ID A2QT90_ASPNC Unreviewed; 638 AA.
AC A2QT90;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=An09g01240 {ECO:0000313|EMBL:CAK49046.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK49046.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK49046.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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}.
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DR EMBL; AM270193; CAK49046.1; -; Genomic_DNA.
DR RefSeq; XP_001393442.1; XM_001393405.2.
DR AlphaFoldDB; A2QT90; -.
DR EnsemblFungi; CAK49046; CAK49046; An09g01240.
DR GeneID; 4983655; -.
DR KEGG; ang:An09g01240; -.
DR VEuPathDB; FungiDB:An09g01240; -.
DR HOGENOM; CLU_014602_0_0_1; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000006706; Chromosome 1L.
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:UP000006706};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 17..638
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5005121085"
FT DOMAIN 53..599
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 638 AA; 68643 MW; 815AB1DF9B6656F6 CRC64;
MKLPLFAAAA AGLANAASLP VERAEAEVAS VAADLIVRAL PNAPDGYTPS NVTCPSTRPS
IRDASGISTN ETEWLKVRRN ATLTPMKNLL SRLNLTGFDT TSYINEHSSN ISNIPNIAIA
ASGGGYRALT NGAGALKAFD SRSDNATNSG QLGGLLQAAT YVSGLSGGSW LVGSMFVNNF
SSIGELQASE KVWRFDKSLL EGPNFDHIQI VSTVEYWKDI TEEVDGKANA GFNTSFTDYW
GRALSYQLVN ASDDKGGPDY TWSSIALMDD FKNGQYPMPI VVADGRNPGE IIVETNATVY
EVNPWEFGSF DPSVYAFAPL QYLGSRFENG SIPDNGTCVS GFDNAGFIMG SSSTLFNQFL
LQINSTSIPT ILKDAFTDIL EDLGERNDDI AVYSPNPFSG YRDSSEDYAT AKDLDVVDGG
EDGENIPLHP LIQPERAVDV IFAIDSSADT DYYWPNGTSL VATYERSLEP SIANGTAFPA
VPDQNTFVNL GLNSRPTFFG CDPKNISGTA PLVIYLPNSP YTYDSNFSTF KLTYSDEERD
SVITNGWNVV TRGNGTVDDN FPSCVACAIL QRSTYRTNTS LPDICTTCFN DYCWNGTTNS
TTPGAYEPSV LIATSGAIKS VLDYSVLALA MGVAAFML
//
