ID E3S5E0_PYRTT Unreviewed; 523 AA.
AC E3S5E0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Putative phospholipase {ECO:0000256|PIRNR:PIRNR018169};
DE EC=3.1.1.47 {ECO:0000256|PIRNR:PIRNR018169};
GN ORFNames=PTT_17842 {ECO:0000313|EMBL:EFQ86808.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ86808.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ86808.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC Evidence={ECO:0000256|PIRNR:PIRNR018169};
CC -!- SIMILARITY: Belongs to the serine esterase family.
CC {ECO:0000256|PIRNR:PIRNR018169}.
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DR EMBL; GL537232; EFQ86808.1; -; Genomic_DNA.
DR RefSeq; XP_003305095.1; XM_003305047.1.
DR AlphaFoldDB; E3S5E0; -.
DR STRING; 861557.E3S5E0; -.
DR EnsemblFungi; EFQ86808; EFQ86808; PTT_17842.
DR KEGG; pte:PTT_17842; -.
DR eggNOG; KOG3847; Eukaryota.
DR HOGENOM; CLU_024458_0_0_1; -.
DR OrthoDB; 2787776at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016715; PAF_acetylhydro_eukaryote.
DR PANTHER; PTHR10272:SF7; PHOSPHOLIPASE-RELATED; 1.
DR PANTHER; PTHR10272; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
DR Pfam; PF03403; PAF-AH_p_II; 1.
DR PIRSF; PIRSF018169; PAF_acetylhydrolase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR018169};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR018169};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR018169};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT ACT_SITE 260
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 310
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 389
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
SQ SEQUENCE 523 AA; 57614 MW; C3FB111C8F5D4F71 CRC64;
MTWLHRLNPT PAFPAHTGPY KVGSVDIEIP TSELESPTAN APPTDLPTVA FRVFYPCKQD
SNEKGVRWIP SPQREYVSAY ARFLGASNAF AGVLSVMPQL LYYVTMPVHQ NADLLAPPPK
SDRWPVMMFS HGLGGTRNAY SHICGSLASH GVVVVAADHR DGSSPLSIHH TPEEKEKVKR
VPYRNIAHSP STETYEARNE QLRIRLWELG MIHDALLKLD DGRKLTNVAQ DQPKGKNLLN
MFTNLMDVHQ PGAIGFAGHS FGACTMIQFV KSVYYRPKAQ IPSYKPLYIP TEDSSIVRQI
TSANSVHLLD LWTLPIQSPD TAWLRSQPMP CYDSKNGGKN LLAIASEGFY NWTSNFNESK
RIIAKPPASR SPYPNQPGPH IFYPIASAHL SQSDFGVLFP WVTTKAFGAK EPERVLRLNT
RAILQVLREN GVRVANTSAT DLELEDTAAK DASVAQDTTI LSRPKDSVRG WINLSADSEQ
GVDTEGVERK SLVGTPMERV GSGGKGPVDA MVEGEALGQI VKE
//
