ARGE_SHIBS
ID ARGE_SHIBS Reviewed; 383 AA.
AC Q31U31;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=SBO_3976;
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000036; ABB68427.1; -; Genomic_DNA.
DR RefSeq; WP_004987941.1; NC_007613.1.
DR AlphaFoldDB; Q31U31; -.
DR SMR; Q31U31; -.
DR MEROPS; M20.974; -.
DR EnsemblBacteria; ABB68427; ABB68427; SBO_3976.
DR KEGG; sbo:SBO_3976; -.
DR HOGENOM; CLU_021802_2_4_6; -.
DR OMA; CAHQPGE; -.
DR UniPathway; UPA00068; UER00110.
DR Proteomes; UP000007067; 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; Zinc.
FT CHAIN 1..383
FT /note="Acetylornithine deacetylase"
FT /id="PRO_1000065061"
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; 42400 MW; 2912196D07EEA0A0 CRC64;
MKNKLPPFIE IYRALIATPS ISATEEALDQ SNADLITLLA DWFKDLGFNV EVQPVPGTRN
KFNMLASIGQ GAGGLLLAGH TDTVPFDDGR WTRDPFTLTE HDGKLYGLGT ADMKGFFAFI
LDALRDIDVT KLKKPLYILA TADEETSMAG ARYFAETTAL RPDCAIIGEP TSLQPVRAHK
GHISNAIRIQ GQSGHSSDPA RGVNAIELMH DAIGHILQLR DNLKERYHYE AFTVPYPTLN
LGHIHGGDAS NRICACCELH MDIRPLPGMT LNELNGLLND ALAPVIERWP GRLTVDELHP
PIPGYECPPN HQLVEVVEKL LGAKTEVVNY CTEAPFIQTL CPTLVLGPGS INQAHQPDEY
LETRFIKPTR ELIIQVIHHF CWH
