ID   A0A229TGQ8_9PSEU        Unreviewed;       350 AA.
AC   A0A229TGQ8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Alpha/beta hydrolase {ECO:0000313|EMBL:OXM70435.1};
GN   ORFNames=CF165_04990 {ECO:0000313|EMBL:OXM70435.1};
OS   Amycolatopsis vastitatis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1905142 {ECO:0000313|EMBL:OXM70435.1, ECO:0000313|Proteomes:UP000215199};
RN   [1] {ECO:0000313|Proteomes:UP000215199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H5 {ECO:0000313|Proteomes:UP000215199};
RA   Adamek M., Alanjary M., Sales-Ortells H., Goodfellow M., Bull A.T.,
RA   Kalinowski J., Ziemert N.;
RT   "Comparative genome mining reveals phylogenetic distribution patterns of
RT   secondary metabolites in Amycolatopsis.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXM70435.1}.
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DR   EMBL; NMUL01000005; OXM70435.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A229TGQ8; -.
DR   OrthoDB; 3206739at2; -.
DR   Proteomes; UP000215199; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR   PANTHER; PTHR23025:SF3; HORMONE-SENSITIVE LIPASE; 1.
DR   PANTHER; PTHR23025; TRIACYLGLYCEROL LIPASE; 1.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OXM70435.1};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}.
FT   DOMAIN          116..322
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
SQ   SEQUENCE   350 AA;  37836 MW;  76C474CDB0A0849C CRC64;
     MAIPLPTRVQ AAASQLAFWL PTPVRRAVAG RPVRIDGQDL ALDAQLLLRL QKIARAELVR
     GSVERSRALL DEARHLVSGR PIEPVSVREI AVPTPDGELP ATLYTPVGLP EKSPLLVFFH
     GGGWVIGTRA SHDNAVRFLA KHAGVRVLSI EYRLAPEFPF PAATEDALAA FEYAVAKASD
     LGADPARIAV GGDSAGGNLA AVTAQQAVRR GGPAPAFQLL IYPATDFARR YRSQDLFAED
     LFLTDVHMKW FEGHYVPEGS DLTDPRLSPL HADTLDGLPP ALIVTAGFDP LRDEGEAYAR
     KLADAGVDVT LRRHEDLIHG FINFTGVGTR FREALAEMAG ALRQGLSKRD
//