EG1_ORYSI
ID EG1_ORYSI Reviewed; 435 AA.
AC A2WY00;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Phospholipase A1 EG1, chloroplastic/mitochondrial {ECO:0000305};
DE EC=3.1.1.32 {ECO:0000305};
DE AltName: Full=Protein EXTRA GLUME 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=EG1 {ECO:0000305}; ORFNames=OsI_04805 {ECO:0000312|EMBL:EAY76846.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Phospholipase that releases free fatty acids from
CC phospholipids. Catalyzes the initial step of jasmonate (JA)
CC biosynthesis. Required for the biosynthesis of endogenous JA in
CC seedling, inflorescence and spikelets. Not essential for JA
CC biosynthesis after wounding. Mediates spikelet development and
CC specification of empty-glume identity. Functions in a high temperature-
CC dependent manner to maintain floral developmental robustness under heat
CC stress conditions. Functions by safeguarding the expression of several
CC floral identity genes, such as MADS1, MADS6 and G1.
CC {ECO:0000250|UniProtKB:Q8S1D9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8S1D9}.
CC Plastid, chloroplast {ECO:0000250|UniProtKB:Q8S1D9}. Note=Localizes
CC predominantly in mitochondrion. {ECO:0000250|UniProtKB:Q8S1D9}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; CM000126; EAY76846.1; -; Genomic_DNA.
DR AlphaFoldDB; A2WY00; -.
DR SMR; A2WY00; -.
DR ESTHER; orysa-Q8S1D9; Plant_phospholipase.
DR EnsemblPlants; BGIOSGA004990-TA; BGIOSGA004990-PA; BGIOSGA004990.
DR Gramene; BGIOSGA004990-TA; BGIOSGA004990-PA; BGIOSGA004990.
DR HOGENOM; CLU_018841_2_0_1; -.
DR OMA; NTLASMW; -.
DR Proteomes; UP000007015; Chromosome 1.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR GO; GO:0010582; P:floral meristem determinacy; IEA:EnsemblPlants.
DR GO; GO:0048449; P:floral organ formation; IEA:EnsemblPlants.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Chloroplast; Hydrolase; Lipid degradation; Lipid metabolism; Mitochondrion;
KW Plastid; Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..435
FT /note="Phospholipase A1 EG1, chloroplastic/mitochondrial"
FT /id="PRO_0000434872"
FT MOTIF 264..268
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:Q8S1D9"
FT ACT_SITE 266
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 324
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 371
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
SQ SEQUENCE 435 AA; 46011 MW; 658FB5E4F3F2BC9B CRC64;
MTLPRQCAAA CRTGGGGGGV VRCRAVAAAG GAVAVRDAVV APVARRGAAR KTAETVAGMW
REVQGCGDWE GMLEPAPHPV LRGEVARYGE LVGACYKAFD LDPASRRYLN CKYGRERMLE
EVGMGGAGYE VTRYIYAAAD VSVPTMEPST SGRGRWIGYV AVSTDEMSRR LGRRDVLVSF
RGTVTPAEWM ANLMSSLEAA RLDPCDPRPD VKVESGFLSL YTSADKTCRF GGAGSCREQL
LREVSRLVAA YSGGGEDVSV TLAGHSMGSA LALLSAYDLA ELGLNRAAPV TVFSFGGPRV
GNAAFKARCD ELGVKALRVT NVHDPITKLP GVFLNEATAG VLRPWRHSCY THVGVELPLD
FFKVGDLASV HDLATYISLL RGADKKQPAA AAADAGGVLA KVMDFVGRRR GGGALPWHDA
AMIQMGGLVQ TLGLI
