ID A0A180GKH9_PUCT1 Unreviewed; 571 AA.
AC A0A180GKH9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=PTTG_09544 {ECO:0000313|EMBL:OAV93287.1};
OS Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=630390 {ECO:0000313|EMBL:OAV93287.1};
RN [1] {ECO:0000313|EMBL:OAV93287.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV93287.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAV93287.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV93287.1};
RA Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA Young S., Zeng Q., Fellers J.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000256|RuleBase:RU362103};
CC -!- SIMILARITY: Belongs to the lysophospholipase family.
CC {ECO:0000256|ARBA:ARBA00008780, ECO:0000256|RuleBase:RU362103}.
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:OAV93287.1}.
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DR EMBL; ADAS02000052; OAV93287.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180GKH9; -.
DR STRING; 630390.A0A180GKH9; -.
DR VEuPathDB; FungiDB:PTTG_09544; -.
DR OrthoDB; 1826981at2759; -.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR PANTHER; PTHR10728:SF33; LYSOPHOSPHOLIPASE 1-RELATED; 1.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51210; PLA2C; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW ProRule:PRU00555};
KW Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103}; Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 20..571
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5007950402"
FT DOMAIN 32..571
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 571 AA; 61995 MW; CCAA4AB799C25C66 CRC64;
MKFLLEFLYL LNIFFSTYSL GQGQTYAPQN ADCPATSLIR TAGTVASGNQ ALGAKESLYI
EERRKKAVPE AYREYWRNVE SSVRRNRARL PEYVKSILLG PSDHLPRVSG ALSGGGLRAS
FVGAGILNAL DGRNQTSASR GTGGLLQAMD YLTGLSGGAC LVMSMSQANF PGIYDLTLGS
IIDETEGWLA DMDFVAPAGL NRILENPIFL DTKWWSTLGF QVSQKALAGF DVTLGDIYSR
ILAYHFVSGT TRDNFFDPQA EHGLEQSLSD LATQESIRSY SQPFPIITSV AESPGQGPIV
QRGDAVPLSN NQYEFNMYES GSWDPNLASF IDTAYLGSSL ENGQPSKAKG CVNQFDNLGF
LVAASSNIFR KYDAFATLFQ PKSYRPFLPA LKGVLSLIPN PFYGLGTAEY LDRKSKTLSL
MDGSFGGENI PFAPLLVPAR EVDVIVAFDA SDDANGWPDG TSLKVTSARS KLFPNEAYPF
PRIPEKLSQI NITQPTIFGC DEPEVPLVIY IPNSPPTDGS ATATNLPTAS LEVSQYRALS
LIEGGTKLAT RGISNDPICV IIERTSRTKS L
//
