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ARGE_VIBC1
ID   ARGE_VIBC1              Reviewed;         378 AA.
AC   A7MXC2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Acetylornithine deacetylase {ECO:0000255|HAMAP-Rule:MF_01108};
DE            Short=AO {ECO:0000255|HAMAP-Rule:MF_01108};
DE            Short=Acetylornithinase {ECO:0000255|HAMAP-Rule:MF_01108};
DE            EC=3.5.1.16 {ECO:0000255|HAMAP-Rule:MF_01108};
DE   AltName: Full=N-acetylornithinase {ECO:0000255|HAMAP-Rule:MF_01108};
DE            Short=NAO {ECO:0000255|HAMAP-Rule:MF_01108};
GN   Name=argE {ECO:0000255|HAMAP-Rule:MF_01108};
GN   OrderedLocusNames=VIBHAR_00044;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of the amide bond of N(2)-acetylated
CC       L-amino acids. Cleaves the acetyl group from N-acetyl-L-ornithine to
CC       form L-ornithine, an intermediate in L-arginine biosynthesis pathway,
CC       and a branchpoint in the synthesis of polyamines. {ECO:0000255|HAMAP-
CC       Rule:MF_01108}.
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:0000255|HAMAP-Rule:MF_01108};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01108};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01108};
CC       Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01108};
CC   -!- COFACTOR:
CC       Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01108};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine
CC       from N(2)-acetyl-L-ornithine (linear): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01108}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01108}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01108}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01108}.
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DR   EMBL; CP000789; ABU69104.1; -; Genomic_DNA.
DR   RefSeq; WP_012126444.1; NC_022269.1.
DR   AlphaFoldDB; A7MXC2; -.
DR   SMR; A7MXC2; -.
DR   EnsemblBacteria; ABU69104; ABU69104; VIBHAR_00044.
DR   KEGG; vha:VIBHAR_00044; -.
DR   PATRIC; fig|338187.25.peg.2479; -.
DR   OMA; CAHQPGE; -.
DR   OrthoDB; 906744at2; -.
DR   UniPathway; UPA00068; UER00110.
DR   Proteomes; UP000008152; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cobalt; Cytoplasm;
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..378
FT                   /note="Acetylornithine deacetylase"
FT                   /id="PRO_1000065066"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
FT   BINDING         351
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01108"
SQ   SEQUENCE   378 AA;  41846 MW;  FD6E922EEB862DB5 CRC64;
     MQLPSFLEVY EGLISTSSIS STDPSWDQGN AKVIEKLASW FKDLGFSVEV IEVEPGKHNM
     IARMGEGEGG LLLAGHSDTV PFDEGRWSFD PHKLTEKDNR FYGLGTADMK GFFAFIYEAV
     KKIDWSKQTK PLYVLATCDE ETTMLGARHF TENAPFKPDY CIIGEPTSLV PIRGHKGHVA
     NAIRVTGKSG HSSDPALGVN AIEIMHEVMF AMMQLRDKLV KEYHHPGFAI PSPTLNLGHI
     HGGDSANRIC GCCELHYDVR PLPGISLDGL ENMLRGALKE VEAKWPGRLE IIPLHDPIPG
     YECQHDHPFI GGVEEICQTS SETVNYCTEA PFLQQLCPTL VLGPGSIDQA HQPDEFLSFD
     FIDPTIDVLS RAMVKYCC
 
 
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