PLD_STRAT
ID PLD_STRAT Reviewed; 556 AA.
AC Q53728;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Phospholipase D {ECO:0000303|PubMed:7765769};
DE EC=3.1.4.4 {ECO:0000269|Ref.2};
DE AltName: Full=Choline phosphatase;
DE Flags: Precursor;
OS Streptomyces antibioticus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1890;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-60; 225-231;
RP 300-312; 325-339; 414-432; 489-524 AND 530-538, AND SUBCELLULAR LOCATION.
RX PubMed=7765769; DOI=10.1007/bf00902731;
RA Iwasaki Y., Nakano H., Yamane T.;
RT "Phospholipase D from Streptomyces antibioticus: cloning, sequencing,
RT expression, and relationship to other phospholipases.";
RL Appl. Microbiol. Biotechnol. 42:290-299(1994).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, DISULFIDE BOND, AND
RP BIOTECHNOLOGY.
RC STRAIN=S-170;
RX DOI=10.1271/BBB.57.1946;
RA Shimbo K., Iwasaki Y., Yamane T., Ina K.;
RT "Purification and properties of phospholipase D of Streptomyces
RT antibioticus.";
RL Biosci. Biotechnol. Biochem. 57:1946-1948(1993).
RN [3] {ECO:0007744|PDB:2ZE4}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 48-556.
RA Suzuki A., Kakuno K., Saito R., Iwasaki Y., Yamane T., Yamane T.;
RT "Crystal structure of phospholipase D from streptomyces antibioticus.";
RL Submitted (DEC-2007) to the PDB data bank.
RN [4] {ECO:0007744|PDB:2ZE9}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 48-556.
RA Suzuki A., Toda H., Iwasaki Y., Yamane T., Yamane T.;
RT "Crystal structure of phospholipase D from streptomyces antibioticus.";
RL Submitted (DEC-2007) to the PDB data bank.
CC -!- FUNCTION: A reversible phospholipase active on phosphatidylcholine (PC)
CC and phosphatidylethanolamine. Lysophosphatidylcholine and egg
CC sphingomyelin are hydrolyzed about 50 times and 100 times more slowly
CC than PC, respectively. During the transphosphatidylation reaction
CC straight-chain hydroxy compounds, such as triethyleneglycol and
CC triethyleneglycol monomethyl ether, were phosphatidylated in good
CC yield, as were monosaccharides. Disaccharides and sugar alcohol reacted
CC slowly, while N-acetyl-D-galactosamine, D-galactosamine and D-
CC galacturonic acid were not phosphatidylated. {ECO:0000269|Ref.2}.
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:0000269|Ref.2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14446;
CC Evidence={ECO:0000269|Ref.2};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14447;
CC Evidence={ECO:0000269|Ref.2};
CC -!- ACTIVITY REGULATION: Inhibited by mercaptoethanol and dithiothreitol.
CC {ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5 in both directions. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius in both directions.
CC {ECO:0000269|Ref.2};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7765769,
CC ECO:0000269|Ref.2}.
CC -!- PTM: Probably has at least 1 disulfide bond. {ECO:0000305|Ref.2}.
CC -!- BIOTECHNOLOGY: May be useful in the production of emulsifiers.
CC {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
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DR EMBL; D16444; BAA03913.1; -; Genomic_DNA.
DR PDB; 2ZE4; X-ray; 2.50 A; A=48-556.
DR PDB; 2ZE9; X-ray; 2.30 A; A=48-556.
DR PDB; 7JRB; X-ray; 2.49 A; A=48-556.
DR PDB; 7JRC; X-ray; 2.01 A; A=48-556.
DR PDB; 7JRU; X-ray; 2.21 A; A=48-556.
DR PDB; 7JRV; X-ray; 2.42 A; A=48-556.
DR PDB; 7JRW; X-ray; 1.99 A; A=48-556.
DR PDB; 7JS5; X-ray; 2.50 A; A=48-556.
DR PDB; 7JS7; X-ray; 2.30 A; A/B=48-556.
DR PDBsum; 2ZE4; -.
DR PDBsum; 2ZE9; -.
DR PDBsum; 7JRB; -.
DR PDBsum; 7JRC; -.
DR PDBsum; 7JRU; -.
DR PDBsum; 7JRV; -.
DR PDBsum; 7JRW; -.
DR PDBsum; 7JS5; -.
DR PDBsum; 7JS7; -.
DR AlphaFoldDB; Q53728; -.
DR SMR; Q53728; -.
DR DrugBank; DB08376; (2R)-3-(phosphonooxy)propane-1,2-diyl diheptanoate.
DR BRENDA; 3.1.4.4; 5974.
DR EvolutionaryTrace; Q53728; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50035; PLD; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Repeat; Secreted; Signal.
FT SIGNAL 1..47
FT /evidence="ECO:0000269|PubMed:7765769"
FT CHAIN 48..556
FT /note="Phospholipase D"
FT /id="PRO_0000024657"
FT DOMAIN 210..237
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 484..511
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 326..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 57
FT /note="D -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="S -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:7JRW"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:7JRW"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 110..124
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 141..156
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:7JRW"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:2ZE4"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:7JRW"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:2ZE9"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 255..274
FT /evidence="ECO:0007829|PDB:7JRW"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 309..319
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:7JRW"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 363..373
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 376..384
FT /evidence="ECO:0007829|PDB:7JRW"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 398..409
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:2ZE9"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:2ZE9"
FT HELIX 439..453
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 456..466
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:7JRC"
FT STRAND 491..495
FT /evidence="ECO:0007829|PDB:7JRW"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:7JRW"
FT STRAND 512..520
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 522..531
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 533..540
FT /evidence="ECO:0007829|PDB:7JRW"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:7JRW"
SQ SEQUENCE 556 AA; 58932 MW; B388F0BDC8C0A596 CRC64;
MTSDQRPARL PTHKGKLLAP HRLHRLIPVS VALTTVCAAL PSSTAYAADT PPTPHLDAIE
RSLRDTSPGL EGSVWQRTDG NRLDAPDGDP AGWLLQTPGC WGDAGCKDRA GTRRLLDKMT
RNIADARHTV DISSLAPFPN GGFEDAVVDG LKAVVAAGHS PRVRILVGAA PIYHLNVVPS
RYRDELIGKL GAAAGKVTLN VASMTTSKTS LSWNHSKLLV VDGKTAITGG INGWKDDYLD
TAHPVSDVDM ALSGPAAASA GKYLDTLWDW TCRNASDPAK VWLATSNGAS CMPSMEQDEA
GSAPAEPTGD VPVIAVGGLG VGIKESDPSS GYHPDLPTAP DTKCTVGLHD NTNADRDYDT
VNPEENALRS LIASARSHVE ISQQDLNATC PPLPRYDIRT YDTLAGKLAA GVKVRIVVSD
PANRGAVGSG GYSQIKSLDE ISDTLRTRLV ALTGDNEKAS RALCGNLQLA SFRSSDAAKW
ADGKPYALHH KLVSVDDSAF YIGSKNLYPA WLQDFGYIVE SPAAAQQLKT ELLDPEWKYS
QQAAATPAGC PARQAG
