ID A0A397IXP5_9GLOM Unreviewed; 612 AA.
AC A0A397IXP5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=Glove_169g43 {ECO:0000313|EMBL:RHZ77874.1};
OS Diversispora epigaea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Diversisporaceae; Diversispora.
OX NCBI_TaxID=1348612 {ECO:0000313|EMBL:RHZ77874.1, ECO:0000313|Proteomes:UP000266861};
RN [1] {ECO:0000313|EMBL:RHZ77874.1, ECO:0000313|Proteomes:UP000266861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT104 {ECO:0000313|EMBL:RHZ77874.1,
RC ECO:0000313|Proteomes:UP000266861};
RA Sun X., Fei Z., Harrison M.;
RT "Genome and evolution of the arbuscular mycorrhizal fungus Diversispora
RT epigaea (formerly Glomus versiforme) and its bacterial endosymbionts.";
RL Submitted (AUG-2018) 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:RHZ77874.1}.
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DR EMBL; PQFF01000159; RHZ77874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397IXP5; -.
DR STRING; 1348612.A0A397IXP5; -.
DR Proteomes; UP000266861; Unassembled WGS sequence.
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:SF40; LYSOPHOSPHOLIPASE; 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|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103};
KW Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW ECO:0000256|RuleBase:RU362103};
KW Reference proteome {ECO:0000313|Proteomes:UP000266861}.
FT DOMAIN 70..612
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 612 AA; 69359 MW; C864E26FD19AF708 CRC64;
MSTTKITLWF AAIKDTFVNR FQEANKSARE VLEAATQDFQ ENIKIVEVLL AFKDLSNIVL
PRLIDTTLYP ELEWDASVRD SIDICEQELK FIKDRRQVIR ESFAKYVGVD VSEIHEEDIP
VIAFMGSGGG FRAMIGAAAY FSAVKESGLY DCGIYHAGLS GGSLFMAQLF SSRFQSAENP
IQTLLEFYRT NLSTSIIDIT NILQELANTS DPRIAVGLSF GSLIHKKASG VGLSIMDIFG
ALLAVKLMIG TDLTNQHGDF KLSEQQKYIE GGKSPMPLYV AVSHIRPWKD VLEPEEASLI
PNYDQVYAAH IMKKDYYQWY EFSPYEIGSD ELPAWIPSWA FGRKFKSGKT IERFPEQNFS
LLMGLFGSAP AAPFIEVITE IETFLYEGKV KQYFKSAYEN ALKSLEDHTR KIVEGLHLIP
PPHNHNFAHR VKPPPYELGH TNNKVLDLLD AGLSNDFPMY PISHPSRKID VVIGFDCSSN
AVDHKNFDIS QDKFCARRGF NRIMRDETNK YCEVLDYIPN GKTDDERLTP AQKQFVLCLL
QYLPNDKVDP TFEPATADFA TLNKFSYSTE NVDLMIKLAK QNWKDGEEKV KEIVIDTWKK
KKDARLNGTV FP
//
