ID D2V310_NAEGR Unreviewed; 486 AA.
AC D2V310;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
DE Flags: Fragment;
GN ORFNames=NAEGRDRAFT_30788 {ECO:0000313|EMBL:EFC48698.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC48698.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC48698.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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};
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DR EMBL; GG738850; EFC48698.1; -; Genomic_DNA.
DR RefSeq; XP_002681442.1; XM_002681396.1.
DR AlphaFoldDB; D2V310; -.
DR STRING; 5762.D2V310; -.
DR EnsemblProtists; EFC48698; EFC48698; NAEGRDRAFT_30788.
DR GeneID; 8852417; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_30788; -.
DR eggNOG; KOG1329; Eukaryota.
DR InParanoid; D2V310; -.
DR OMA; RDERYEW; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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; 2.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 136..163
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 405..432
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT NON_TER 486
FT /evidence="ECO:0000313|EMBL:EFC48698.1"
SQ SEQUENCE 486 AA; 56146 MW; 1A6C823F271C705F CRC64;
MYHLDNRKGA EGEACRFNSY APERQKVRAK WYVDGKDAFQ DIALAISLAK EEIFIADWCL
HPTLYLLRGD GKEVADSRLD ILLKKKASQG VRIYILLWNE TSLAGLNLNT KKTKNYLKSL
YPKNIYVKTH PKQYPVEWSH HQKLVVIDQS IGFLGGLDMC YGRWDDYKHN ITDMNHSHSK
YPGNDYQNPN YHAYYKYADK LDSFTDVIDR EYSTRQAWHD IHCSVTGLAA KDCSFNFVER
WNFSINGSKD SKENKNEGFL CNAQLVRSLC KWSGSPRDEQ SVYAAYLHLI DNAKHYIYIE
NQYFIGSTSD LPKNVIPEYI ARKVVEKMKA KEVFRVIIVV PSHPEGDMAA STTQQIMKYS
YNTIKNGPNS MFSYIKKHVT GATDKDIENY IFFCTLRNYG FAVTEHIYVH SKMMIVDDYI
TIIGSANIND RSMLGTRDSE IAVVIQDHPT SVIHTKMNGR HYKSGKFAHS LRIRCWREHL
GLLPSQ
//
