ID A0A085VH66_PSESX Unreviewed; 605 AA.
AC A0A085VH66;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Phospholipase {ECO:0000313|EMBL:KFE54779.1};
GN ORFNames=IV01_15095 {ECO:0000313|EMBL:KFE54779.1};
OS Pseudomonas syringae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=317 {ECO:0000313|EMBL:KFE54779.1, ECO:0000313|Proteomes:UP000028631};
RN [1] {ECO:0000313|EMBL:KFE54779.1, ECO:0000313|Proteomes:UP000028631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAW0119 {ECO:0000313|EMBL:KFE54779.1,
RC ECO:0000313|Proteomes:UP000028631};
RA Baltrus D.A., Berge O., Morris C.;
RT "Draft Genome Sequences of Environmental Pseudomonas syringae strains.";
RL Submitted (JUL-2014) 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:KFE54779.1}.
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DR EMBL; JPQU01000041; KFE54779.1; -; Genomic_DNA.
DR RefSeq; WP_032629336.1; NZ_JPQU01000041.1.
DR AlphaFoldDB; A0A085VH66; -.
DR PATRIC; fig|317.175.peg.3141; -.
DR OrthoDB; 8828485at2; -.
DR Proteomes; UP000028631; 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; 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; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 495..522
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 244..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 68415 MW; AC3DDAD90188236A CRC64;
MNQSDIVTPA ALQHTNEVTC ASPWYVLKTK YRPAKATYQP LVNGEEAFRA VHMAVAKASK
TIDIICWGFQ PSMFFIRDSC TPSIGELLMI KASEGVKVRV LGWEFPLNLA GAAGETNLPG
KGKLRILQRE LQHTTEDQYA YDKYWYATCA VSGNKAAGHD PRLPVFVGRG FSWQERGEIS
HWVKYQGLDP DISAKMRYVM KLAPSHHQKT VLVDYQVPDR AVGFVMGHNM LDEYWDTDKH
SALNRTENTK PAPNVGPRGK EPRQDISCQL SGPILEHLHH NFATAWFNET GEDLLGPREA
KQVGPVLQCA PEVTRQLAQI VRTQPQEKAL DIEQLYLKAV NNATRFIYIE NQYFRWPPLA
KLINEVAERQ IKGGVDPGKE GALHLFVITN ASDDGMGKGT VKTQRMLETL GRADTMPNVT
KLQRIEEVKH NAPPRPRPDL RDQVGQRELK QWQAALDRQI KEINDSTIDV QKRPGLKIHV
CSLVAPDSPA GKDWMPVYIH SKLMIIDDVF TTHGSANINS RSMEVDSEIN VAHEWASVTE
RLRRRLWDLH TGGMGVQDDP AVAFKAWGNV IEENRKRQND KEKAWEPYAP LIEFYYGEKT
MADLD
//
