DEACT_BRUA4
ID DEACT_BRUA4 Reviewed; 402 AA.
AC A6X391;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Deacetylase Oant_2987;
DE EC=3.1.1.-;
GN OrderedLocusNames=Oant_2987;
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(2011).
RN [2]
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND LACK OF
RP AMINOHYDROLASE ACTIVITY.
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=23214420; DOI=10.1021/bi301483z;
RA Ornelas A., Korczynska M., Ragumani S., Kumaran D., Narindoshvili T.,
RA Shoichet B.K., Swaminathan S., Raushel F.M.;
RT "Functional annotation and three-dimensional structure of an incorrectly
RT annotated dihydroorotase from cog3964 in the amidohydrolase superfamily.";
RL Biochemistry 52:228-238(2013).
CC -!- FUNCTION: Esterase that catalyzes the deacetylation of acetyl-(R)-
CC mandelate (in vitro). Can also hydrolyze acetyl glycolate, but with
CC lower efficiency. Has very low N-acetyl-D-amino acid deacetylase
CC activity with N-acetyl-D-serine and N-acetyl-D-threonine (in vitro).
CC Theoretical substrate docking studies suggest that other N-acetylated
CC amino acids may optimally occupy the active site and may in fact be the
CC physiological substrates. {ECO:0000269|PubMed:23214420}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250, ECO:0000269|PubMed:23214420};
CC Note=Binds 2 zinc ions per subunit. After heterologous expression, a
CC stoichiometry of 1 zinc ion per subunit is observed. {ECO:0000250,
CC ECO:0000269|PubMed:23214420};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for acetyl-(R)-mandelate {ECO:0000269|PubMed:23214420};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Atu3266/EF_0837 deacetylase family. {ECO:0000305}.
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DR EMBL; CP000759; ABS15695.1; -; Genomic_DNA.
DR RefSeq; WP_011982716.1; NC_009668.1.
DR AlphaFoldDB; A6X391; -.
DR SMR; A6X391; -.
DR STRING; 439375.Oant_2987; -.
DR EnsemblBacteria; ABS15695; ABS15695; Oant_2987.
DR KEGG; oan:Oant_2987; -.
DR PATRIC; fig|439375.7.peg.3138; -.
DR eggNOG; COG3964; Bacteria.
DR HOGENOM; CLU_036699_2_0_5; -.
DR OMA; IGNNPPN; -.
DR OrthoDB; 1319925at2; -.
DR Proteomes; UP000002301; Chromosome 2.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:CACAO.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR020043; Deacetylase_Atu3266-like.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR42717; PTHR42717; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF039004; ADE_EF_0837; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..402
FT /note="Deacetylase Oant_2987"
FT /id="PRO_0000429020"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT SITE 170
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 168
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 402 AA; 43606 MW; 1D0DD823BAF2AB67 CRC64;
MISGEQAKPL LITNVKPVAF GVEHSDATTD ILVGKDGSIS AIGKSLNAPA DVERVDGKGA
WISPGWVDLH VHIWHGGTDI SIRPSECGAE RGVTTLVDAG SAGEANFHGF REYIIEPSKE
RIKAFLNLGS IGLVACNRVP ELRDIKDIDL DRILECYAAN SEHIVGIKVR ASHVITGSWG
VTPVKLGKKI AKILKVPMMV HVGEPPALYD EVLEILGPGD VVTHCFNGKS GSSIMEDEDL
FNLAERCSGE GIRLDIGHGG ASFSFKVAEA AIERGLLPFS ISTDLHGHSM NFPVWDLATT
MSKLLSVNMP FENVIEAVTH NPASVIKLSM ENRLSVGQRA DFTIFDLVDA DLEATDSNGD
VSRLNRLFEP RYAVIGAEAI TASRYIPRAR KLVRHSHGYS WR
