ID   ACMB_GORST              Reviewed;         401 AA.
AC   A1IHE7;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Methyl acetate hydrolase {ECO:0000303|PubMed:17071761};
DE            EC=3.1.1.114 {ECO:0000269|PubMed:17071761};
GN   Name=acmB {ECO:0000303|PubMed:17071761};
OS   Gordonia sp. (strain TY-5).
OC   Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia.
OX   NCBI_TaxID=235467;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-33, FUNCTION,
RP   CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=TY-5;
RX   PubMed=17071761; DOI=10.1128/jb.01054-06;
RA   Kotani T., Yurimoto H., Kato N., Sakai Y.;
RT   "Novel acetone metabolism in a propane-utilizing bacterium, Gordonia sp.
RT   strain TY-5.";
RL   J. Bacteriol. 189:886-893(2007).
CC   -!- FUNCTION: Plays an important role in the metabolism of acetone derived
CC       from propane oxidation (PubMed:17071761). Catalyzes the hydrolysis of
CC       methyl acetate to acetate and methanol (PubMed:17071761).
CC       {ECO:0000269|PubMed:17071761}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + methyl acetate = acetate + H(+) + methanol;
CC         Xref=Rhea:RHEA:60440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17790, ChEBI:CHEBI:30089, ChEBI:CHEBI:77700;
CC         EC=3.1.1.114; Evidence={ECO:0000269|PubMed:17071761};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60441;
CC         Evidence={ECO:0000269|PubMed:17071761};
CC   -!- INDUCTION: Induced by propane, 2-propanol and acetone.
CC       {ECO:0000269|PubMed:17071761}.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; AB252677; BAF43792.1; -; Genomic_DNA.
DR   SMR; A1IHE7; -.
DR   MEROPS; S12.950; -.
DR   KEGG; ag:BAF43792; -.
DR   BioCyc; MetaCyc:MON-19815; -.
DR   BRENDA; 3.1.1.114; 14626.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:17071761"
FT   CHAIN           2..401
FT                   /note="Methyl acetate hydrolase"
FT                   /id="PRO_0000453643"
FT   ACT_SITE        71
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:B6H6L7"
FT   ACT_SITE        74
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:B6H6L7"
FT   ACT_SITE        182
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:B6H6L7"
SQ   SEQUENCE   401 AA;  43457 MW;  9DF2B5F633B98657 CRC64;
     MTSTFSSLDV SAFTSAADRI LAEAVTGDAR VPGVVAMVTD RDRTVYSGAA GQRSLGGSAP
     MTTDDVFAIF STTKAITATA ALQLVEEGLL DLDAPASTYA PAIGTLQVIE GFDDAGEPIL
     RAPKSVPTTR QLLTHTGGFG YDFFDEIYNR LAEEKGQPSV TTASRAALMT PLLFDPGERW
     QYGTNIDWVG QVVEGLRGKR LGEVFAERIF APLGIENMSF ILREDFRSHL TEIHARNADG
     SLTPMGLELP SPPEVDFGGH GLYGTVGEYM KFIRMWLNDG VGEGGRVLKA ETVEMALRNH
     LGDLPVTMLP GVIPSLSNDA EFFPGQSKSW SLPFMINNET APTGRPAGAQ GWAGLANLFY
     WIDRQNGYGG YWATQILPFG DPTSFTKYME FETAFYDALK S