ID A0A2T7SXC9_9ACTN Unreviewed; 447 AA.
AC A0A2T7SXC9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=Y717_23445 {ECO:0000313|EMBL:PVE07568.1};
OS Streptomyces scopuliridis RB72.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1440053 {ECO:0000313|EMBL:PVE07568.1, ECO:0000313|Proteomes:UP000245992};
RN [1] {ECO:0000313|EMBL:PVE07568.1, ECO:0000313|Proteomes:UP000245992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB72 {ECO:0000313|EMBL:PVE07568.1,
RC ECO:0000313|Proteomes:UP000245992};
RA Olson J.B.;
RT "Annotated genome of Streptomyces scopuliridis.";
RL Submitted (DEC-2013) 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:PVE07568.1}.
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DR EMBL; AZSP01000275; PVE07568.1; -; Genomic_DNA.
DR RefSeq; WP_051745738.1; NZ_JOEI01000007.1.
DR AlphaFoldDB; A0A2T7SXC9; -.
DR STRING; 1440053.GCA_000718095_01892; -.
DR Proteomes; UP000245992; 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; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000245992};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..447
FT /note="phospholipase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015601156"
FT DOMAIN 98..238
FT /note="Phospholipase D-like"
FT /evidence="ECO:0000259|Pfam:PF13091"
FT DOMAIN 303..440
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"
SQ SEQUENCE 447 AA; 47975 MW; DE52A4C43356F6C8 CRC64;
MHRHRHRRIR LLGLAVALMS VVAVPGAAWA DGDDGSEFRA PSEAESPSRA ESPSPSRLPA
GAPGAPVTTG AIFNDPAGTT AQRNRIRDHV VSLVDGSAAG SSITLSLYTF TDDNVRKALI
AAKDRGVAVR AILDRKSHET VTAGGEYENL AAALGTDRAR PSWVMSCPSN RSCVGNRTIG
SRAINHNKFF LFSRTGGVEN VVVQTSANMT GTQRTDLFNN AVTIADPGLY DNYAAYFSDQ
LKYGASGSGL ATYYRTPSSA TDPAYKTYFF PRRETSGADY RKDPATDTVK LLLDKVACSS
TQHSEVRMAA NLFYRDQIAS KLVAMKNAGC LVYLAGDGNP NGGGAGVPSL GKTVTSIVSG
KLTQRVECWE DPPTSGAPKI GLHSKYVLVK GTYEGVANKK IVWTGSHNYS WQALRSNDET
LLKIDNAAVH DQYKANHDQL MRYCAGT
//