ID D3P5X2_AZOS1 Unreviewed; 759 AA.
AC D3P5X2;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00018392};
DE AltName: Full=Choline phosphatase {ECO:0000256|ARBA:ARBA00029594};
GN Name=pld {ECO:0000313|EMBL:BAI76051.1};
GN OrderedLocusNames=AZL_d02250 {ECO:0000313|EMBL:BAI76051.1};
OS Azospirillum sp. (strain B510).
OG Plasmid pAB510d {ECO:0000313|EMBL:BAI76051.1,
OG ECO:0000313|Proteomes:UP000002040}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI76051.1, ECO:0000313|Proteomes:UP000002040};
RN [1] {ECO:0000313|EMBL:BAI76051.1, ECO:0000313|Proteomes:UP000002040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B510 {ECO:0000313|EMBL:BAI76051.1,
RC ECO:0000313|Proteomes:UP000002040};
RC PLASMID=pAB510d {ECO:0000313|EMBL:BAI76051.1};
RX PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA Nakayama S., Yamada M., Tabata S., Sato S.;
RT "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT sp. B510.";
RL DNA Res. 17:37-50(2010).
CC -!- FUNCTION: Could be a virulence factor. {ECO:0000256|ARBA:ARBA00003145}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; AP010950; BAI76051.1; -; Genomic_DNA.
DR AlphaFoldDB; D3P5X2; -.
DR KEGG; azl:AZL_d02250; -.
DR HOGENOM; CLU_011094_0_0_5; -.
DR OrthoDB; 8828485at2; -.
DR Proteomes; UP000002040; Plasmid pAB510d.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004630; F:phospholipase D activity; IEA:RHEA.
DR GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR CDD; cd09140; PLDc_vPLD1_2_like_bac_1; 1.
DR CDD; cd09143; PLDc_vPLD1_2_like_bac_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 InterPro; IPR032816; VTT_dom.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF09335; SNARE_assoc; 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, ECO:0000313|EMBL:BAI76051.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Plasmid {ECO:0000313|EMBL:BAI76051.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002040};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 570..595
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 680..702
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 714..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 156..183
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 386..408
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 186..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..258
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 83491 MW; 3BC2099D41AFC1E8 CRC64;
MDAPSPRPLL SAGPMPAATE SDAVAPAAVA RPILQPGRTC WRVEDTGRLG VIVDAENYFA
LAKAAMRRAR RSIYLTAWDF DARIRLMPQT RRPRRPDRLG TLLNWLATTR PDLHIHVLKW
DYAELFDIAR WSHPFMLRNW LTHRRLQYRL DGDHPTGACH HQKLLVIDDR LAFCGGLDIT
ANRWDSRAHH GHDPRRRQPD GRPYEPFHDV MMAVDGDAAR ALGEMFRDRW ARATGERLTP
PAPKPGRPAR RHPLAADPWP PGFEPLLRDV RVGIARTDPA CNGREEVREV EALHLAAIAA
AREVIYLESQ YFASTAVAEA LKARLSEEDG PEVIIVNPVR TTSWLENTVM LGVRARLSRE
LREADRHGRF HLFAALTDNG ACITVHAKVM VVDDRLLRIG SANLNNRSMG LDTECDLALE
AGPGPEHAET RRAIRHTRDD LIAEHLGTSP EQVAAARRRL GSLGAAIASL RRPVGRRLEP
LHDPEPEGLA AAVADARVFD PEHPVDAVEI VRRVLPSRIP RTRHWLTLAG ILALLGLWGM
WRYGALSDWA SLDAVLAVFH GLGDSPLTPL WLMLAYVAGG YVMFPLTVLI AATAIVMGPW
WGFPTAMAGA VASAVAMFWT GRVAGRDLLD RHGGPLIASL NQRLSDGGIL AVAGVRAVPV
APYTVVNLAA GASKLRFDDY LIGTMVGLAP GILAFTLLGR QLERTLTHPD AGDVALLAAM
AAVAIGLGWL TGRLLGRGRN PVRQDERADE RPKGRNLKP
//
