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Database: UniProt
Entry: A0A167WS45_9BURK
LinkDB: A0A167WS45_9BURK
Original site: A0A167WS45_9BURK 
ID   A0A167WS45_9BURK        Unreviewed;       401 AA.
AC   A0A167WS45;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Acylhydrolase {ECO:0000313|EMBL:ANB78099.1};
GN   ORFNames=AYM40_37425 {ECO:0000313|EMBL:ANB78099.1};
OS   Paraburkholderia phytofirmans OLGA172.
OG   Plasmid polga2 {ECO:0000313|Proteomes:UP000076852}.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB78099.1, ECO:0000313|Proteomes:UP000076852};
RN   [1] {ECO:0000313|EMBL:ANB78099.1, ECO:0000313|Proteomes:UP000076852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLGA172 {ECO:0000313|EMBL:ANB78099.1,
RC   ECO:0000313|Proteomes:UP000076852};
RC   PLASMID=polga2 {ECO:0000313|Proteomes:UP000076852};
RX   PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA   Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT   "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT   chlorocatechol degradative operon in a region of genome plasticity.";
RL   Gene 586:239-247(2016).
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DR   EMBL; CP014581; ANB78099.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167WS45; -.
DR   KEGG; buz:AYM40_37425; -.
DR   Proteomes; UP000076852; Plasmid polga2.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   CDD; cd01847; Triacylglycerol_lipase_like; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   InterPro; IPR020610; Thiolase_AS.
DR   PANTHER; PTHR45648; GDSL LIPASE/ACYLHYDROLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_4G14700); 1.
DR   PANTHER; PTHR45648:SF22; GDSL LIPASE/ACYLHYDROLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_4G14700); 1.
DR   Pfam; PF00657; Lipase_GDSL; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ANB78099.1};
KW   Plasmid {ECO:0000313|EMBL:ANB78099.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076852};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..401
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007894087"
SQ   SEQUENCE   401 AA;  40241 MW;  469DEE6654633A20 CRC64;
     MQTGSDRNTL ARFAQLAIAG AAFAMLAACG GGGGGSSNTS SANTSTPTGG VNLQVVSFGD
     SLSDVGTYAP VITASFGGGR FTTNPGEVWT QKVAEYYGGT LSAAYLGGFG QPLAASTGLG
     YAQGGARVQD PVGEGHAPVG TANADYSAAT TVPVTQQLQN YLAAHGSFNA NQLVLINGGA
     NDIFELESTI QAAVAADVAG GMDPATAIQN EATASLGPVA QTFAGVIQQI VAAGASHVVV
     SNVPDIGQTP LGVTGGSSAQ QLLTALSSVY NAALTQAIQG LGLPASKVIQ IDAFSWQDGI
     NASYQTNGFT VSNTGTACNL QSMAANATAY GTQNPSVLNG LTPAQYGASF ASALFCSPQT
     YTVAGADQTY MFADNVHPST HLHALFAQYV EQQVAKSGLG K
//
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