ID A0A0T1WHR3_9MYCO Unreviewed; 329 AA.
AC A0A0T1WHR3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=ASD37_30365 {ECO:0000313|EMBL:KQY08611.1};
OS Mycobacterium sp. Root135.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1736457 {ECO:0000313|EMBL:KQY08611.1, ECO:0000313|Proteomes:UP000051127};
RN [1] {ECO:0000313|EMBL:KQY08611.1, ECO:0000313|Proteomes:UP000051127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root135 {ECO:0000313|EMBL:KQY08611.1,
RC ECO:0000313|Proteomes:UP000051127};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY08611.1, ECO:0000313|Proteomes:UP000051127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root135 {ECO:0000313|EMBL:KQY08611.1,
RC ECO:0000313|Proteomes:UP000051127};
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:KQY08611.1}.
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DR EMBL; LMEZ01000002; KQY08611.1; -; Genomic_DNA.
DR RefSeq; WP_056550094.1; NZ_LMEZ01000002.1.
DR AlphaFoldDB; A0A0T1WHR3; -.
DR STRING; 1736457.ASD37_30365; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000051127; 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; cd09127; PLDc_unchar1_1; 1.
DR CDD; cd09128; PLDc_unchar1_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 PANTHER; PTHR43856; CARDIOLIPIN HYDROLASE; 1.
DR PANTHER; PTHR43856:SF1; MITOCHONDRIAL CARDIOLIPIN HYDROLASE; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051127}.
FT DOMAIN 91..118
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 243..270
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 304..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 329 AA; 36954 MW; A464689CEECB10A6 CRC64;
MQPLGPRLIV QPDDGLGPVL EFIGSAQTSL LIKQFTFTDE SLIDAVVARK QAGVDVRVML
NAARSGGDRA NDETFERFCA AGISVQWANP KFYVTHEKSM VVDEKSALVA TFNMCLKYFT
RTRDYGVIID DPVQVTQIVE VFNADWNHDD WVPTVYRGLL WSNSNSRLHM ARFIDTATHR
IDVQHPKFVD AVITDHLAAA IDRGVKVHVL CGGRHGISEG DVLDTFASLR TLRRFGAKVH
KQKNLRVHAK LMIVDDERAL VGSMNIDRSA FDLRRELGIT VDDPAVVARL RAVFEEDWAL
SHPYSPPDPL DPSTHHEDDF PHDPELVHE
//
