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
//