ID J2VUY0_9BURK Unreviewed; 192 AA.
AC J2VUY0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=PMI40_00290 {ECO:0000313|EMBL:EJN10027.1};
OS Herbaspirillum sp. YR522.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1144342 {ECO:0000313|EMBL:EJN10027.1, ECO:0000313|Proteomes:UP000007507};
RN [1] {ECO:0000313|EMBL:EJN10027.1, ECO:0000313|Proteomes:UP000007507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR522 {ECO:0000313|EMBL:EJN10027.1,
RC ECO:0000313|Proteomes:UP000007507};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJN10027.1}.
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DR EMBL; AKJA01000010; EJN10027.1; -; Genomic_DNA.
DR RefSeq; WP_008111271.1; NZ_AKJA01000010.1.
DR AlphaFoldDB; J2VUY0; -.
DR STRING; 1144342.PMI40_00290; -.
DR PATRIC; fig|1144342.3.peg.234; -.
DR eggNOG; COG1502; Bacteria.
DR OrthoDB; 5294698at2; -.
DR Proteomes; UP000007507; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
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; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR PROSITE; PS50035; PLD; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007507};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..192
FT /note="phospholipase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003757035"
FT DOMAIN 125..156
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 192 AA; 21042 MW; 57B00B13249CD8CA CRC64;
MRTITCRAWS LAALLLLASV GGAQARSLAP AAPPVLQARG TVQVAFAPWD DIEGIIIARL
ADARRQVLMQ AYLLTNRRIV DALIAAHARG IDVQVMMDRG QLDKNSTERL RQLRAAAIPV
WFETLYRSAH NKVIVIDAGQ PTAAVITGSF NFTWSAQHRN AENIVVLAGD DALVARYAAN
WQRHREDAEV AP
//
