ID G3AC71_9RALS Unreviewed; 587 AA.
AC G3AC71;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=RALSY_mp30465 {ECO:0000313|EMBL:CCA87145.1};
OS Ralstonia syzygii R24.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=907261 {ECO:0000313|EMBL:CCA87145.1};
RN [1] {ECO:0000313|EMBL:CCA87145.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R24 {ECO:0000313|EMBL:CCA87145.1};
RX PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT solanacearum strains form a single genomic species despite divergent
RT lifestyles.";
RL PLoS ONE 6:e24356-e24356(2011).
RN [2] {ECO:0000313|EMBL:CCA87145.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R24 {ECO:0000313|EMBL:CCA87145.1};
RA Genoscope - CEA;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664}.
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DR EMBL; FR854092; CCA87145.1; -; Genomic_DNA.
DR AlphaFoldDB; G3AC71; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd09172; PLDc_Nuc_like_unchar1_1; 1.
DR CDD; cd09173; PLDc_Nuc_like_unchar1_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR025202; PLD-like_dom.
DR PANTHER; PTHR43856; CARDIOLIPIN HYDROLASE; 1.
DR PANTHER; PTHR43856:SF1; MITOCHONDRIAL CARDIOLIPIN HYDROLASE; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
PE 3: Inferred from homology;
FT DOMAIN 190..333
FT /note="Phospholipase D-like"
FT /evidence="ECO:0000259|Pfam:PF13091"
FT DOMAIN 475..525
FT /note="Phospholipase D-like"
FT /evidence="ECO:0000259|Pfam:PF13091"
SQ SEQUENCE 587 AA; 63376 MW; FB7AC3FDFEAE1EF5 CRC64;
MPASIDSFQV KVYQGDSAVL FAFDVAEADR AGLAGFAIQC TPQGQAPYWV PNRLTFDTPV
HADAPLRAGK YADSIDAPFQ SFHWVHFPPH AAGQYRYTVH ARYFVSTDPV QLETRAIHTI
GVTLKTPMTD WATVGMVRGY VSSQAFIDHC GGNTALAPDN RAQAKSPLLY DTQPYRDQYA
YLGATGRQLI IDLLNQCKAS DGYGIDVLAY DLDEPDIIRA FAWLAQQGRK VRVIQDDSVG
TGAHPTGHGT PDAFETQAVA LFGQAGAEVR RTHLARFQHH KAILLRDAAG KPVRVLAGSA
NLSLRGLYVQ ANSVLVFGQD AAQLYAEVFD RLWDLIGGED GAVPGSQVAA GFRKDALAAD
WHPVPPTGTP RARFAFSPHQ TDALLTEAAD RVRNAASSVL FAVMATDGGG AMVDTLEHVV
PQTAGLLSLG VIDKAGGVSA FAPGRDVPSQ TVSFAYLKDE APAPFKQEVD AGTGQHIHHK
FVVCDFNGEQ PVVFCGSSNL SRGGEEQNGD SLIAIHDPAI VTAYAIEAVR LFDHYRFRAS
QSKATAANPL VLKTTDAWAD PYYDPHNIKF TERTLFAQST EREAALA
//