ID W0LCW9_9GAMM Unreviewed; 385 AA.
AC W0LCW9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Acetylornithine deacetylase {ECO:0000256|HAMAP-Rule:MF_01108};
DE Short=AO {ECO:0000256|HAMAP-Rule:MF_01108};
DE Short=Acetylornithinase {ECO:0000256|HAMAP-Rule:MF_01108};
DE EC=3.5.1.16 {ECO:0000256|HAMAP-Rule:MF_01108};
DE AltName: Full=N-acetylornithinase {ECO:0000256|HAMAP-Rule:MF_01108};
DE Short=NAO {ECO:0000256|HAMAP-Rule:MF_01108};
GN Name=argE {ECO:0000256|HAMAP-Rule:MF_01108};
GN ORFNames=Z042_11180 {ECO:0000313|EMBL:AHG20122.1};
OS Chania multitudinisentens RB-25.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Chania.
OX NCBI_TaxID=1441930 {ECO:0000313|EMBL:AHG20122.1, ECO:0000313|Proteomes:UP000019030};
RN [1] {ECO:0000313|EMBL:AHG20122.1, ECO:0000313|Proteomes:UP000019030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB-25 {ECO:0000313|EMBL:AHG20122.1,
RC ECO:0000313|Proteomes:UP000019030};
RA Robson E.H.J.;
RT "Isolation of Serratia multitudinisentens RB-25 from Ex-Landfill site.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AHG20122.1, ECO:0000313|Proteomes:UP000019030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB-25 {ECO:0000313|EMBL:AHG20122.1,
RC ECO:0000313|Proteomes:UP000019030};
RA Chan K.-G.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01108};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01108};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01108};
CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01108};
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC Evidence={ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01108}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01108}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
CC {ECO:0000256|ARBA:ARBA00005691, ECO:0000256|HAMAP-Rule:MF_01108}.
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DR EMBL; CP007044; AHG20122.1; -; Genomic_DNA.
DR RefSeq; WP_037407245.1; NZ_JAJC01000034.1.
DR AlphaFoldDB; W0LCW9; -.
DR STRING; 1441930.Z042_11180; -.
DR KEGG; sfo:Z042_11180; -.
DR PATRIC; fig|1441930.4.peg.2223; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_4_6; -.
DR UniPathway; UPA00068; UER00110.
DR Proteomes; UP000019030; 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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01108};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_01108}; Cobalt {ECO:0000256|HAMAP-Rule:MF_01108};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01108};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01108};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01108}; Reference proteome {ECO:0000313|Proteomes:UP000019030};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01108}.
FT DOMAIN 176..283
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 80
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01108"
FT ACT_SITE 142
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01108"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01108"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01108"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01108"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01108"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01108"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01108"
SQ SEQUENCE 385 AA; 42045 MW; 4D62429963E68FAF CRC64;
MKLPPFIELY RALIATPSIS ATDGALDQSN EALINLLAGW FSDLGFRVDV QPVPGTRSKF
NLLASIGTGS GGLLLAGHTD TVPYDQGRWT RDPFTLTEHD NKLYGLGTAD MKGFFAFILD
AVRDLDAAKL TKPLYILATA DEETTMAGAR YFAASTTIRP DFAIIGEPTS LQPVRAHKGH
LSNAIRIVGQ SGHSSDPARG VNAIDLMHES IGHLMELRKT LQERYNNPAF AVPYPTMNFG
HISGGDAANR ICACCELHMD IRPLPGMTLD NINELLHDAL APVSQRWPGR LSIDELHPPI
PGYECPTDHH MVAVIEKLLG SRTEVVNYCT EAPFVQEVCP TLVLGPGSIN QAHQPDEYID
TAFIEPTRKL LGQLVDHFCQ SISPD
//
