ID A0A0Q6M4Q5_9BURK Unreviewed; 556 AA.
AC A0A0Q6M4Q5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=ASC88_26240 {ECO:0000313|EMBL:KQU74915.1};
OS Rhizobacter sp. Root29.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736511 {ECO:0000313|EMBL:KQU74915.1, ECO:0000313|Proteomes:UP000051195};
RN [1] {ECO:0000313|EMBL:KQU74915.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU74915.1,
RC ECO:0000313|Proteomes:UP000051195};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQU74915.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU74915.1,
RC ECO:0000313|Proteomes:UP000051195};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KQU74915.1}.
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DR EMBL; LMCN01000016; KQU74915.1; -; Genomic_DNA.
DR RefSeq; WP_056815678.1; NZ_LMCN01000016.1.
DR AlphaFoldDB; A0A0Q6M4Q5; -.
DR STRING; 1736511.ASC88_26240; -.
DR OrthoDB; 9789376at2; -.
DR Proteomes; UP000051195; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR CDD; cd09172; PLDc_Nuc_like_unchar1_1; 1.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000051195}.
FT DOMAIN 436..467
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 556 AA; 60907 MW; 0CA788455B86EE5A CRC64;
MRVRNENGGL TAMAVAGTYV VLLGWDMPEA TLLAQGVLGF AVRRLRERDG ERIWLSGMKT
FEQVEPFPVP GEPVTSFLHP LQTFQWADYS ASPDERYVYT IVPMGGAPGA LVLGPGVDLA
VATERVDQGR HAVFFNRGAV ASQEYARRFQ NRPPDDAGPS AFNWLSRGLV EGLEAFIGQA
AQGDALEGAF FEFKSPRIYT ALKAAKARGA AVSVLYDGDS QGEGNEKALE GQGMDGMVKS
REHSGGFAHN KFLVLRQGGV PKQVWTGSTN LSVNGMFGHS NNAHIVRDDV IAARYHQYWR
LLDSDQTRKP TATQDEALSP LPADGSPLDA LFSPRLGLQA LDWYAGLAAG AKRGVFMTFA
FGMNSRFVPS YDKTDGVLRF ALMEKKGTGK TYKAQAAEID RIRRHPNVTV AVGNRVELNL
FDRWLAELDR IADEAHVLYV HTKYMLVDPL GDAPTVVVGS ANFSAASTTD NDENMLVIRG
DTAVADIYLG EFMRLFSHYA FRESLQFKDA TSDANALLRK YLVPSPDWIH GGGGAGQSYF
RAGSDRALRR LYFSGQ
//
