ID A0A1E4S033_CYBJN Unreviewed; 663 AA.
AC A0A1E4S033;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN ORFNames=CYBJADRAFT_168376 {ECO:0000313|EMBL:ODV72859.1};
OS Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617
OS / NBRC 0987 / NRRL Y-1542) (Torula yeast) (Candida utilis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=983966 {ECO:0000313|EMBL:ODV72859.1, ECO:0000313|Proteomes:UP000094389};
RN [1] {ECO:0000313|EMBL:ODV72859.1, ECO:0000313|Proteomes:UP000094389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC NRRL Y-1542 {ECO:0000313|Proteomes:UP000094389};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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; KV453933; ODV72859.1; -; Genomic_DNA.
DR RefSeq; XP_020069898.1; XM_020215342.1.
DR AlphaFoldDB; A0A1E4S033; -.
DR STRING; 983966.A0A1E4S033; -.
DR GeneID; 30989738; -.
DR OMA; ESSATKM; -.
DR OrthoDB; 1826981at2759; -.
DR Proteomes; UP000094389; 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 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:UP000094389};
KW Signal {ECO:0000256|RuleBase:RU362103}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT CHAIN 20..663
FT /note="Lysophospholipase"
FT /evidence="ECO:0000256|RuleBase:RU362103"
FT /id="PRO_5009027730"
FT DOMAIN 27..564
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 601..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 71207 MW; 8117B925F24B52A5 CRC64;
MLPFACLAVL AQLIDVSYSS YAPVNVSCPQ DATLVRSASS ISDDEKSWLE KRHSVTDDAL
SEFLERADLD GFDAKDFLNS LNRSITIGLA FSGGGYRAML NGAGQVAALD SRTEGANEHG
LGGLLQASTY FVGLSGGNWL TGTLALNNWT SVEEILSNDT IWDLENSIVT PGGSDVFETA
LRWQSIKADV DEKAEAGFDT SLTDLWGRAL AYQFFGEEND AEASLTYSSI VDIEAFQNGE
MPFPISIALG RAPDTKIINL NSTVFEFNPF ELGSWDPSLY SFANLKYIGS NVTNGEPTSD
ICVEGFDNAG FVLGTSSSLF NTVSLNVTGF AGLSSSLIST FLGGLDGAND DVAVYSPNPF
FQAGYASLKT IVESEELYLV DGGEDGQNIP FAPMLQQERD VDVIFAFDNS DNTEDNFPDG
TALVATYNRQ FSVQGNGTGF PYVPTNDTFL HNKLGEKPMF LGCNSSNLTD LGTIPPLIVY
IPNIAYTAWS NTSTLKMSYS TEDRNAIIQN GFEATTRFNL TIDENWPKCV ACAIIHREQE
RNGWGQSDEC AECFEEYCWN GEQYTGDDTI VDRSFNYTSS SNLDKSDMSS GVFEITVESS
STVGGSSTTS ASDAISTASS TSSGVSSASS SGTTTSASSK NNAMMTTPSM NFGALVMAMG
FLL
//
