ID S5R4B4_9PROT Unreviewed; 194 AA.
AC S5R4B4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=SSDC_01800 {ECO:0000313|EMBL:AGS07044.1};
OS Candidatus Profftella armatura.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Profftella.
OX NCBI_TaxID=669502 {ECO:0000313|EMBL:AGS07044.1, ECO:0000313|Proteomes:UP000015216};
RN [1] {ECO:0000313|EMBL:AGS07044.1, ECO:0000313|Proteomes:UP000015216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC {ECO:0000313|EMBL:AGS07044.1,
RC ECO:0000313|Proteomes:UP000015216};
RX PubMed=23850282; DOI=10.1016/j.cub.2013.06.027;
RA Nakabachi A., Ueoka R., Oshima K., Teta R., Mangoni A., Gurgui M.,
RA Oldham N.J., van Echten-Deckert G., Okamura K., Yamamoto K., Inoue H.,
RA Ohkuma M., Hongoh Y., Miyagishima S.Y., Hattori M., Piel J., Fukatsu T.;
RT "Defensive bacteriome symbiont with a drastically reduced genome.";
RL Curr. Biol. 23:1478-1484(2013).
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}.
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DR EMBL; CP003468; AGS07044.1; -; Genomic_DNA.
DR RefSeq; WP_020915619.1; NZ_CP012591.1.
DR AlphaFoldDB; S5R4B4; -.
DR STRING; 669502.SSDC_01800; -.
DR KEGG; ssdc:SSDC_01800; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_080814_3_1_4; -.
DR OrthoDB; 5294698at2; -.
DR Proteomes; UP000015216; Chromosome.
DR GO; GO:0016787; F:hydrolase 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 SMART; SM00155; PLDc; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR PROSITE; PS50035; PLD; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000015216}.
FT DOMAIN 128..155
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 194 AA; 22234 MW; BA8F2F366038E8C2 CRC64;
MSILKKKIKN LTSSNKIIKK ITIILLIFFL TLPIFSNSNF FNHNNNIEVG FSPGNAKKIV
LNAIQEAKKS IEIAAYSFTN KDIAKILVKS YKKGINIRII ADKKANSGKY TAVTYLANNN
IPIRLNNNYA IMHNKFIIID HKSVETGSLN YTQNAMNRNA ENVIYFRNKP NVSEKFLLEF
DRLWSESKNL NPKY
//
