ID I1BSN8_RHIO9 Unreviewed; 1172 AA.
AC I1BSN8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=RO3G_03923 {ECO:0000313|EMBL:EIE79218.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE79218.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE79218.1, ECO:0000313|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000313|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
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|PIRNR:PIRNR009376}.
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DR EMBL; CH476733; EIE79218.1; -; Genomic_DNA.
DR AlphaFoldDB; I1BSN8; -.
DR STRING; 246409.I1BSN8; -.
DR VEuPathDB; FungiDB:RO3G_03923; -.
DR eggNOG; KOG1329; Eukaryota.
DR InParanoid; I1BSN8; -.
DR OMA; CAVHNTE; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000009138; 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; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
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; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50035; PLD; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000009138}.
FT DOMAIN 504..531
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 789..816
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 1172 AA; 135323 MW; 4EEA542E40FCBB9D CRC64;
MNTITPLIMA MYFTRDEHNK HRIPVFLKNI VCKVTLVDEQ DEKRKMLSGS VFKITIQYGS
GAGKIIWSVY RTYWDFVKLH YRYRDAAASR LPPFPSLPRH YFHKRQRKTS FNKQNQNLPG
SYMDEETIMA IVNHTLHPER DGDSTASLAP SQIVDVVDPD RTVLNALEDY LNELVSSIEP
CGYINRICRF LEISWIGLHL AAKYPGLHGK EGFAVLQSRT DREPKQTRRR LHNGFICFSL
NPGRKKQKPK WFIVRESYLA CVDDPSESEI YDVFLFDQAF EVHRLNIFGD RSNHQVKNSS
KKLSNAIANA SHWASGRSVL CIKNKQGVYH FRTKSERHAK QFEISLRALA SRSIWCEQHR
FGSFAPVCHQ TGVTWFVDGR DYFWDLSVAL ENAKETIYIH DWWLELVSFI SLDVFPIHSS
SNPNNPQFLR RPASRHPEWR LDRVLKRKAH QGIKIYIVMY KEVAVALPLY SHLAKRHLLS
LSPNIYVQRH PSRALDVFHK DSIFFWAHHE KICVIDNEIA FLGGIDACFG RYDGPGHILV
DDGQETIWPG KDYSNPRIID FHTLDKPFED NMDRSRLPRM PWHDISMRLV GSAAQHVARH
FVERWNFLRR KKPAAPKRPT PMLLPVPEID RVLPMSDSRL LHPYTSTLCQ VQILRSVSPW
SIGSTEHVEH SILNAYVECI KESRHFIYIV IENGIGQAIV DRILRAKREG KKWRAIIVIP
LVPGFPANID ETEATTVRLI MQCQYLSIGR GPHSLLAKLH AAGITQTHEY INFYGLRNWA
ELNHQYVTEQ VYIHAKTMIV DDQKVITGSA NINERSQLGT RDSEIAACVE DRDWVDSVLD
GQPVKVARYA HSLRMRLMCE HVGLDVDQMD RDRSTQGDLL CSPYLKQPVW DESKVCDTKD
TIDCLPPFVQ VSPERVERVV EAVEESEEVF VVSPDSETSS CTEDEETKRV KAKVEQLNEH
GGQVLTKTSS NERDSVMSPT KSIFSKRKSS KEDYLDFWTT LDCDTDNNGD RPFSSRLPEY
YASPNVMPLF FESKTKGLTV GEVYEILRDP MRDDFQEFWH VLARSNTNLF RRSFLVMPDN
NVKNWDQYHH FIKMAKLFLG RTDPKHGGTK TTVAAAAVTT LPIFQQGGET VHDLLKHIKG
HLVIWPNSFM EEEKDNEFIF QIDKIPPIEI FD
//
