL Nucleic Acids Res. 10:8031-8048(1982).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RX PubMed=6292860; DOI=10.1093/nar/10.19.5935;
RA Charlier D.R.M., Piette J., Glansdorff N.;
RT "IS3 can function as a mobile promoter in E. coli.";
RL Nucleic Acids Res. 10:5935-5948(1982).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10684608; DOI=10.1021/bi992177f;
RA Javid-Majd F., Blanchard J.S.;
RT "Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase.";
RL Biochemistry 39:1285-1293(2000).
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, ECO:0000269|PubMed:10684608,
CC ECO:0000269|PubMed:1551850}.
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:0000269|PubMed:10684608, ECO:0000269|PubMed:1551850};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15942;
CC Evidence={ECO:0000269|PubMed:10684608, ECO:0000269|PubMed:1551850};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01108,
CC ECO:0000269|PubMed:10684608};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01108,
CC ECO:0000269|PubMed:10684608};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.56 uM for N(2)-acetyl-L-ornithine {ECO:0000269|PubMed:1551850};
CC KM=2.5 mM for N(2)-acetyl-L-ornithine {ECO:0000269|PubMed:10684608};
CC KM=1.3 mM for N(2)-acetyl-L-ornithine (in the presence of cobalt)
CC {ECO:0000269|PubMed:10684608};
CC KM=3.8 mM for N(2)-acetyl-L-ornithine (in the presence of cadmium)
CC {ECO:0000269|PubMed:10684608};
CC KM=2.2 mM for N(2)-acetyl-L-ornithine (in the presence of magnesium)
CC {ECO:0000269|PubMed:10684608};
CC KM=1.3 mM for N(2)-acetyl-L-ornithine (in the presence of nickel)
CC {ECO:0000269|PubMed:10684608};
CC KM=7.2 mM for N(2)-acetyl-L-ornithine (in the presence of zinc)
CC {ECO:0000269|PubMed:10684608};
CC KM=1 mM for N(2)-acetyl-L-alanine {ECO:0000269|PubMed:10684608};
CC KM=8.3 mM for N(2)-acetyl-L-asparagine {ECO:0000269|PubMed:10684608};
CC KM=13 mM for N(2)-acetyl-L-cysteine {ECO:0000269|PubMed:10684608};
CC KM=2.4 mM for N(2)-acetyl-L-glutamine {ECO:0000269|PubMed:10684608};
CC KM=7 mM for N(2)-chloroacetylglycine {ECO:0000269|PubMed:10684608};
CC KM=7 mM for N(2)-acetyl-L-leucine {ECO:0000269|PubMed:10684608};
CC KM=4.1 mM for N(2)-acetyl-L-lysine {ECO:0000269|PubMed:10684608};
CC KM=0.81 mM for N(2)-acetyl-L-methionine
CC {ECO:0000269|PubMed:10684608};
CC KM=2 mM for N(2)-formyl-L-methionine {ECO:0000269|PubMed:10684608};
CC KM=6.7 mM for N(2)-acetyl-serine {ECO:0000269|PubMed:10684608};
CC pH dependence:
CC Optimum pH is 7.7. {ECO:0000269|PubMed:10684608};
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, ECO:0000305|PubMed:1551850}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01108,
CC ECO:0000269|PubMed:1551850}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01108,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01108, ECO:0000305}.
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; X55417; CAA39076.1; -; Genomic_DNA.
DR EMBL; X62807; CAA44625.1; -; Genomic_DNA.
DR EMBL; AY330219; AAP92671.1; -; Genomic_DNA.
DR EMBL; AY331711; AAP92815.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43063.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76939.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77354.1; -; Genomic_DNA.
DR EMBL; J01587; AAB59145.1; -; Genomic_DNA.
DR EMBL; J01589; AAA23484.2; -; Genomic_DNA.
DR PIR; B42377; B42377.
DR RefSeq; NP_418392.1; NC_000913.3.
DR RefSeq; WP_001298964.1; NZ_SSZK01000065.1.
DR AlphaFoldDB; P23908; -.
DR SMR; P23908; -.
DR BioGRID; 4259568; 71.
DR STRING; 511145.b3957; -.
DR MEROPS; M20.974; -.
DR jPOST; P23908; -.
DR PaxDb; P23908; -.
DR PRIDE; P23908; -.
DR EnsemblBacteria; AAC76939; AAC76939; b3957.
DR EnsemblBacteria; BAE77354; BAE77354; BAE77354.
DR GeneID; 66672133; -.
DR GeneID; 948456; -.
DR KEGG; ecj:JW3929; -.
DR KEGG; eco:b3957; -.
DR PATRIC; fig|1411691.4.peg.2748; -.
DR EchoBASE; EB1263; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_4_6; -.
DR InParanoid; P23908; -.
DR OMA; CAHQPGE; -.
DR PhylomeDB; P23908; -.
DR BioCyc; EcoCyc:ACETYLORNDEACET-MON; -.
DR BioCyc; MetaCyc:ACETYLORNDEACET-MON; -.
DR BRENDA; 3.5.1.16; 2026.
DR SABIO-RK; P23908; -.
DR UniPathway; UPA00068; UER00110.
DR PRO; PR:P23908; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IDA:EcoliWiki.
DR GO; GO:0050897; F:cobalt ion binding; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0006526; P:arginine biosynthetic process; IDA:EcoCyc.
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 1: Evidence at protein level;
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_0000185240"
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; 42347 MW; AFE04B99B296540B CRC64;
MKNKLPPFIE IYRALIATPS ISATEEALDQ SNADLITLLA DWFKDLGFNV EVQPVPGTRN
KFNMLASIGQ GAGGLLLAGH TDTVPFDDGR WTRDPFTLTE HDGKLYGLGT ADMKGFFAFI
LDALRDVDVT KLKKPLYILA TADEETSMAG ARYFAETTAL RPDCAIIGEP TSLQPVRAHK
GHISNAIRIQ GQSGHSSDPA RGVNAIELMH DAIGHILQLR DNLKERYHYE AFTVPYPTLN
LGHIHGGDAS NRICACCELH MDIRPLPGMT LNELNGLLND ALAPVSERWP GRLTVDELHP
PIPGYECPPN HQLVEVVEKL LGAKTEVVNY CTEAPFIQTL CPTLVLGPGS INQAHQPDEY
LETRFIKPTR ELITQVIHHF CWH
