(data stored in ACNUC7421 zone)

SWISSPROT: Q2ING1_ANADE

ID   Q2ING1_ANADE            Unreviewed;       371 AA.
AC   Q2ING1;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 97.
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=Adeh_0568 {ECO:0000313|EMBL:ABC80344.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80344.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|EMBL:ABC80344.1, ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|EMBL:ABC80344.1,
RC   ECO:0000313|Proteomes:UP000001935};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000251; ABC80344.1; -; Genomic_DNA.
DR   RefSeq; WP_011419627.1; NC_007760.1.
DR   STRING; 290397.Adeh_0568; -.
DR   MEROPS; M20.974; -.
DR   EnsemblBacteria; ABC80344; ABC80344; Adeh_0568.
DR   KEGG; ade:Adeh_0568; -.
DR   eggNOG; ENOG4105C9Y; Bacteria.
DR   eggNOG; COG0624; LUCA.
DR   HOGENOM; HOG000243772; -.
DR   KO; K01438; -.
DR   OMA; FPEVPPF; -.
DR   BioCyc; ADEH290397:G1G5W-584-MONOMER; -.
DR   UniPathway; UPA00068; UER00110.
DR   Proteomes; UP000001935; 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; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2ING1.
DR   SWISS-2DPAGE; Q2ING1.
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:UP000001935};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00786827,
KW   ECO:0000313|EMBL:ABC80344.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00786925};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Zinc {ECO:0000256|SAAS:SAAS00756243}.
FT   DOMAIN      166    274       M20_dimer. {ECO:0000259|Pfam:PF07687}.
SQ   SEQUENCE   371 AA;  39083 MW;  1C62BB4FEB4A3C3A CRC64;
     MDLVPLLRSL VALDTTSART NLPALDLLER EAHAAGFATR RQRWTDAAGV EKGNLVCRRG
     PDVPGGLALV GHTDCVPFDP EWKEALSGEL VDGRLVGRGS ADTKAFLAAA LTAARAAAPG
     RLPLTLVFTA DEEIGCLGAK KLLAEGALHP AHAIVGEPTR LTPIRAHKGY CAVEVVVSGI
     EGHSAYPEVG ASAIHHVGRL WPELEAIGAD LTRETDQAFS PPYTTWNVGV IRGGKARNII
     AGECRFTFEW RPLPGHDPKR ALRLLEDACA RLAAASGGKV AVKVIPLRTD AAAVTPPGAE
     IVRFLEAESG NPAATVPFGT ELPELIGMGA EACVFGPGDI REAHRTGESV PLDQVERTVT
     ILGNAIARFC A
//

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