ID B9U0W0_CRYNE Unreviewed; 626 AA.
AC B9U0W0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
DE Flags: Fragment;
GN Name=PLB1 {ECO:0000313|EMBL:ACB41984.1};
OS Cryptococcus neoformans (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=5207 {ECO:0000313|EMBL:ACB41984.1};
RN [1] {ECO:0000313|EMBL:ACB41984.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WM148 {ECO:0000313|EMBL:ACB41984.1};
RX PubMed=19517012; DOI=10.1371/journal.pone.0005862;
RA Ngamskulrungroj P., Gilgado F., Faganello J., Litvintseva A.P., Leal A.L.,
RA Tsui K.M., Mitchell T.G., Vainstein M.H., Meyer W.;
RT "Genetic diversity of the Cryptococcus species complex suggests that
RT Cryptococcus gattii deserves to have varieties.";
RL PLoS ONE 4:E5862-E5862(2009).
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}.
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DR EMBL; EU408627; ACB41984.1; -; Genomic_DNA.
DR AlphaFoldDB; B9U0W0; -.
DR VEuPathDB; FungiDB:CKF44_06085; -.
DR VEuPathDB; FungiDB:CNAG_06085; -.
DR VEuPathDB; FungiDB:CNBM0810; -.
DR VEuPathDB; FungiDB:CNM00920; -.
DR VEuPathDB; FungiDB:LQV05_001998; -.
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}; Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 20..626
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5005124591"
FT DOMAIN 46..569
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT NON_TER 626
FT /evidence="ECO:0000313|EMBL:ACB41984.1"
SQ SEQUENCE 626 AA; 67718 MW; 74A217E0A4F15701 CRC64;
MSIATATFAF SLFATIAFAV PPETPRIELQ AERGLGDKSY APWQVDCPSN VTWIRNATTG
LGSGERAYIE AREKLVQPVI EQMMAARGLE TPPRTPNIGV ALSGGGYRAM LTGLGGIMGM
MNESTEASES ETGGWLDGVS YWAGLSGGSW ATRTFMSNGG QLPTNLLENL WNIDSNLVFP
DDDKLSFYTE LYTETNAKSD LGFPIQITDV WGLAIGSHVL PERYQLSNTP NLTFSSLPSV
VSALGNASLP MPIIIAAERE AGELVIAENA TVWEFTPYEF GSWAFGSQYK SPGAFTPIEY
LGTSVDDGSP NGTCWKGFDQ LSFVMGTSAT LFNGAFLELN GTDSGLLTNL ITAFLADLGE
DQADISRIPN TFSNYNSGEN PIYNLTYITL VDAGETNQNI PLEPLLVPTR DVDAIVAFDS
SYDTDYIWPN GTALRTTYER AKVLAEHENT RVLMPEVPSM NGFVNGGYNS RPTFFGCNDT
TTPLIIYVPS YPWSFAANTS TYQLSYENDE ANEMLLNGMR SLTLNHSVPT WPTCFACALT
DRSFMYTSEN RSTTCQKCFD IWCWAGDDNT TEPATYEPVI NSVPPWLVAN NLSIGVADAP
ASNESTAGTA SSGAAKAGVS MGMVAL
//
