ID B9U0X2_CRYNE Unreviewed; 626 AA.
AC B9U0X2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:ACB41996.1};
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:ACB41996.1};
RN [1] {ECO:0000313|EMBL:ACB41996.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HamdenC3-1 {ECO:0000313|EMBL:ACB41996.1}, and LA511
RC {ECO:0000313|EMBL:ACB42000.1};
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; EU408639; ACB41996.1; -; Genomic_DNA.
DR EMBL; EU408643; ACB42000.1; -; Genomic_DNA.
DR AlphaFoldDB; B9U0X2; -.
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_5007360847"
FT DOMAIN 46..569
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT NON_TER 626
FT /evidence="ECO:0000313|EMBL:ACB41996.1"
SQ SEQUENCE 626 AA; 67601 MW; A15A099B0FBA6453 CRC64;
MSIATATFAF SLFATIAFAV PPETPRIELQ AERGLGDKSY APWQVDCPSN VTWIRNATTG
LGSGERAYIE AREKLVQPVI EQMMAARGLE TPPRTPNIGV ALAGGGYRAM LTGLGGIMGM
MNESTEASES ETGGWLDGVS YWAGLSGGSW ATGTFMSNGG QLPTNLLENL WNIDSNLIFP
DDDKLSFYTE LYTETNAKSD LGFPIQITDV WGLAIGSHVL PERYQLSNTP NLTFSSLPSV
VSALGNASLP MPIIIAAERE AGELVIAENA TVWEFTPYEF GSWAFGSQYK SPGAFTPIEY
LGTSVDDGSP NGTCWKGFDQ LSFVMGTSAT LFNGAFLELN GTDSGLLTNL ITAFLADLGE
DQADISRIPN TFSNYNSGEN PIYNLTYITL VDAGETNQNI PLEPLLVPIR DVDAIVAFDS
SYDTDYIWPN GTALRTTYER AKVLAEHENT RVLMPEVPSM NGFVNGGYNS RPTFFGCNDT
TTPLIIYVPS YPWSFAANTS TYQLSYENDE ANEMLLNGMR SLTLNHTVPT WPTCFACALT
DRSFMYTSEN RSTTCQKCFD TWCWAGDDNT TEPATYEPVI NSVPPWLVAN NLSIGVADAP
ASNESTAGAA SSGAAKAGVS MGMVAL
//
