ID A0A0Q9Q5G9_9ACTN Unreviewed; 485 AA.
AC A0A0Q9Q5G9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Phospholipase {ECO:0000313|EMBL:KRE95451.1};
GN ORFNames=ASG76_07325 {ECO:0000313|EMBL:KRE95451.1};
OS Nocardioides sp. Soil774.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736408 {ECO:0000313|EMBL:KRE95451.1, ECO:0000313|Proteomes:UP000051100};
RN [1] {ECO:0000313|EMBL:KRE95451.1, ECO:0000313|Proteomes:UP000051100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil774 {ECO:0000313|EMBL:KRE95451.1,
RC ECO:0000313|Proteomes:UP000051100};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE95451.1, ECO:0000313|Proteomes:UP000051100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil774 {ECO:0000313|EMBL:KRE95451.1,
RC ECO:0000313|Proteomes:UP000051100};
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 -!- 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:KRE95451.1}.
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DR EMBL; LMSM01000006; KRE95451.1; -; Genomic_DNA.
DR RefSeq; WP_056601935.1; NZ_LMSM01000006.1.
DR AlphaFoldDB; A0A0Q9Q5G9; -.
DR STRING; 1736408.ASG76_07325; -.
DR OrthoDB; 8828485at2; -.
DR Proteomes; UP000051100; 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; cd09105; PLDc_vPLD1_2_like_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; 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}.
FT DOMAIN 118..151
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 358..385
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 147..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 54776 MW; 4F91822F1E81011F CRC64;
MNDWFLPETE RPWTSGNHVV PRVHGADYFA RLVEVVGATG AGDRIFFTDW RGDSDERLTD
DGPTVGELLK SAVARGVEVR ALMWRSHPGQ LNGEENGHLG RILNECGGEA LLDERVRRGG
SHHQKLLVVR RKDHPDQDVA FVGGIDLSHG RRDDASHAGD PQAPPLDDRY GDTPPWHDAM
AEIRGPAVAH VLDTFTERWD DGTPLDHRNP YRATAHRIAR MPRHPESLPE RWDPPPEAGR
HKVQVLRTYP AKRPAYPFAP HGERSIARAY SRAFGRARRL VYIEDQYFWS EVVAATLADA
LRREPGLHVI AVVPRFPEED NRVAGPPMLH GQRLAWQRLR DAGGDRFEMF DLHNDAGTPV
YVHAKVCIVD DAWMTIGSDN LNLRSWTHDS ELTCAVVDPD GELPRSLRTT LWAEHLGLPA
DDERLLDIDD PMTLWRSRVG APGSRIGVHE PPELPRRTRA WARTAYRLFY DPDGRPRPLR
GTGDF
//
