Y130_ARCFU
ID Y130_ARCFU Reviewed; 359 AA.
AC O30107;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable deacetylase AF_0130 {ECO:0000305};
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q48935};
GN OrderedLocusNames=AF_0130;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
CC -!- FUNCTION: Probable deacetylase. {ECO:0000250|UniProtKB:Q48935}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q48935};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q48935};
CC -!- SIMILARITY: Belongs to the histone deacetylase family. {ECO:0000305}.
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DR EMBL; AE000782; AAB91099.1; -; Genomic_DNA.
DR PIR; B69266; B69266.
DR RefSeq; WP_010877642.1; NC_000917.1.
DR AlphaFoldDB; O30107; -.
DR SMR; O30107; -.
DR STRING; 224325.AF_0130; -.
DR EnsemblBacteria; AAB91099; AAB91099; AF_0130.
DR GeneID; 24793683; -.
DR KEGG; afu:AF_0130; -.
DR eggNOG; arCOG00324; Archaea.
DR HOGENOM; CLU_007727_8_2_2; -.
DR OMA; CFWHSTG; -.
DR OrthoDB; 34461at2157; -.
DR PhylomeDB; O30107; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR003084; His_deacetylse_1.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; SSF52768; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..359
FT /note="Probable deacetylase AF_0130"
FT /id="PRO_0000114744"
FT ACT_SITE 126
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT SITE 293
FT /note="Polarizes the scissile carbonyl of the substrate"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
SQ SEQUENCE 359 AA; 40468 MW; CEC0D294311157AC CRC64;
MVTGIVFHEE YLKHEQSPTH PERRERLAYT MDQLREEGIF ESERIVLLEP FKASLEDVLE
VHTEEYVRFL EMESKKGGII DFDTNIPVGV FDRALLAAGG AIRAAQAVLN KECENAFAMI
RPPGHHAKPY IGAGFCYLNN MAIMVKWLLK QGFERIAILD WDAHHGDGTQ EIFYNDDRVL
FISTHQMPLY PGTGYPEECG TGKGEGYTVN IPLPPGTGDE GYMMVIDEII EPVVNEFKPQ
FIAISAGQDN HFTDPITSLA LTARGYAEMM RRAVAMAEKH CDGRLVAVLE GGYSVEGALP
YTNLGIIAAM AGFDLSAIRE PENYLPELLW RKRDSALVKL KHNIEDVKRV HSKYWKCFK