(data stored in SCRATCH zone)

SWISSPROT: Q500E9_PSEU2

ID   Q500E9_PSEU2            Unreviewed;       385 AA.
AC   Q500E9;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 94.
DE   RecName: Full=Acetylornithine deacetylase {ECO:0000256|SAAS:SAAS00756257};
DE            EC=3.5.1.- {ECO:0000256|SAAS:SAAS00787082};
DE            EC=3.5.1.16 {ECO:0000256|SAAS:SAAS00756259};
GN   OrderedLocusNames=Psyr_0150 {ECO:0000313|EMBL:AAY35223.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35223.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35223.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35223.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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|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;
CC         Evidence={ECO:0000256|SAAS:SAAS00756246};
CC   -!- COFACTOR:
CC       Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC         Evidence={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|SAAS:SAAS00756240}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|SAAS:SAAS00756245}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
CC       {ECO:0000256|SAAS:SAAS00756241}.
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DR   EMBL; CP000075; AAY35223.1; -; Genomic_DNA.
DR   RefSeq; WP_011266226.1; NC_007005.1.
DR   RefSeq; YP_233261.1; NC_007005.1.
DR   STRING; 205918.Psyr_0150; -.
DR   MEROPS; M20.974; -.
DR   EnsemblBacteria; AAY35223; AAY35223; Psyr_0150.
DR   GeneID; 3365626; -.
DR   KEGG; psb:Psyr_0150; -.
DR   PATRIC; fig|205918.7.peg.147; -.
DR   eggNOG; ENOG4107RK1; Bacteria.
DR   eggNOG; COG0624; LUCA.
DR   HOGENOM; HOG000243772; -.
DR   KO; K01438; -.
DR   OMA; GSIHVAH; -.
DR   BioCyc; PSYR205918:G1G4J-151-MONOMER; -.
DR   UniPathway; UPA00068; UER00110.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03894; M20_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   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; Q500E9.
DR   SWISS-2DPAGE; Q500E9.
KW   Amino-acid biosynthesis {ECO:0000256|SAAS:SAAS00756253};
KW   Arginine biosynthesis {ECO:0000256|SAAS:SAAS00756254};
KW   Cobalt {ECO:0000256|SAAS:SAAS00756242};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00786827};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00786925};
KW   Zinc {ECO:0000256|SAAS:SAAS00756243}.
FT   DOMAIN      171    280       M20_dimer. {ECO:0000259|Pfam:PF07687}.
FT   COILED      270    290       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   385 AA;  42048 MW;  FA2FD33D20E2FF1A CRC64;
     MSPRALEILK RLIAFDTVSS EPNMALIEYV RELLASKGIE SLIVKDETGK KANLFASTGP
     REVPGVLLSG HTDVVPAAGQ AWTMPPFQAT LRDGRIYGRG TCDMKGFIAL AIDAMLDAAD
     MPLTRPLQLA LSHDEEIGCV GVRRLLDVLH LAPVRPFLCV VGEPTLMQFA VGHKGKASYR
     TFCRGQEAHS SLAPRAVNAI HLASDFIAEL RKSQKQIEQQ GARDEGYDIP YSTVHIGRID
     GGKALNIVPN LCTLEFEYRN LPGDNPDALL EQLRERAEVL VREARQLSGV ADIEIEVMNE
     YPALETHPSV EAVRLLHAFA EPGTQHIKVS YGTEGGLFAG RLNVPVVVCG PGSIEQAHKP
     DEFIDESQMD AGERFLQSLL GSLKQ
//

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