ID A0A2G7FF92_9EURO Unreviewed; 595 AA.
AC A0A2G7FF92;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Lysophospholipase {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
GN ORFNames=AARAC_004245 {ECO:0000313|EMBL:PIG79280.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG79280.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG79280.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG79280.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC {ECO:0000256|ARBA:ARBA00002169}.
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|ARBA:ARBA00000960,
CC 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:PIG79280.1}.
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DR EMBL; NEXV01000694; PIG79280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G7FF92; -.
DR STRING; 656916.A0A2G7FF92; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000231358; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000231358};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..595
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013553130"
FT DOMAIN 37..555
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 595 AA; 64584 MW; FE830C566020B1B1 CRC64;
MKLNTLLLGA TLASAAPSLD LRALPNAPDE YAPANVSCPA VKPTVRSASK LSQNETDWLE
SRRKEVVSPL KNLLGRLNLT NFDASAYIDR VSTNMSNLPN VGIAVSGGGY RAMLNGAGAL
KAFDSRTTNS TASGQLGGLL QSATYLSALS GGGWLVGSVF VNNFTTINDL QTTENTWDLR
NNILEGPDVK HFQIFKTVDY WTELVDTFIN ASNGGPDYTW SSIALMDNFQ RGQTPLPILV
ADGRNPGELV VGSNSTVYEF NPWEFGTFDP AIYSFAPLEY LGSDFKGGKI SSNGSCVRGF
DNAGYIMGTS SSLFNQGLLR LNGTKIPKIF KSAMESILED LGQDNNDIAN YPNPFYQYTG
ATTNIASRSH LSVVDGGEDG QNIPLHPLIQ PERHVDVIFA VDSTANIHNW PSGKSLVRTY
ERSLSSTVSN GTVFPAVPDP NTFINLGLNK RPTFFGCDSK NLTGPAPLIV YLPNAPYTYL
SNTSTFDLSY SYEDRDDMIT NGYNVVTRGN GTEDANWPSC VGCAILSRSA ERTSTTLPEV
CSKCFKDYCW DGTINSTEPE NYEPQLMIKT SLAPRELPGS FAAMFSFALA LVMML
//