(data stored in SCRATCH zone)

SWISSPROT: D3VH70_XENNA

ID   D3VH70_XENNA            Unreviewed;       385 AA.
AC   D3VH70;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=Acetylornithine deacetylase {ECO:0000256|HAMAP-Rule:MF_01108};
DE            Short=AO {ECO:0000256|HAMAP-Rule:MF_01108};
DE            Short=Acetylornithinase {ECO:0000256|HAMAP-Rule:MF_01108};
DE            EC=3.5.1.16 {ECO:0000256|HAMAP-Rule:MF_01108};
DE   AltName: Full=N-acetylornithinase {ECO:0000256|HAMAP-Rule:MF_01108};
DE            Short=NAO {ECO:0000256|HAMAP-Rule:MF_01108};
GN   Name=argE {ECO:0000256|HAMAP-Rule:MF_01108,
GN   ECO:0000313|EMBL:CBJ88355.1};
GN   OrderedLocusNames=XNC1_0267 {ECO:0000313|EMBL:CBJ88355.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88355.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88355.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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|HAMAP-Rule:MF_01108,
CC         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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01108};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01108};
CC       Note=Binds 2 Zn(2+) or Co(2+) ions per subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_01108};
CC   -!- COFACTOR:
CC       Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01108,
CC         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|HAMAP-Rule:MF_01108, ECO:0000256|SAAS:SAAS00756240}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01108,
CC       ECO:0000256|SAAS:SAAS00756245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01108}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01108, ECO:0000256|SAAS:SAAS00756241}.
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DR   EMBL; FN667742; CBJ88355.1; -; Genomic_DNA.
DR   RefSeq; WP_013183205.1; NC_014228.1.
DR   STRING; 406817.XNC1_0267; -.
DR   MEROPS; M20.974; -.
DR   EnsemblBacteria; CBJ88355; CBJ88355; XNC1_0267.
DR   KEGG; xne:XNC1_0267; -.
DR   eggNOG; ENOG4105CWC; Bacteria.
DR   eggNOG; COG0624; LUCA.
DR   HOGENOM; HOG000243769; -.
DR   KO; K01438; -.
DR   OMA; FPEVPPF; -.
DR   UniPathway; UPA00068; UER00110.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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; D3VH70.
DR   SWISS-2DPAGE; D3VH70.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01108,
KW   ECO:0000256|SAAS:SAAS00756253};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01108,
KW   ECO:0000256|SAAS:SAAS00756254};
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_01108,
KW   ECO:0000256|SAAS:SAAS00756242};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01108};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01108,
KW   ECO:0000256|SAAS:SAAS00786827, ECO:0000313|EMBL:CBJ88355.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01108,
KW   ECO:0000256|SAAS:SAAS00786925};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01108, ECO:0000256|SAAS:SAAS00756243}.
FT   DOMAIN      178    288       M20_dimer. {ECO:0000259|Pfam:PF07687}.
FT   ACT_SITE     82     82       {ECO:0000256|HAMAP-Rule:MF_01108}.
FT   ACT_SITE    144    144       {ECO:0000256|HAMAP-Rule:MF_01108}.
FT   METAL        80     80       Cobalt or zinc 1. {ECO:0000256|HAMAP-
FT                                Rule:MF_01108}.
FT   METAL       112    112       Cobalt or zinc 1. {ECO:0000256|HAMAP-
FT                                Rule:MF_01108}.
FT   METAL       112    112       Cobalt or zinc 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_01108}.
FT   METAL       145    145       Cobalt or zinc 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_01108}.
FT   METAL       169    169       Cobalt or zinc 1. {ECO:0000256|HAMAP-
FT                                Rule:MF_01108}.
FT   METAL       355    355       Cobalt or zinc 2. {ECO:0000256|HAMAP-
FT                                Rule:MF_01108}.
SQ   SEQUENCE   385 AA;  42262 MW;  83D79DF9C6D9EFFC CRC64;
     MNIKLPSFIK LYHQLIAAPS ISANDAELDQ SNEVVINLLA EWLKEIGFTI EIQPVPATRG
     KFNLLATLGE GTGGVLLCGH TDTVPFDDGR WTQDPFTLTE RDGKLYGLGT ADMKGFFAFI
     IDAVRDIDTS KLSHPLYILA TADEETSMAG ARYFAANTNI RPDFAIIGEP TSLQPIRAHK
     GHLSQAIRIE GKSGHSSDPA RGVNAIDLMH ESITQLMELR NTLQERYHNP AFVIPYPTMN
     FGHIHGGDAA NRICACCELH MDIRPLPGLS LQDLDGLLND ALEPVKQRWP GRLSVTELHP
     PIPGYECPTD HKLVGVIEKL LGTKADTVNY CTEAPFIQAL CPTLVLGPGS IEQAHQPDEF
     LDMAFIEPTR KLLSQLVAHF CLEAG
//

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