ID A0A290ZJQ0_9RHOO Unreviewed; 188 AA.
AC A0A290ZJQ0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=CCZ27_04020 {ECO:0000313|EMBL:ATE59235.1};
OS Thauera sp. K11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=2005884 {ECO:0000313|EMBL:ATE59235.1, ECO:0000313|Proteomes:UP000217984};
RN [1] {ECO:0000313|EMBL:ATE59235.1, ECO:0000313|Proteomes:UP000217984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K11 {ECO:0000313|EMBL:ATE59235.1,
RC ECO:0000313|Proteomes:UP000217984};
RA Xi L., Qiao N.;
RT "Thauera phenolivorans sp. nov., a phenol derivative-degrading bacterium
RT isolated from activated sludge and an emended description of the genus
RT Thauera.";
RL Submitted (SEP-2017) 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 -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP023439; ATE59235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A290ZJQ0; -.
DR KEGG; thk:CCZ27_04020; -.
DR OrthoDB; 5294698at2; -.
DR Proteomes; UP000217984; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR CDD; cd09170; PLDc_Nuc; 1.
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 Endonuclease {ECO:0000313|EMBL:ATE59235.1};
KW Hydrolase {ECO:0000313|EMBL:ATE59235.1};
KW Nuclease {ECO:0000313|EMBL:ATE59235.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217984};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..188
FT /note="phospholipase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013036061"
FT DOMAIN 115..146
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 188 AA; 20263 MW; 71E87A21F79BBA4F CRC64;
MPERRRLAAC LLAFAVAGSA AASQRFAARG EVEVAFSPRD DAEGVLIGVI GGARRTLLVQ
AYAFTSRRIA DALVAASRRG VRVEVLADAQ MNRRGTGNAL PRLLEAGIPV ALETGYNAAH
NKLLIVDADG PGCAVVTGSY NFTWSAQNRN AENLLVLRGH CTLADAYRDN WRRHRAEATP
ITRLPWSP
//
