ID A0A1F7ZNY9_9EURO Unreviewed; 619 AA.
AC A0A1F7ZNY9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=ABOM_009837 {ECO:0000313|EMBL:OGM41157.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM41157.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM41157.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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:OGM41157.1}.
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DR EMBL; LYCR01000119; OGM41157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ZNY9; -.
DR STRING; 109264.A0A1F7ZNY9; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000179179; 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 CDD; cd07203; cPLA2_Fungal_PLB; 1.
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:UP000179179};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..619
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012768770"
FT DOMAIN 37..579
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 619 AA; 66744 MW; B6AAF31A4D56D00B CRC64;
MKLNVLLLGA ALASATPDLH LRALPNAPDG YAPANVSCPA VKPAVRSASK LSQNETDWLD
ARRKEVVSPL KNLLGRLNLT NFDASAYIDR VSANTSNLPT VGISVSGGGY RAMLNGAGAL
KAFDSRTTNS TASGQLGGLL QSATYLSALS GGGWLVGSVF INNFTTISDL QTSENTWDLT
NNILEGPSVK HFQLLNTVDY WTELVDTVKT KKEAGFNTSL TDYWGRALSY QFINASSGGP
DYTWSSIALM ENFQRGQTPL PILVADGRNP GELVIGSNST VYEFNPWEFG TFDPAIYSFA
PLEYLGSDFK GGQISSNGSC VRGFDNAGYV MGTSSSLFNQ GLLRLNGTKI PKIFKSAIAS
ILEDLGQGND DIANYPNPFY EYTGATEAIA RRSHLSVVDG GEDGQNIPLH PLIQPERHVD
VIFAVDSTAN IHSWPSGKSL VRTYERSLNS TISNGTVFPA VPDPNTFINL GLNKRPTFFG
CDSKNLTGPA PLIVYLPNAP YTFLSNTSTF DLSYSYEDRD AMITNGYNVA TRGNGTEDAS
WPSCVGCAIL SRSAERTGTT LPEVCSQCFK NYCWDGTINS TEPADYEPQL MIKTSLAPRK
LPGYTAAIFP FALALAMML
//