Y1194_METTH
ID Y1194_METTH Reviewed; 331 AA.
AC O27262;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable deacetylase MTH_1194 {ECO:0000305};
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q48935};
GN OrderedLocusNames=MTH_1194;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(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; AE000666; AAB85683.1; -; Genomic_DNA.
DR PIR; C69026; C69026.
DR RefSeq; WP_010876818.1; NC_000916.1.
DR AlphaFoldDB; O27262; -.
DR SMR; O27262; -.
DR STRING; 187420.MTH_1194; -.
DR EnsemblBacteria; AAB85683; AAB85683; MTH_1194.
DR GeneID; 1471602; -.
DR KEGG; mth:MTH_1194; -.
DR PATRIC; fig|187420.15.peg.1172; -.
DR HOGENOM; CLU_007727_8_0_2; -.
DR OMA; GRAMGFC; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR000286; His_deacetylse.
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 SUPFAM; SSF52768; SSF52768; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..331
FT /note="Probable deacetylase MTH_1194"
FT /id="PRO_0000114746"
FT ACT_SITE 118
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
FT SITE 283
FT /note="Polarizes the scissile carbonyl of the substrate"
FT /evidence="ECO:0000250|UniProtKB:Q48935"
SQ SEQUENCE 331 AA; 36722 MW; 489054F32965EDCF CRC64;
MVIIHSPSYD LHNHEGHVEN SGRTRAILRA IESSDLSPRF VEPGMAGIDD ILMVHSSTHV
EYLEVFAGRG GGWLDYDTYM TPESFSVARL SAGGAMLAAE EALRDGWSYS LGRPPGHHAT
YDRSMGFCIF NNIAIAIEHA RRNLGVSRPL VLDFDVHHGN GTSSIFYRDR DVMYISIHQD
PRTLFPGTGF IDETGSGEGE GFNLNIPMPR GSGNREYLWI LGMILPAVLE GFRPDMIFVS
AGFDAHRRDP LAEIMVDEEF FSWIGWFIHQ TGLPCTAVLE GGYDPEALGR SNIAFMRGLD
GEEYEPETAA PGGVSEIFSQ LSDRFSAYFN F