ID M3HPV0_CANMX Unreviewed; 1741 AA.
AC M3HPV0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, 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};
GN ORFNames=G210_5726 {ECO:0000313|EMBL:EMG49502.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG49502.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG49502.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG49502.1}.
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DR EMBL; AOGT01000643; EMG49502.1; -; Genomic_DNA.
DR STRING; 1245528.M3HPV0; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_3_0_1; -.
DR OMA; DSLWTKH; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000011777; 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; 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; 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:UP000011777}.
FT DOMAIN 763..790
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1073..1100
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1544..1677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1741 AA; 199633 MW; 53E4A4DF203EF802 CRC64;
MPPTVDEHGL QSLPSEKLRR KKPVSDDDED DEQTQVKVPR TANEIPINGQ QKENNQPLRE
DPDVDRIFQS VDEGPITPKS YERSPSPTTR GGSETVVPNA FQFTYSEDPQ QQRHRQYRFP
FSSHYQHNRR SDTNISGHND TMNEASEIDR FETVNDDDVA DTSAFRRDTT TSQRHPFTHS
QTLSSLIPSR LKGRSASTFH DPLTSTNPDQ TNIQEVLNSR NDKNKHNRFK NFLRTNRRKG
KDKRQSVIPT NDESENAAID RAEKLLAGMA AGGPAINLMA SCLLEDEHGI SRAPLLLSLL
GFKVTDVTVK ETTRNRRFRI DLEYGIDRQR MKWSIEKNAT DLAYLAYKFE RARLVGRVAG
NKTQPLPKFP VPPIRKHENK KSRKFRTMIS DNQNKTEQQQ HGDDDNHSIS PVASIISRTR
SRLGSITSIA SLERHHESVE TRRQKIAQYI KDVDFYLREM IEAASLKPQS NILFVFFEVS
PLSSLLSYEQ GYSGKQGPVH IGGTARSQGW RVGHFKANDL KGIYERRAEK WMLIRNSYLT
YVSDINSTSP LDVFLVDSSF KIHSRKLEVT TKDDDESVFD NASLTEKKII DSESKFFPHL
KITLENAERS LVISPKSPRD HKLWLNSLQT MQSLTPWSEP HRFSSFAPVR KNCFAQWFVD
GRDYFWAVSS AIEMAKDTIM IHDWWLSPEL YLRRPANGNQ QYRLDRLLQR KASEGVKIFV
VIYRNVGTTV ATDSLYTKHS ILSLNEENIH VIRSPNQLLQ NTYFWAHHEK LCIIDHTYAF
LGGIDLCYGR YDTPDHTLVD DSAVDFAALG SDDRITAQTF ADFQVFPGKD YSNPRVKDFF
ELEKPYESMY NRNAVPRMPW HDIHMYTCGQ TARDLSRHFV QRWNYLIRQK RPSRLTPLLL
PPSDLAEDDI LAHGLDGTCE VQLLRSSGNW SLGLKQHEQS IQNAYLKLIE TSEHFVYIEN
QFFITSCFID GTEIKNRIGD ALVDRIIRAH QEGTNWKAII VIPLMPGFEA QVDEAEGSSV
RVIMQCQFMS ISRGDSSIFA KLRKKGINPD QYIQFFSLRK WGRIGNDRTL VTEQLYIHAK
AMVADDRTAI IGSANINERS MRGLRDSEVA AVVRDTEMVQ TTMNGQPYLA GKFAHTLRMR
LMREHLGVDV DILDVVERRF KRFENFVRSE EGIKYATNKF RNTENIYLSA MVEVASRDIL
QQHSGTRRWK RFIHISKLDA EIADVNFEEE ESEYPPPLFL PISFNNRTGP SEANKGIRDS
KKHSYDNRVQ NNEAHKLDVY GDGLDKYRTK LAKRARVSSA KFLSELSLLA MEDNPTGPFL
PDFDTVRDFL ESDDCHMHDE MDEESEKIIA ERNKERWLLL KKISYLQRVA AKEKSLSEEE
DEKRAKLGLP LLCKNGLPAS AGTANGGANG SAANATNILG TSEGIETDFS MDKEHPTVSL
SEPAAKEIIN NLTSPDASIS NFIDPYEFED PVGPDFYELR WNEIARRNTD LFRMVFHCQP
DDVVSRWSEY THFTKLQSYF MNAQDVEMNG KRSSEEIVVT EKLDEPETFE PRLANNTDVP
KDGLLGDEFG LLGRAPPVKG QEPKPEHEAT NLRAKLGRRV STFGSDRDKK SDHEQEHQQL
NEPVNEAENP IPEYEEDSPD LEKALTEDEV FDKSSGSPND VPKQPRSRQS SKIRRGRSTA
FLARRKIQSG DAIYDRTSAE RLLNAIQGHL VYFPTEWLDV ELRNNNWFYN TDRLPPMDIY
D
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