ID A0A0C9MJ70_9FUNG Unreviewed; 1231 AA.
AC A0A0C9MJ70;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=MAM1_0424d10446 {ECO:0000313|EMBL:GAN10896.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN10896.1};
RN [1] {ECO:0000313|EMBL:GAN10896.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN10896.1};
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 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000798,
CC ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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DR EMBL; DF836713; GAN10896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9MJ70; -.
DR STRING; 91626.A0A0C9MJ70; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR CDD; cd01254; PH_PLD; 1.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815}.
FT DOMAIN 287..419
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 425..530
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 657..684
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1025..1052
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..980
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1231 AA; 142434 MW; 4FD0FF678B1D63EA CRC64;
MEYFKKVHHH RNNNNSHHHQ HHHGIKTSYF ERGGYEEDDE YSDFVDTERS DTEDEAADAS
ASKWHSIFRR MSINIQRDEG TPDKDITSGT AANPSDHERA LMLNIPHSDG SEVCETFEDD
TLPTVEQVAV DCVNVQDPPC TRYFENPFES DSTSTDDTMY VAATANEMKQ SQLHPLSHAP
AATHGLVMPE KKKIHGAMFT STPDSAMKND APQATNNKAK MQWAKTFEKI KVVNSLGGNN
QRRSSSAHYT TTRQPLAPYY PSAFIPGYLS LMCRDEHGRK APPILFDALN VSITDSEIDH
SAIHRLWTFR IELQYGEIKW VINRTIIEFY NLHLTLKFKY ISGFISEPPP SFPSQLAHLT
NAALTSMRIA REEEDGVWRD AALKRRDALE VYLKALIQGA SMLVNYELCE FLELSAISIV
KDMGWKGKEG YLEYNLNPSS MRLFHWHRWQ KEWLILRDSY IAFCKDIGST APADVLLFDK
HLKVVRTQST FGSIHQTHFI ISNSSRRIEV KAPTSKHIEE WIENLDKVQN ESPWIMNHRF
GSYAPVRENA KAKWFVDGHD YFEAVAQAIL SAKSEIYIED WWLSPQLYLR RPVKGNEEYR
LDRLLKRKAC EGVMIYIVIY KNVSVALPLD SQHTRDWMHH VHPNIIVQRH ANLTSSPFWA
HHEKILVVDY RLAFVGGLDL CFGRYDTSKH DLTDYKSFDE KVVFPGQDYS NPRIKDFHKV
SQYNMELIDK QCAARMPWHD IHTAMIGPPA RDIARHFIQR WNFIKSNRAK ERSEVPFLLP
KGEYVAARDE AKFKGTCRIQ VLRSSAEWSL GITREYSIYS AYMECIFKAK HFIYIENQFF
ITTTSPNDKL IKNKIGQAIV ERIKRAHREK QKFRVIVVIP IAPGFEGDFI QVDRKSMPLR
SVAQYQYRSI SRGKYSVFEQ LRKANIPIKD YIGFYSLRNW GKVKKSTPTP VPIMRDEFGQ
IIPPPPPPPP PPPPPPLQPR SKRRLKSRSS SQNKSNEDFQ QQLQLERALL EQQQYNDGRM
DFVTEQVYIH TKLMIVDDRT VICGSANLND RSQLGNRDSE IAVVIEDTDL VDSRMNGQPY
KASKYALTLR MQLFKEHLGL LNVQSSNEYH VNGYRDMKRE DVVVMDPLHD EFYYDIWNKT
AEKNTLVYRD VFRCVPDDTV HSVEQHRQFV PDPTRVLPGH VAEPWNRTNE QIQAKLDDIQ
GHLVEFPTEY LKNISMTASV MQEAVPPIVF T
//
