ID A8Q4N8_MALGO Unreviewed; 692 AA.
AC A8Q4N8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=MGL_2589 {ECO:0000313|EMBL:EDP42993.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP42993.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP42993.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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:EDP42993.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAYY01000009; EDP42993.1; -; Genomic_DNA.
DR RefSeq; XP_001730207.1; XM_001730155.1.
DR AlphaFoldDB; A8Q4N8; -.
DR STRING; 425265.A8Q4N8; -.
DR GeneID; 5854512; -.
DR KEGG; mgl:MGL_2589; -.
DR VEuPathDB; FungiDB:MGL_2589; -.
DR InParanoid; A8Q4N8; -.
DR OMA; SWWKANE; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 668..690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..616
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 47..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 76162 MW; 1E8CDBBFE94239B0 CRC64;
MSAQQASAVH KDENGVNVYT EQDMNAMLSP AEREKLIETM ARARNVVRAE HRRQRRMSPK
DSYAPAKVPC PKKPEGNNYV NYVRNASDHR MNELEQGYMQ RHRDNTRSLW VDWLKSVGLD
GDGGLPGGAE QFVSENQPKV GISVSGGGYR AMLVALGVSQ GFDSRNETSK NEGVGGFLQL
ADYYAGLSGG SWATGAQAIN GWPTAQSLVD DIMELSSNLV NPNHDSLSFY EDLFKDVSAK
KHADFPISIS DYWGRALSYQ LMNDTQYSDH GQRITYSDIV NQTGFRDATY PFPIVLSIGR
QPDQIMINPN ATYFEFTPYE FGTWQPTLEA FFPVGYLGTD VVDGNPKDGS SCIANYENFG
YTVGTSSTLF NGAYNKLLES NSTGFLNDVL KTILEDVDKG YNDVAPVPNP FKGYRQSSNH
FVDAKYIDLV DGGEANQNIP LEPLLQPARG LDLIVAVDAS SDQVNWPNGT ALIEVEKRSN
LSDFSYMAFP RVPDARTFVN RGFNTRPTFF GCDPNDATNA KTSVGNSTAP VLIYLPNYPY
SGFSNSSTFE LAYNVHHQHD MLDNARNVAT MGGQMDNWPL CLACASALRP MQRSGAKIPD
KCQQCMDMYC WDGKYDTSPT RNYTPPVGPP PFVTSHGQKS VEPPTTGSND STDTDYGKII
SSKDKSAAAP MGVSSAVFTS LFLASLLAMF MN
//
