(data stored in ACNUC7421 zone)

SWISSPROT: A0KFU9_AERHH

ID   A0KFU9_AERHH            Unreviewed;       381 AA.
AC   A0KFU9;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 95.
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   Name=argE {ECO:0000313|EMBL:ABK38365.1};
GN   OrderedLocusNames=AHA_0592 {ECO:0000313|EMBL:ABK38365.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK38365.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK38365.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(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|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; CP000462; ABK38365.1; -; Genomic_DNA.
DR   RefSeq; WP_011704559.1; NC_008570.1.
DR   RefSeq; YP_855125.1; NC_008570.1.
DR   STRING; 380703.AHA_0592; -.
DR   MEROPS; M20.974; -.
DR   EnsemblBacteria; ABK38365; ABK38365; AHA_0592.
DR   GeneID; 4489259; -.
DR   KEGG; aha:AHA_0592; -.
DR   PATRIC; fig|380703.7.peg.588; -.
DR   eggNOG; ENOG4105CWC; Bacteria.
DR   eggNOG; COG0624; LUCA.
DR   HOGENOM; HOG000243769; -.
DR   KO; K01438; -.
DR   OMA; FPEVPPF; -.
DR   BioCyc; AHYD380703:G1G7B-593-MONOMER; -.
DR   UniPathway; UPA00068; UER00110.
DR   Proteomes; UP000000756; 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; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KFU9.
DR   SWISS-2DPAGE; A0KFU9.
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:UP000000756};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00786827,
KW   ECO:0000313|EMBL:ABK38365.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00786925};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Zinc {ECO:0000256|SAAS:SAAS00756243}.
FT   DOMAIN      175    282       M20_dimer. {ECO:0000259|Pfam:PF07687}.
SQ   SEQUENCE   381 AA;  41617 MW;  682EAACC1ABD1D47 CRC64;
     MANLDFFSLY KNIIAIPSIS STDPRWDQSN EAVIRLLADW FGQLGFQCEV TALPDLPGKF
     NLVATIGQGE GGLLLAGHTD TVPFDEGAWR KDPFKVTEEG NRLYGLGTID MKGFFAFIVE
     ALKEIDLKTL SKPLRILATA DEETTMAGAR AIAAAAELKP DYAVIGEPTG LVPVVAHKGH
     MSEAIRITGR SGHSSDPANG VNALEIMHQA MGQVLKLQHS LKEKYADHRF AVPQPTLNLG
     YIQGGDSPNR ICGCCELHID MRPTPQVGPD ELMGMLKEAL SPIEIHQPGC LHLQHLHEPI
     PAYACADDSE LVREAERASG RAAESVNYCT EAPFIQQLGC ETIVLGPGHI AQAHQPDEYL
     DLSFVKPTTR VLQHLIRRFC L
//

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