ID   BAH_STRHY               Reviewed;         299 AA.
AC   Q01109;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 3.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Acetyl-hydrolase;
DE            EC=3.1.1.-;
GN   Name=bah;
OS   Streptomyces hygroscopicus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=1912;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21705 / DSM 41527 / SF-1293;
RX   PubMed=2066341; DOI=10.1128/jb.173.14.4454-4463.1991;
RA   Raibaud A., Zalacain M., Holt T.G., Tizard R., Thompson C.J.;
RT   "Nucleotide sequence analysis reveals linked N-acetyl hydrolase,
RT   thioesterase, transport, and regulatory genes encoded by the bialaphos
RT   biosynthetic gene cluster of Streptomyces hygroscopicus.";
RL   J. Bacteriol. 173:4454-4463(1991).
CC   -!- FUNCTION: This protein removes the N-acetyl group from bialaphos as one
CC       of the final steps of the bialaphos biosynthetic pathway.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; bialaphos biosynthesis.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; M64783; AAA79277.1; -; Genomic_DNA.
DR   PIR; A47031; A47031.
DR   AlphaFoldDB; Q01109; -.
DR   SMR; Q01109; -.
DR   ESTHER; strhy-bahli; Hormone-sensitive_lipase_like.
DR   BioCyc; MetaCyc:MON-15055; -.
DR   UniPathway; UPA00197; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR   InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR   PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Hydrolase.
FT   CHAIN           1..299
FT                   /note="Acetyl-hydrolase"
FT                   /id="PRO_0000071553"
FT   MOTIF           73..75
FT                   /note="Involved in the stabilization of the negatively
FT                   charged intermediate by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000250|UniProtKB:O06350,
FT                   ECO:0000255|PROSITE-ProRule:PRU10038"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000250|UniProtKB:O06350"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000250|UniProtKB:O06350"
SQ   SEQUENCE   299 AA;  32096 MW;  4265C8E6E10FAE97 CRC64;
     MASPELELVR ELIELNWHTR NGEVEPRRIA YDRAQEAFGN LGVPPGDVVT VGHCTAEWVR
     PARQDGRTLL YLHGGSYALG SPQSHRHLSS ALGDAAGAAV LALHYRRPPE SPFPAAVEDA
     VAAYRMLLEQ GCPPGRVTLA GDSAGAGLAV AALQALRDAG TPLPAAAVCI SPWADLACEG
     ASHTTRKARE ILLDTADLRR MAERYLAGTD PRHPLASPAH GDLTGLPPLL IQVGSEEVLH
     DDARALEQAA LKAGTPVTFE EWPEMFHVWH WYHPVLPEGR RAIEVAGAFL RTATGEGLK