ARGE_BUCAI
ID ARGE_BUCAI Reviewed; 381 AA.
AC P57155;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=BU047;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(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}.
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, ECO:0000305}.
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DR EMBL; BA000003; BAB12770.1; -; Genomic_DNA.
DR RefSeq; NP_239884.1; NC_002528.1.
DR RefSeq; WP_010895917.1; NC_002528.1.
DR AlphaFoldDB; P57155; -.
DR SMR; P57155; -.
DR STRING; 107806.10038735; -.
DR EnsemblBacteria; BAB12770; BAB12770; BAB12770.
DR KEGG; buc:BU047; -.
DR PATRIC; fig|107806.10.peg.56; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_4_6; -.
DR OMA; CAHQPGE; -.
DR UniPathway; UPA00068; UER00110.
DR Proteomes; UP000001806; 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..381
FT /note="Acetylornithine deacetylase"
FT /id="PRO_0000185238"
FT ACT_SITE 81
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT ACT_SITE 143
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
SQ SEQUENCE 381 AA; 43045 MW; A837B49131A1E0ED CRC64;
MIRKIPSFIE VYKSLIQIPT ISSNNKLLDQ SNKNFIDLLS NYFSDLNFSV KNYQIPHTDK
YNMLACVGSG NGGLLLSGHS DTVDFDEKKW TKDPFKLTET NNKFYGLGAV DMKGFFALIL
EVISSINIKK INKPIYILAT ANEETDMSGA RNFIQSTIIK PDCIIIGEPT SLKLINAHKG
HMSYSIKVIG DTGHSSNPDH GVNSIEIMHD VIRSLLILKK YFKEEYQHPN FSIPYPTMNL
SSIHGGSAIN RICPLCILNF EIRPIPGLTL TQIEIVIKEK LETIMKKWSH RIFIKKLFSS
VPAYECPHNS GTIKIVEKLC QLNSAAVNYC TEAPFLQRIA PTLILGPGSI EQAHQPDEYL
EHYFIQPTKN IITKLINKFC Y
