(data stored in ACNUC7421 zone)

SWISSPROT: Q4ZZU6_PSEU2

ID   Q4ZZU6_PSEU2            Unreviewed;       395 AA.
AC   Q4ZZU6;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 98.
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_0253 {ECO:0000313|EMBL:AAY35326.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35326.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35326.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35326.1,
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; AAY35326.1; -; Genomic_DNA.
DR   RefSeq; WP_011266278.1; NC_007005.1.
DR   RefSeq; YP_233364.1; NC_007005.1.
DR   STRING; 205918.Psyr_0253; -.
DR   MEROPS; M20.974; -.
DR   EnsemblBacteria; AAY35326; AAY35326; Psyr_0253.
DR   GeneID; 3365729; -.
DR   KEGG; psb:Psyr_0253; -.
DR   PATRIC; fig|205918.7.peg.252; -.
DR   eggNOG; ENOG4105CWC; Bacteria.
DR   eggNOG; COG0624; LUCA.
DR   HOGENOM; HOG000243769; -.
DR   KO; K01438; -.
DR   OMA; YIVGEPT; -.
DR   BioCyc; PSYR205918:G1G4J-254-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   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; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4ZZU6.
DR   SWISS-2DPAGE; Q4ZZU6.
KW   Amino-acid biosynthesis {ECO:0000256|SAAS:SAAS00756253};
KW   Arginine biosynthesis {ECO:0000256|SAAS:SAAS00756254};
KW   Cobalt {ECO:0000256|SAAS:SAAS00756242};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00786827,
KW   ECO:0000313|EMBL:AAY35326.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00786925};
KW   Zinc {ECO:0000256|SAAS:SAAS00756243}.
FT   DOMAIN      188    295       M20_dimer. {ECO:0000259|Pfam:PF07687}.
SQ   SEQUENCE   395 AA;  42824 MW;  437CF34CC20B7631 CRC64;
     MMGRVPSRLQ EASMPLPSMK DQFAALIAVP SVSCTQPSLD QSNRPVIDLL AGWLGDLGFA
     CDIQQVSPGK FNLLATYGTG PGGLVLAGHS DTVPFDEALW KTDPLKLTEV DGRWVGLGSC
     DMKGFFALVI EAVRGLLDQP FKQPLLILAT CDEESSMAGA RALADAGRPL GRAAVIGEPT
     GLKPIRLHKG VMMERIDILG RSGHSSDPSL GHSALEAMHD AISELKGLRT QWQAKYRNPQ
     FTVPQPTLNL GCIHGGDNPN RICGQCSLEF DLRPLPGMDP EMLRSAIRQK LQPLAELHQV
     QIDYAPLFPE CAPFEQIADA ELVRVAERLT GHTAAAVAFG TEAPYLQRLG CETLVLGPGD
     IACAHQPGEY LEMSRLDPTV RLLRQLIEHY CLTPQ
//

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