ID A0A0J9WGZ5_FUSO4 Unreviewed; 580 AA.
AC A0A0J9WGZ5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Putative phospholipase {ECO:0000256|PIRNR:PIRNR018169};
DE EC=3.1.1.47 {ECO:0000256|PIRNR:PIRNR018169};
GN ORFNames=FOXG_01282 {ECO:0000313|EMBL:KNA95891.1};
OS Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS / NRRL 34936) (Fusarium vascular wilt of tomato).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=426428 {ECO:0000313|EMBL:KNA95891.1, ECO:0000313|Proteomes:UP000009097};
RN [1] {ECO:0000313|EMBL:KNA95891.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4287 {ECO:0000313|EMBL:KNA95891.1};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA Brockman W., MacCallum I.A., Young S., LaButti K., DeCaprio D.,
RA Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA Larson L., White J., O'Leary S., Kodira C., Zeng Q., Yandava C.,
RA Alvarado L., Kistler C., Shim W.-B., Kang S., Woloshuk C.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KNA95891.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4287 {ECO:0000313|EMBL:KNA95891.1};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS231696; KNA95891.1; -; Genomic_DNA.
DR RefSeq; XP_018233937.1; XM_018378095.1.
DR AlphaFoldDB; A0A0J9WGZ5; -.
DR GeneID; 28943547; -.
DR KEGG; fox:FOXG_01282; -.
DR VEuPathDB; FungiDB:FOXG_01282; -.
DR OrthoDB; 2787776at2759; -.
DR Proteomes; UP000009097; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF11; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009097};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 117..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 397
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 425
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
FT ACT_SITE 489
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR018169-1"
SQ SEQUENCE 580 AA; 64301 MW; 2C090233919EAE55 CRC64;
MRPDPLASSP PSSLTNKKHS THHLTSHHFP HHNLLVPILI PQEMPQSQNS IDLELNRLNS
PFSDSSSDPD LPLTMDPPAP KPRWLDPRPS SIFTRITSSV KPFAQYLRHV LRPRLTWRYV
ACSVIGVYVL YCFVTWQPLF SSRLPAYSGP HDVGAIDLEI PLEKPKRLSE TLLKSTKKPA
FEVESVLFTV YYPAVKGARS KDAPHPWVPK PLSLTAEGYA RAAGVNNFII RPIFTFALWV
LVGSIKIPAK VDVPLLGSDG EKFPVMVFSH GSVSSRTDYT HYLGELASRG HVIAALEHRD
GSCPGSMVQI KNKKDRPVFL LKEGDLISEP PMNDTLLKKE QLAFRTEEIM QAIRVLKDVN
DGKGKDIFTS SSRGEGSTLD GWKDRLDFKH LTINGHSYGA TGALQALKTA NTTAANPAIG
GIALDPGKSS GQLNTNIPVP LLVVHSNSWS KTHSIFFGRP HFDTVLDLVR GVRDEVGSAW
FLTSVGTAHP SVTDAPLLQP LLLNFATGAT ADVKKALGEY VKVTMDFLEF TKTNKENGVL
DEAVTHEKYG EWVSKEREKS FPKEYAKYWE VHVCPLDQDK
//
