(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NTE7_YERPA

ID   A0A0E1NTE7_YERPA        Unreviewed;       387 AA.
AC   A0A0E1NTE7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   16-JAN-2019, entry version 32.
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   OrderedLocusNames=YPA_0096 {ECO:0000313|EMBL:ABG12065.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12065.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12065.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12065.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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         ECO:0000256|SAAS:SAAS01122628};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|SAAS:SAAS00756239};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01108};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01108};
CC       Note=Binds 2 Zn(2+) or Co(2+) ions per subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_01108};
CC   -!- COFACTOR:
CC       Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01108,
CC         ECO:0000256|SAAS:SAAS00756256};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       ornithine from N(2)-acetyl-L-ornithine (linear): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01108, ECO:0000256|SAAS:SAAS00756240}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01108,
CC       ECO:0000256|SAAS:SAAS00756245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01108}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01108, ECO:0000256|SAAS:SAAS00756241}.
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; CP000308; ABG12065.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABG12065; ABG12065; YPA_0096.
DR   EnsemblBacteria; AJJ78563; AJJ78563; CH58_2931.
DR   KEGG; ypa:YPA_0096; -.
DR   PATRIC; fig|360102.15.peg.3085; -.
DR   KO; K01438; -.
DR   OMA; FPEVPPF; -.
DR   UniPathway; UPA00068; UER00110.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
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   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;
DR   PRODOM; A0A0E1NTE7.
DR   SWISS-2DPAGE; A0A0E1NTE7.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01108,
KW   ECO:0000256|SAAS:SAAS00756253};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01108,
KW   ECO:0000256|SAAS:SAAS00756254};
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_01108,
KW   ECO:0000256|SAAS:SAAS00756242};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01108};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01108,
KW   ECO:0000256|SAAS:SAAS00786827, ECO:0000313|EMBL:ABG12065.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01108,
KW   ECO:0000256|SAAS:SAAS00786925};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01108, ECO:0000256|SAAS:SAAS00756243}.
FT   ACT_SITE     85     85       {ECO:0000256|HAMAP-Rule:MF_01108}.
FT   ACT_SITE    147    147       {ECO:0000256|HAMAP-Rule:MF_01108}.
FT   METAL        83     83       Cobalt or zinc 1. {ECO:0000256|HAMAP-
FT                                Rule:MF_01108}.
FT   METAL       115    115       Cobalt or zinc 1. {ECO:0000256|HAMAP-
FT                                Rule:MF_01108}.
FT   METAL       115    115       Cobalt or zinc 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_01108}.
FT   METAL       148    148       Cobalt or zinc 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_01108}.
FT   METAL       172    172       Cobalt or zinc 1. {ECO:0000256|HAMAP-
FT                                Rule:MF_01108}.
FT   METAL       358    358       Cobalt or zinc 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_01108}.
SQ   SEQUENCE   387 AA;  42690 MW;  9A4D12D3B69A43E8 CRC64;
     MKLPPFIELY RALIATPSIS AADSALDQSN EALINLLAGW FADLGFRVEI QPVPDTRHKF
     NLLASIGENE NGEGHGGLLL AGHTDTVPYD EGRWTRDPFT LTEHDHKLYG LGTADMKGFF
     AFILDAVRDI DASKLTKPLY ILATADEETT MAGARYFAAN TQLRPDFAII GEPTSLQPVR
     AHKGHISNAI RITGQSGHSS DPARGVNAID LMHESITQLM ALRTTLQERY HNPAFTIPYP
     TMNFGHINGG DAANRICACC ELHMDIRPLP GLTLSDLNEL MTEALEPVSQ RWPGRLSIDE
     LHPPIPGYEC PTDHHMVGVI EKLLGERTAV VNYCTEAPFI QQVCPTLVLG PGSINQAHQP
     DEFIDMAFIE PTRELIGQLV DHFCQQK
//

If you have problems or comments...

PBIL Back to PBIL home page