PLD_STRCW
ID PLD_STRCW Reviewed; 556 AA.
AC Q8KRU5;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Phospholipase D;
DE Short=PLD;
DE EC=3.1.4.4;
DE Contains:
DE RecName: Full=Phospholipase D catalytic chain;
DE Contains:
DE RecName: Full=Phospholipase D regulatory chain;
DE Flags: Precursor;
GN Name=pld;
OS Streptomyces chromofuscus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=42881;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32, ACTIVITY REGULATION, SUBUNIT,
RP PTM, AND CHARACTERIZATION OF PROTEOLYTICALLY CLEAVED PLD.
RX PubMed=15588701; DOI=10.1016/j.bbapap.2004.09.014;
RA Yang H., Roberts M.F.;
RT "Expression and characterization of a heterodimer of Streptomyces
RT chromofuscus phospholipase D.";
RL Biochim. Biophys. Acta 1703:43-51(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-556, CATALYTIC ACTIVITY, DOMAIN,
RP AND MUTAGENESIS OF HIS-118; CYS-169; HIS-217; HIS-233; HIS-246 AND HIS-272.
RC STRAIN=ATCC 23616 / INA 9052;
RX PubMed=12441393; DOI=10.1110/ps.0225302;
RA Yang H., Roberts M.F.;
RT "Cloning, overexpression, and characterization of a bacterial Ca2+-
RT dependent phospholipase D.";
RL Protein Sci. 11:2958-2968(2002).
RN [3]
RP PROTEIN SEQUENCE OF 47-66 AND 397-410, FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND
RP PTM.
RX PubMed=10082951; DOI=10.1016/s0167-4838(99)00005-9;
RA Geng D., Baker D.P., Foley S.F., Zhou C., Stieglitz K., Roberts M.F.;
RT "A 20-kDa domain is required for phosphatidic acid-induced allosteric
RT activation of phospholipase D from Streptomyces chromofuscus.";
RL Biochim. Biophys. Acta 1430:234-244(1999).
RN [4]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, AND MUTAGENESIS OF CYS-169;
RP ASP-197; TYR-200; HIS-258; GLU-259; ASP-435 AND HIS-437.
RX PubMed=12519726; DOI=10.1074/jbc.m210363200;
RA Zambonelli C., Roberts M.F.;
RT "An iron-dependent bacterial phospholipase D reminiscent of purple acid
RT phosphatases.";
RL J. Biol. Chem. 278:13706-13711(2003).
CC -!- FUNCTION: Catalyzes the hydrolysis of the ester bond between the
CC phosphatidic acid and alcohol moieties of phospholipids. Can catalyze a
CC transphosphatidylation reaction in the presence of high concentrations
CC of primary alcohols. Has also phosphatase activity toward p-nitrophenyl
CC phosphate. {ECO:0000269|PubMed:10082951, ECO:0000269|PubMed:12519726}.
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|PubMed:12441393};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:12519726};
CC Note=Binds 1 iron ion. Iron is essential for catalysis.
CC {ECO:0000269|PubMed:12519726};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:12519726};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12519726};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:12519726};
CC Note=Binds metal ions, iron, manganese or zinc. The ion could be
CC involved in the binding of substrate and/or the release of the product.
