ID A0A0Q9T3N6_9ACTN Unreviewed; 478 AA.
AC A0A0Q9T3N6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=ASG94_19710 {ECO:0000313|EMBL:KRF30240.1};
OS Nocardioides sp. Soil805.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736416 {ECO:0000313|EMBL:KRF30240.1, ECO:0000313|Proteomes:UP000051356};
RN [1] {ECO:0000313|EMBL:KRF30240.1, ECO:0000313|Proteomes:UP000051356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF30240.1,
RC ECO:0000313|Proteomes:UP000051356};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF30240.1, ECO:0000313|Proteomes:UP000051356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF30240.1,
RC ECO:0000313|Proteomes:UP000051356};
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:KRF30240.1}.
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DR EMBL; LMSU01000006; KRF30240.1; -; Genomic_DNA.
DR RefSeq; WP_056928203.1; NZ_LMSU01000006.1.
DR AlphaFoldDB; A0A0Q9T3N6; -.
DR STRING; 1736416.ASG94_19710; -.
DR OrthoDB; 3740959at2; -.
DR Proteomes; UP000051356; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..478
FT /note="phospholipase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006384003"
FT DOMAIN 113..255
FT /note="Phospholipase D-like"
FT /evidence="ECO:0000259|Pfam:PF13091"
FT REGION 32..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..59
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 52568 MW; DC81C3F33D813A3D CRC64;
MKSTRPITAA VAALALLAPL TFLATGANAG EPVAASAPTT TPTPTPTPTP TPTPVPTTTT
PTATPTTTPT EDPTQDATTT WHPRAGVRFN EPRDPAESHK INRYIRSAIA NTPKGQSMKL
VTWNFSNQLF VNDIIAAHKR GVSVRLIMAN GLAESQSRSN GYFWQVQRAL QKGNKKRPGY
LKSWARTCKN SCRGKEGIQH GKWFVFSRTG GRNLVVMSTS ANLTDAAAYN QWNDLLTVQG
RQGTYDAYVN VFKEMSRDRQ VKPAFKTFDD KNYDGWFFPQ MGPLRNHNVI RLLNKVKCTG
ARGDAGKNGK TVIRVSQAVF NGRPGSAIAG KLKKLKKAGC NVKLVYGVLN NNSRSLLKDI
PSRTILEDTN GDGFVDRYVH MKALTISGHY ARNRQAHVVY QGSANFSGMA TLSDEQGFII
NSKKLEQSYS KFINYLFKNP PPQGQDLIKE IVLRQAPGFD PFEKVRAEMG MGSMVPAE
//
