ID   A0A1S3TK73_VIGRR        Unreviewed;       414 AA.
AC   A0A1S3TK73;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Phospholipase A1 {ECO:0000256|RuleBase:RU367093};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU367093};
GN   Name=LOC106756298 {ECO:0000313|RefSeq:XP_014494157.1,
GN   ECO:0000313|RefSeq:XP_022634406.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|RefSeq:XP_014494157.1};
RN   [1] {ECO:0000313|RefSeq:XP_014494157.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014494157.1,
RC   ECO:0000313|RefSeq:XP_022634406.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Acylhydrolase that catalyzes the hydrolysis of phospholipids
CC       at the sn-1 position. {ECO:0000256|RuleBase:RU367093}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU367093}.
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DR   RefSeq; XP_014494157.1; XM_014638671.2.
DR   RefSeq; XP_022634406.1; XM_022778685.1.
DR   GeneID; 106756298; -.
DR   KEGG; vra:106756298; -.
DR   OrthoDB; 1210884at2759; -.
DR   Proteomes; UP000087766; Chromosome 2.
DR   GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00519; Lipase_3; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002921; Fungal_lipase-like.
DR   InterPro; IPR033556; PLA.
DR   PANTHER; PTHR31828:SF10; PHOSPHOLIPASE A1-IIDELTA; 1.
DR   PANTHER; PTHR31828; PHOSPHOLIPASE A1-IIGAMMA; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU367093};
KW   Lipid degradation {ECO:0000256|RuleBase:RU367093};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU367093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087766}.
FT   DOMAIN          131..304
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
SQ   SEQUENCE   414 AA;  46127 MW;  B08406B275A22AA2 CRC64;
     MASQPTWAEL LGHNDWAGLL DPLHPSLRNL ILRCGDFIQA TYDAFNNDKN SPFCGASRYG
     KTSFFRKVML DDADHYNVTA FLYGTARVSV PEAFLLHSLS REAWDRESNW IGYVAVTSDS
     RSKELGRREI YVVWRGTTRD MEWINVFGAG QESASALLNA ESVKELKARN KDGNSSSDDE
     DDSEIPKVML GWLTIYTSDD PKSPFTKTSA RTQVLSHVKS LVERYKSENP SVLIMGHSLG
     ASLSIVSGFD LVENGVTDVP VTAVVFGSPQ VGNKAFNNRF KKKGNLKVLH VTNVIDLIPH
     YPGRLLGYEH TGVELVIDTR KSPSLKESKN PSDWHNLQAM LHVVAGWNGA RGEFELNVKR
     SLALVNKSSS FLKDEIGVPG SWWVEKNKGM VKREDGEWVS NAPDEEDVPV PEQI
//