CC {ECO:0000269|PubMed:12519726};
CC -!- ACTIVITY REGULATION: Activated by calcium. Allosterically activated by
CC phosphatidic acid in the presence of calcium. Proteolytically cleaved
CC PLD is more active than the full-length enzyme, but is no longer
CC activated by phosphatidic acid. {ECO:0000269|PubMed:10082951,
CC ECO:0000269|PubMed:12519726, ECO:0000269|PubMed:15588701}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.05 mM for dihexanoyl-phosphatidylcholine (full-length form)
CC {ECO:0000269|PubMed:10082951};
CC KM=0.17 mM for dihexanoyl-phosphatidylcholine (proteolytically
CC cleaved form) {ECO:0000269|PubMed:10082951};
CC KM=0.5 mM for dihexanoyl-phosphatidylethanolamine (full-length form)
CC {ECO:0000269|PubMed:10082951};
CC KM=0.4 mM for dihexanoyl-phosphatidylethanolamine (proteolytically
CC cleaved form) {ECO:0000269|PubMed:10082951};
CC KM=0.6 mM for dihexanoyl-phosphatidylserine (full-length form)
CC {ECO:0000269|PubMed:10082951};
CC KM=4.5 mM for dihexanoyl-phosphatidylserine (proteolytically cleaved
CC form) {ECO:0000269|PubMed:10082951};
CC Vmax=61.5 umol/min/mg enzyme with dihexanoyl-phosphatidylcholine as
CC substrate (full-length form) {ECO:0000269|PubMed:10082951};
CC Vmax=130.0 umol/min/mg enzyme with dihexanoyl-phosphatidylcholine as
CC substrate (proteolytically cleaved form)
CC {ECO:0000269|PubMed:10082951};
CC Vmax=75.0 umol/min/mg enzyme with dihexanoyl-phosphatidylethanolamine
CC as substrate (full-length form) {ECO:0000269|PubMed:10082951};
CC Vmax=128.2 umol/min/mg enzyme with dihexanoyl-
CC phosphatidylethanolamine as substrate (proteolytically cleaved form)
CC {ECO:0000269|PubMed:10082951};
CC Vmax=41.3 umol/min/mg enzyme with dihexanoyl-phosphatidylserine as
CC substrate (full-length form) {ECO:0000269|PubMed:10082951};
CC Vmax=282.6 umol/min/mg enzyme with dihexanoyl-phosphatidylserine as
CC substrate (proteolytically cleaved form)
CC {ECO:0000269|PubMed:10082951};
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:10082951};
CC -!- SUBUNIT: Full-length phospholipase D is a monomer in solution.
CC Proteolytically cleaved PLD is a heterodimer composed of one
CC phospholipase D catalytic chain and one phospholipase D regulatory
CC chain. {ECO:0000269|PubMed:10082951, ECO:0000269|PubMed:15588701}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10082951}.
CC -!- DOMAIN: The N-terminal region contains the catalytic domain and the C-
CC terminal region contains regulatory elements.
CC {ECO:0000269|PubMed:10082951, ECO:0000269|PubMed:12441393}.
CC -!- PTM: In late stationary phase, is proteolytically cleaved to a more
CC active form where the two parts of the molecule (phospholipase D
CC catalytic chain and phospholipase D regulatory chain) are still tightly
CC associated.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the PhoD family. {ECO:0000305}.
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DR EMBL; AF523823; AAM77916.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KRU5; -.
DR SMR; Q8KRU5; -.
DR BindingDB; Q8KRU5; -.
DR BRENDA; 3.1.4.4; 5993.
DR SABIO-RK; Q8KRU5; -.
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 CDD; cd07389; MPP_PhoD; 1.
DR Gene3D; 3.60.21.70; -; 1.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR018946; PhoD-like_MPP.
DR InterPro; IPR038607; PhoD-like_sf.
DR InterPro; IPR032093; PhoD_N.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF09423; PhoD; 1.
DR Pfam; PF16655; PhoD_N; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Direct protein sequencing; Hydrolase; Lipid degradation;
KW Lipid metabolism; Secreted; Signal.
FT SIGNAL 1..46
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:10082951"
FT CHAIN 47..556
FT /note="Phospholipase D"
FT /id="PRO_5000063969"
FT CHAIN 47..396
FT /note="Phospholipase D catalytic chain"
FT /id="PRO_0000398873"
FT CHAIN 397..556
FT /note="Phospholipase D regulatory chain"
FT /id="PRO_0000398874"
FT MUTAGEN 118
FT /note="H->N: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:12441393"
FT MUTAGEN 169
FT /note="C->A: Loss of activity and strongly reduced content
FT of iron. No change in secondary structure and
FT thermostability."
