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Database: UniProt
Entry: A0A0C9M6Z6_9FUNG
LinkDB: A0A0C9M6Z6_9FUNG
Original site: A0A0C9M6Z6_9FUNG 
ID   A0A0C9M6Z6_9FUNG        Unreviewed;       864 AA.
AC   A0A0C9M6Z6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   ORFNames=MAM1_0099d05195 {ECO:0000313|EMBL:GAN05721.1};
OS   Mucor ambiguus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN05721.1};
RN   [1] {ECO:0000313|EMBL:GAN05721.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN05721.1};
RA   Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT   "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT   ambiguus NBRC6742.";
RL   Submitted (SEP-2014) 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}.
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DR   EMBL; DF836388; GAN05721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9M6Z6; -.
DR   STRING; 91626.A0A0C9M6Z6; -.
DR   OrthoDB; 1997175at2759; -.
DR   Proteomes; UP000053815; 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:SF40; LYSOPHOSPHOLIPASE; 1.
DR   Pfam; PF01735; PLA2_B; 2.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
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|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053815}.
FT   DOMAIN          161..864
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          344..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          759..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..744
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   864 AA;  97166 MW;  BD72CEE9740904F2 CRC64;
     MGKGVTSSIS TRSKVALVTL ISVSVLGSVY YSKYKHNKSN KRKSIDLADK KLAATIDDNS
     LYNDFVASLP SSLNLIDDSA DNFLSSLFNS SYSPSDYIPG FIPTSIEELK EQMASLYPSF
     ESQFETIREM YNSFWEFLSL EEFRNIVQES IQEDDDPEMH PEIEQDAYVR TGQALSEEEI
     QFTEARKQKM RAAFAFFIGV DEHEVEIEDI PNIGIASSGG GYRAMVACSG YLHALNETGI
     LDCVLYMAGV SGSTWAMSQF YSPLTNASVD TLKDHLSSRI HTHIANLSNF LTVLNASRHN
     AKILLHGVVQ RYYQQNGSIS LVDIFGMLLG GTLLAKKVTV APPDKEKSDR IMENDAHSYT
     ESIEDPSELG LKNKEDHTQP GTVHEDDGAE VKPRLLKKNE IKLSMQKDYF QDGSLPMPIY
     CAVRHEVELA SVTKAATVSS KQGVEPCQKV DDGEEDEALE HVEADDAKSE DTEKETKDDG
     GNEAEETDKK TEEDEEHQKE EAVEEEMNDL YQWFEFTPYD MGSEEINAWI PIWAFGRKFE
     NGKNTERLPE QSLGILMGMF GSAFVASLAH FYQEIRLLLP TSAIEKADEM INNYQASVST
     IHPISPASFP NPFYKMPTTV QDKDASQDKE EVLRSESLVE SELIGLMDAG MDNNLPFYPL
     LRQGRDVDII LAIDLSADIQ EAPYFDRAEG YVKRRGIKGW PVGAGWPRKE EESHESEKSD
     ADPVKVEHPK KPSAKDSKQQ EPKESKYALD TCTVFASSSS ETIPSSSDED ASTTITSYPE
     NTNPITLVYF PLIVNENYDP EFDPQTAEFC STWNFVYSSE QVNKLHGLAE ANVKDNLEKV
     RKVIKETWKR KRDERLRRES LPRI
//
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