ID A0A1E3HN93_9TREE Unreviewed; 559 AA.
AC A0A1E3HN93;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=L202_04930 {ECO:0000313|EMBL:ODN77807.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN77807.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN77807.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN77807.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:ODN77807.1}.
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DR EMBL; AWGJ01000007; ODN77807.1; -; Genomic_DNA.
DR RefSeq; XP_018993043.1; XM_019139100.1.
DR AlphaFoldDB; A0A1E3HN93; -.
DR GeneID; 30156239; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000094065; 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 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:UP000094065}.
FT DOMAIN 1..487
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 559 AA; 60009 MW; 540148656C8A0D5B CRC64;
MMVARGLENP PRIPNIGVAL SGGGYRAMLV GLGGVMGLMN QSQEASESGT GGWLEAVTYW
SGLSGGSWAT GSFMANGGPL PSSLIDSLWD LSSNLIYPSD NKVSFYSELY TEVTAKQDED
FPVQVTDLWG LALGSHLLPE DYHLDNSPNF TISSLPQMIP AIANASLPMP IIIAAEREQG
ELVIAENATV YEFTPYEFGS WAFGSDYKSA GAFTSVEYLG TSLDNGTANG TCWKGFDQLS
FVMGTSATLF NSAWLTLNQS DTGLVGDLLQ SILEDLGDSQ VDVSRIPNPF ANYNTGENPV
SSFEYITLID AGETNQNIPF EPLIAPSRNV DAIIAFDASY DTNTTWPNGT APRTTFERAM
VLAQYQNVEV RMPEVPSQNG FINGGYNSRP TLFGCDRTDT PIVVYVPSFP WSYGSNTSTY
QMSYDNDEAL EVMLSGMRSL TLNGSAETWP TCLACALTDR AFAYTSSNRS STCQTCFDTW
CWDGTDDTSE PEEYAPEIGG VPPWLAVKGL IIGVQDAPSS DTSRNSSSES GGFRVAGSVP
WAMSMALAAA GVAALALDL
//