FT /evidence="ECO:0000269|PubMed:12441393,
FT ECO:0000269|PubMed:12519726"
FT MUTAGEN 169
FT /note="C->S: Loss of activity. No change in secondary
FT structure and thermostability."
FT /evidence="ECO:0000269|PubMed:12441393,
FT ECO:0000269|PubMed:12519726"
FT MUTAGEN 197
FT /note="D->A: Almost complete loss of activity and strongly
FT reduced content of iron, but little change in secondary
FT structure."
FT /evidence="ECO:0000269|PubMed:12519726"
FT MUTAGEN 200
FT /note="Y->F: Almost complete loss of activity and strongly
FT reduced content of iron, but little change in secondary
FT structure."
FT /evidence="ECO:0000269|PubMed:12519726"
FT MUTAGEN 217
FT /note="H->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:12441393"
FT MUTAGEN 233
FT /note="H->A: Loss of activity. Altered secondary
FT structure."
FT /evidence="ECO:0000269|PubMed:12441393"
FT MUTAGEN 233
FT /note="H->N: No change in activity."
FT /evidence="ECO:0000269|PubMed:12441393"
FT MUTAGEN 246
FT /note="H->A: Loss of activity. Altered secondary
FT structure."
FT /evidence="ECO:0000269|PubMed:12441393"
FT MUTAGEN 246
FT /note="H->N: No change in activity."
FT /evidence="ECO:0000269|PubMed:12441393"
FT MUTAGEN 258
FT /note="H->A: Little effect on metal content, visible
FT absorption spectrum and on activity."
FT /evidence="ECO:0000269|PubMed:12519726"
FT MUTAGEN 259
FT /note="E->A: Little effect on metal content, visible
FT absorption spectrum and on activity."
FT /evidence="ECO:0000269|PubMed:12519726"
FT MUTAGEN 272
FT /note="H->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:12441393"
FT MUTAGEN 435
FT /note="D->A: Little effect on metal content, visible
FT absorption spectrum and on activity."
FT /evidence="ECO:0000269|PubMed:12519726"
FT MUTAGEN 437
FT /note="H->A: Almost complete loss of activity and strongly
FT reduced content of iron, but little change in secondary
FT structure."
FT /evidence="ECO:0000269|PubMed:12519726"
FT CONFLICT 47..50
FT /note="TTGT -> ADQA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="L -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 59646 MW; 8ECE96B420441FA1 CRC64;
MTSRYRSSEA HQGLASFSPR RRTVVKAAAA TAVLAGPLAA ALPARATTGT PAFLHGVASG
DPLPDGVLLW TRVTPTADAT PGSGLGPDTE VGWTVATDKA FTNVVAKGST TATAASDHTV
KADIRGLAPA TDHWFRFSAG GTDSPAGRAR TAPAADAAVA GLRFGVVSCA NWEAGYFAAY
RHLAARGDLD AWLHLGDYIY EYGAGEYGTR GTSVRSHAPA HEILTLADYR VRHGRYKTDP
DLQALHAAAP VVAIWDDHEI ANDTWSGGAE NHTEGVEGAW AARQAAAKQA YFEWMPVRPA
IAGTTYRRLR FGKLADLSLL DLRSFRAQQV SLGDGDVDDP DRTLTGRAQL DWLKAGLKSS
DTTWRLVGNS VMIAPFAIGS LSAELLKPLA KLLGLPQEGL AVNTDQWDGY TDDRRELLAH
LRSNAIRNTV FLTGDIHMAW ANDVPVNAGT YPLSASAATE FVVTSVTSDN LDDLVKVPEG
TVSALASPVI RAANRHVHWV DTDRHGYGVL DITAERAQMD YYVLSDRTQA GATASWSRSY
RTRSGTQRVE RTYDPE
