ARGE_YERP3
ID ARGE_YERP3 Reviewed; 389 AA.
AC A7FCZ8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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};
GN OrderedLocusNames=YpsIP31758_0126;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS46874.1; -; Genomic_DNA.
DR AlphaFoldDB; A7FCZ8; -.
DR SMR; A7FCZ8; -.
DR MEROPS; M20.974; -.
DR EnsemblBacteria; ABS46874; ABS46874; YpsIP31758_0126.
DR KEGG; ypi:YpsIP31758_0126; -.
DR HOGENOM; CLU_021802_2_4_6; -.
DR OMA; CAHQPGE; -.
DR UniPathway; UPA00068; UER00110.
DR Proteomes; UP000002412; 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..389
FT /note="Acetylornithine deacetylase"
FT /id="PRO_1000065067"
FT ACT_SITE 87
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT ACT_SITE 149
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
SQ SEQUENCE 389 AA; 42950 MW; AF6E66533CE62038 CRC64;
MKMKLPPFIE LYRALIATPS ISAADSALDQ SNEALINLLA GWFADLGFRV EIQPVPDTRH
KFNLLASIGE NENGEGHGGL LLAGHTDTVP YDEGRWTRDP FTLTEHDHKL YGLGTADMKG
FFAFILDAVR DIDASKLTKP LYILATADEE TTMAGARYFA ANTQLRPDFA IIGEPTSLQP
VRAHKGHISN AIRITGQSGH SSDPARGVNA IDLMHESITQ LMALRTTLQE RYHNPAFTIP
YPTMNFGHIN GGDAANRICA CCELHMDIRP LPGLTLSDLN ELMTEALEPV SQRWPGRLSI
DELHPPIPGY ECPTDHHMVG VIEKLLGERT AVVNYCTEAP FIQQVCPTLV LGPGSINQAH
QPDEFIDMAF IEPTRELIGQ LVDHFCQQK
