ID A0A163B0S1_PHYB8 Unreviewed; 764 AA.
AC A0A163B0S1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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=PHYBLDRAFT_179930 {ECO:0000313|EMBL:OAD77611.1};
OS Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS 33097 / NRRL 1555).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD77611.1, ECO:0000313|Proteomes:UP000077315};
RN [1] {ECO:0000313|Proteomes:UP000077315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-2015) 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; KV440974; OAD77611.1; -; Genomic_DNA.
DR RefSeq; XP_018295651.1; XM_018438235.1.
DR AlphaFoldDB; A0A163B0S1; -.
DR STRING; 763407.A0A163B0S1; -.
DR GeneID; 28999141; -.
DR VEuPathDB; FungiDB:PHYBL_179930; -.
DR InParanoid; A0A163B0S1; -.
DR OrthoDB; 1997175at2759; -.
DR Proteomes; UP000077315; 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:UP000077315}.
FT DOMAIN 187..764
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 764 AA; 86850 MW; 240FA0ECF52CB365 CRC64;
MPFFAAWSIQ TVRQRAFLIG VGASTVTGVL LKCHYAKDNT PLIIREPSLP FRILCNFIPI
VALEPADPST PQSPPKGGPG AWLDSTRKIF QVDRMQEDVR RENDFISKMF SLKSTLPTMP
KINIPEPHIP SVEEINQRMN ELYPTFASQF DTLRESYEHF WDFLTMEDFR KLIDDIQRED
QDGLIYPEVG EDAIVREGSG LSKEEKKFIK VRKERQRQSF AKFMRVDPHE VELEDMPIVG
IASSGGGYRA MAGCAGYLKG MRDTGVLDCV MYMAGVSGSC WTMALYYSPL SGGSLEKLSG
HLQTHMHTHL ANVSSFLTVL SASKNNAKLL MQGVLERYYQ QNNTLNVVDV FGMLIGATLL
TKKKIDNTMA SESSECQDHS IDTEGSSKKK EDILRGIVTE EDGTQRKPIL LSKNAMKLSC
QDDVFGDGSQ PMPIYCAVRH DNAHTAEEEK DIYQWYEFTP FEMGCEEIDA WIPMWGFGRK
FDQGKNLERL PEQVFGSAFA ASLVQFYQEV RSFLPKRAID ASDEIVLRYQ ESMSNYHPIS
PASFPNPFYN LPEYGPIEEG CTFSRPKSLI ESKELCLMDA GMDNNIPFYP LLRQGRDVDV
ILAVDLSADI QTAHHFDRAE GYAKRRGVKG WPVDAGWPKQ HHSSKTNDYP LGTCTVFASH
ALETETEEAT GETYQTKAQR VTVVYFPFIL NKAFDPEFDP QTAEFCSTWN FVYTSDQVNK
LEGLAEKNWT ENIDQVREVL RKVWDRKRRQ RLEKLPDIEN PFTL
//
