ID A0A0L1J823_ASPNO Unreviewed; 659 AA.
AC A0A0L1J823;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=ANOM_003741 {ECO:0000313|EMBL:KNG87840.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG87840.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG87840.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG87840.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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:KNG87840.1}.
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DR EMBL; JNOM01000068; KNG87840.1; -; Genomic_DNA.
DR RefSeq; XP_015408763.1; XM_015548998.1.
DR AlphaFoldDB; A0A0L1J823; -.
DR STRING; 1509407.A0A0L1J823; -.
DR GeneID; 26805545; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000037505; 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:UP000037505};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 21..659
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5005394363"
FT DOMAIN 51..607
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 613..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 70741 MW; F61BCEE3B6AF17C8 CRC64;
MKNTFLLGTV AVSLFPGITA SPLIPSQHQV TNVNPRALPN ALNGYAPVHV TCPKTRPSLR
NGATLSSEET SWLEARRGKT LPALKDFFGH VQIDGFDAVS YLESHAHDLT NTPTIGLAIS
GGGLTAALNG AGTFKAFDSR TEGTMAKGQL GGLLQSTTYF SALSGGSWML GSVYINNFTT
VSALQEQGNL WNFSSGNIFA GPPNMDPQEF WGNITTQVKT KRAAGFVTSD PDVWGRVQGY
FFFNASHGGV DYTWSSIAKS QAFQDAEMPL PVVVVKGQSF DKALEAPTNS EPIYEVSPWE
FGTYDSSIYG FVPLEYLGTR FINGIVPENE TCVRGFDNAG FITGSSSDIW NQGKSADIVG
TLKSMLSEIS KQSPEEAQFL KLVIAGVISA TNSTNSTLTG SAAYEPNPFY QYNTDSSPFA
QEKRLTIVDG GEGGQNIPFN PLIQRKRNVD VIFGVDSLGS DGSWPTGSAI ISTYERTLDD
LANTSFPYIP DQNTILNLDL NARPTFFGCN SSNLTTPAPL VVYLPNHPVT YNATTTLTDT
DFSSARRDGF IMNGYNVATQ ANGTLDSEWT TCVGCAILSR SFDRTSTTVP EACSRCFQRY
CWNGTIDDRT PPPYSPSVLL PNTTSTTGTS PTASSMGSSL DAAVWSAIAM VGMAVFVIG
//
