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Database: UniProt
Entry: A0A5C4ND81_9RHOB
LinkDB: A0A5C4ND81_9RHOB
Original site: A0A5C4ND81_9RHOB 
ID   A0A5C4ND81_9RHOB        Unreviewed;       495 AA.
AC   A0A5C4ND81;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   02-APR-2025, entry version 25.
DE   RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00018392};
DE   AltName: Full=Choline phosphatase {ECO:0000256|ARBA:ARBA00029594};
GN   ORFNames=FHG71_15495 {ECO:0000313|EMBL:TNC67507.1};
OS   Rubellimicrobium roseum.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodobacterales; Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=687525 {ECO:0000313|EMBL:TNC67507.1, ECO:0000313|Proteomes:UP000305709};
RN   [1] {ECO:0000313|EMBL:TNC67507.1, ECO:0000313|Proteomes:UP000305709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 48858 {ECO:0000313|EMBL:TNC67507.1,
RC   ECO:0000313|Proteomes:UP000305709};
RA   Jiang L.;
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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:TNC67507.1}.
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DR   EMBL; VDFV01000028; TNC67507.1; -; Genomic_DNA.
DR   RefSeq; WP_139082610.1; NZ_VDFV01000028.1.
DR   AlphaFoldDB; A0A5C4ND81; -.
DR   OrthoDB; 8828485at2; -.
DR   Proteomes; UP000305709; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:TreeGrafter.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
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   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 metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000305709};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          137..164
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          352..379
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   495 AA;  55010 MW;  69162427154CFD81 CRC64;
     MDGDGVDARP ASDILRPGDT CWRIAHADRL RVIVDAADYF ATFRSVAQEA RHSLLLIGWD
     FDTRIELDRA DGHSEVPNRL GRFLSWLVRN RPNLQIHMLE WDVGLLLALG RGSTPLRVAD
     LVSSKRVRLQ LDHAHPAGAA HHQKIVVIDD VLAFCGGIDM TAGRWDTPAH QDHDPLRVSP
     TLGWRFPPWH DVTTVVDGDA ARALGDLARE RWRRACGEEV APPPPTAPIW PEGLVPTLED
     VEVGISRSAP DYDGRDGVRE IEALYLDIVK SARRHLYIES QYFASRRIAE AMAERLREPD
     GPEIVVVNPL SAQGWLEEEA MGSARAKLLR MVRRADRYGR FGLYTPVAKG GTPIYVHAKV
     VIMDDRLLRV GSSNLNNRSM GFDTECDLTV EVGPGDPDGA NRRRHIAALR ADLLAEHLGV
     RPDDVEVALA QAGGFLIGAI EALRSDGRSL VPFKPPELNA LEEEVLAENE LLDPERASRR
     WRPLSLPKRL PWSAA
//
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