ID A0A0J1CL25_9BURK Unreviewed; 602 AA.
AC A0A0J1CL25;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=EOS_37000 {ECO:0000313|EMBL:KLU21244.1};
OS Caballeronia mineralivorans PML1(12).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU21244.1, ECO:0000313|Proteomes:UP000035963};
RN [1] {ECO:0000313|EMBL:KLU21244.1, ECO:0000313|Proteomes:UP000035963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX PubMed=26205858;
RA Uroz S., Oger P.;
RT "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT Ability.";
RL Genome Announc. 3:e00798-15(2015).
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}.
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:KLU21244.1}.
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DR EMBL; AEJF01000228; KLU21244.1; -; Genomic_DNA.
DR RefSeq; WP_047897180.1; NZ_AEJF01000228.1.
DR AlphaFoldDB; A0A0J1CL25; -.
DR PATRIC; fig|908627.4.peg.8300; -.
DR OrthoDB; 9789376at2; -.
DR Proteomes; UP000035963; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
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.
DR PROSITE; PS50035; PLD; 1.
PE 3: Inferred from homology;
FT DOMAIN 485..517
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 39..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 64462 MW; D3F670B8E18C2C34 CRC64;
MSAKCIALSN NDVILVAWTF EHKLVGCVGF DVRRVDASEA QTGSSAPQGV SLPAMAGFPS
NPDSGHAGQT TAQGPIQKFF WKDLYVSDAH AQGVYVYQII PLQGRFSKDA PPKLAPLEGA
PILYSNPVGL TAEHGPHEDP GAVKCYFNRG ILATQALARQ LPKSKSDLPD SGVLLKRIAD
PTDPLRKSLA GDLLTVLPSL LAEAKAHGGS CYAALYELAD KQLEASLVGN KQLHLILSNT
VDSTTHDDDK ENAPAREALH HSGVDVTDRM LPDGSHIGHN KFMLYVDARG KPDIVLTGST
NWTPTGLCAQ TNNSIVLRSP SLASAYSTYW DALKKDTLDA GTDPHALQSK AFRTANASPV
AVEIPGAKKA TLWFSPNTLQ KNKAKGVTPP DMADVYARIE GAKSAVLFLA FDPGQPSIVD
AAASAQEKNG KLFIRGALTN ADRAGNFVID LHNNNSTPAD PAQVIPTEGV NDAFGVWQKE
LAKVGHAVIH DKIVVIDPFD PDRCTVVVGS HNLGNKASST NDENFIIIEG NVSLACAYAV
HVIDVYDHYR WRYLLAQHGT QDSWQGLHED DTWQSAYFSP SGEPSNAELA FWLGASAAGK
GE
//
