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Database: UniProt
Entry: G7JB30_MEDTR
LinkDB: G7JB30_MEDTR
Original site: G7JB30_MEDTR 
ID   G7JB30_MEDTR            Unreviewed;       822 AA.
AC   G7JB30;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
GN   Name=11436615 {ECO:0000313|EnsemblPlants:AES73658};
GN   OrderedLocusNames=MTR_3g107360 {ECO:0000313|EMBL:AES73658.1};
GN   ORFNames=MtrunA17_Chr3g0137821 {ECO:0000313|EMBL:RHN70646.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:AES73658.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:AES73658.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES73658.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES73658,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:AES73658.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES73658,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:AES73658}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES73658};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
RN   [4] {ECO:0000313|Proteomes:UP000265566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|Proteomes:UP000265566};
RX   PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA   Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA   Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA   Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA   Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA   Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA   Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT   "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL   Nat. Plants 4:1017-1025(2018).
RN   [5] {ECO:0000313|EMBL:RHN70646.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:RHN70646.1};
RA   Pecrix Y., Gamas P., Carrere S.;
RT   "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL   Nat. Plants 0:0-0(2018).
CC   -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC       phosphodiesteric bond. {ECO:0000256|PIRNR:PIRNR036470}.
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:PIRNR036470};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913,
CC         ECO:0000256|PIRNR:PIRNR036470};
CC   -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC       {ECO:0000256|ARBA:ARBA00010683, ECO:0000256|PIRNR:PIRNR036470}.
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DR   EMBL; CM001219; AES73658.1; -; Genomic_DNA.
DR   EMBL; PSQE01000003; RHN70646.1; -; Genomic_DNA.
DR   RefSeq; XP_003603407.1; XM_003603359.2.
DR   AlphaFoldDB; G7JB30; -.
DR   STRING; 3880.G7JB30; -.
DR   PaxDb; 3880-AES73658; -.
DR   EnsemblPlants; AES73658; AES73658; MTR_3g107360.
DR   GeneID; 11436615; -.
DR   Gramene; AES73658; AES73658; MTR_3g107360.
DR   KEGG; mtr:11436615; -.
DR   eggNOG; KOG1329; Eukaryota.
DR   HOGENOM; CLU_004684_0_0_1; -.
DR   OMA; RIYCAHT; -.
DR   OrthoDB; 875955at2759; -.
DR   Proteomes; UP000002051; Chromosome 3.
DR   Proteomes; UP000265566; Chromosome 3.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0004630; F:phospholipase D activity; IBA:GO_Central.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR   GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR   CDD; cd04015; C2_plant_PLD; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR024632; PLipase_D_C.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   InterPro; IPR011402; PLipase_D_pln.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR18896:SF204; PHOSPHOLIPASE D ALPHA 3; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF12357; PLD_C; 1.
DR   Pfam; PF00614; PLDc; 2.
DR   PIRSF; PIRSF036470; PLD_plant; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRNR:PIRNR036470};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036470};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR036470};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR036470};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051}.
FT   DOMAIN          1..134
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          336..373
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          664..691
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   822 AA;  93519 MW;  9F662A5E17462245 CRC64;
     MPQLLHGTLK VTISEVDRLQ AGCNLDFIRK GTTHKGKRFL AQVKGCILCR PEIVGTRLYA
     TVDLDKARVG RTRMIGNQPS NPKWNETFEI YCAHYISNIV FTVKDDNPIG ATLIGRAYIP
     SEKILKGPII DRWVEILDEE DHRPVPGGSK IRVSMQFSSV IEDRKCLWSQ GIHMPFLGVQ
     RTFFDQRQGC SVTLYQDAHV PESVHPWIPI SGTKYYVPGR CWEDIYNAIM NAKVFIYITG
     WSVHTEITLI RDPNKTTESS ITLGEMLKKK ANEGVNVLVL VWDDRTSVPA FKKDGLMGTH
     DQETAEYFKN TKVHCVLCPR NPDGGKSIVQ GFETSTMFTH HQKTIVVDGH HVEASQKRTV
     ISFIGGIDLC DGRYDTMEHP LFSTLNTIHH DDFHQPNFPG ASIKKGGPRE PWHDIHCKLE
     GPIAWDVLYN FEQRWEKQVG KQFLFPIEVL DRILIHPSDA MLSEEDGETW SVQLFRSIDG
     GAVSNFPQAP NEVIELGLVS GKDNIIDRSI QDAYINAIRR AKNFIYIENQ YFLGSSYGWH
     STDIKVEDIG ALHLIPKELS LKIISKIEAG ERFVVYVVIP MWPEGIPESA SVQAILDWQR
     RTMEMMYTEI ADAIKKKNIE AHPRDYLTFY CLGKRESKKD GEYTPPEEPA PDSDYHRAQK
     SRRFMIYVHS KMMIVDDEYI VIGSANINQR SMDGGRDTEI AMGAFQPHHL ASTSNGSQRP
     QGQVYGFRRA LWYEHIGDNS DDFDEPERLE CVKLLNRVAE RNWKLYCDDA LDESVNTHLL
     RYPVEVGEDG SVTSLSGMQY FPDTMALILG SKSDYLPPIL TT
//
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