ID H8GWE4_DEIGI Unreviewed; 437 AA.
AC H8GWE4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN OrderedLocusNames=DGo_CA1767 {ECO:0000313|EMBL:AFD25694.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD25694.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD25694.1, ECO:0000313|Proteomes:UP000007575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC {ECO:0000313|Proteomes:UP000007575};
RX PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA Lin M.;
RT "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT Deinococcus gobiensis: insights into the extreme environmental
RT adaptations.";
RL PLoS ONE 7:E34458-E34458(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};
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DR EMBL; CP002191; AFD25694.1; -; Genomic_DNA.
DR AlphaFoldDB; H8GWE4; -.
DR STRING; 745776.DGo_CA1767; -.
DR KEGG; dgo:DGo_CA1767; -.
DR PATRIC; fig|745776.4.peg.1815; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_042779_0_0_0; -.
DR Proteomes; UP000007575; Chromosome.
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 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; 2.
DR PROSITE; PS50035; PLD; 2.
PE 4: Predicted;
FT DOMAIN 148..170
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 361..388
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 437 AA; 47707 MW; FAC2ACAD23A16EBC CRC64;
MATADDRPDL SCDNAFVGYL RTPRGPGTPQ DAFEVIAQQV RGARREVLLT SMEWQGGQGA
GGQASPGYTF ASAVRDLYAR VRADPATYPQ GMRVRVVMGG YPDFTRPDGM TQVLSLARDL
RALGVPLEDA ALDWHVSVLD YGFFPHSHAK LHVIDGEDVT VEGYNFADTH LPDGENGGRG
LHDLGLRMRG PVAQDAVAAF DDLWRHSRQL RCPADVAAAE VEARCALDES DPPAHPARAR
AATPAGDARA FVFYRRPGSD VADQAQQAAL LAARREIDLL EADFSPDLSC WLAYLNPDGC
GRETFPPYLA ALLDAMERGV HVRVLTVNYG YGAFANRSGV ALLRAEARRR GLDALFEARY
VDFKLHSKAV TLDRELVMAG SVNFHFSSWG PLGLNEALIA TSDPSAVAGQ QASFEDLWAG
HSTPVPEEWW MRFVRRG
//
