(data stored in SCRATCH zone)

SWISSPROT: E6V2C2_VARPE

ID   E6V2C2_VARPE            Unreviewed;       388 AA.
AC   E6V2C2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=Acetylornithine deacetylase {ECO:0000256|SAAS:SAAS00756257};
DE            EC=3.5.1.16 {ECO:0000256|SAAS:SAAS00756259};
GN   OrderedLocusNames=Varpa_0331 {ECO:0000313|EMBL:ADU34553.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34553.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34553.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34553.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
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; CP002417; ADU34553.1; -; Genomic_DNA.
DR   RefSeq; WP_013538799.1; NC_014931.1.
DR   STRING; 595537.Varpa_0331; -.
DR   MEROPS; M20.974; -.
DR   EnsemblBacteria; ADU34553; ADU34553; Varpa_0331.
DR   GeneID; 29714430; -.
DR   KEGG; vpe:Varpa_0331; -.
DR   eggNOG; ENOG4105CWC; Bacteria.
DR   eggNOG; COG0624; LUCA.
DR   HOGENOM; HOG000243772; -.
DR   KO; K01438; -.
DR   OMA; LVGHHDV; -.
DR   OrthoDB; 906744at2; -.
DR   BioCyc; VPAR595537:G1GQO-333-MONOMER; -.
DR   UniPathway; UPA00068; UER00110.
DR   Proteomes; UP000008917; 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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03894; M20_ArgE; 1.
DR   InterPro; IPR010169; AcOrn-deacetyl.
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.
PE   3: Inferred from homology;
DR   PRODOM; E6V2C2.
DR   SWISS-2DPAGE; E6V2C2.
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:UP000008917};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00756249};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00756255};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   Zinc {ECO:0000256|SAAS:SAAS00756243}.
FT   DOMAIN      175    284       M20_dimer. {ECO:0000259|Pfam:PF07687}.
SQ   SEQUENCE   388 AA;  42042 MW;  71908C5B3B609FD1 CRC64;
     MPHTLSPQSL ALAQSLVRMN TVSENSNLQL IDLAQSHLAA LGVKSRITYN AERTKANLFA
     TLGEGKPAGV IISGHTDTVP WDGQDWSVDP LSAVVQHERL YGRGSADMKS FIAIALSNAK
     RFLESDSPFA VHFAFSYEEE IGCFGVKELI ADMRDAGIKP LACIVGEPTS MVPAIAHKGV
     YRYKCCVRGK EAHSSLTPKS VNAIEMAARV IGKVRDMAED FERSEPRYEG FDVPFSTASV
     GQFHGGIADN VVPRDAEFRY EFRDLPTADA KRMQSDVLAY AAGLEPAMKK VAPDAGFKFE
     TICEIPSFLG AANDPVTLLA QRLAGEDRTT LVAFGTEAGL FKNAGIPTVV CGPGSIEQAH
     QPDEFVSLEQ LARCELFMER LATSHTIG
//

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