ID A0A2S2BRV2_9NOCA Unreviewed; 498 AA.
AC A0A2S2BRV2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Phospholipase {ECO:0000313|EMBL:AWK71323.1};
GN ORFNames=CBI38_06775 {ECO:0000313|EMBL:AWK71323.1};
OS Rhodococcus oxybenzonivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1990687 {ECO:0000313|EMBL:AWK71323.1, ECO:0000313|Proteomes:UP000245711};
RN [1] {ECO:0000313|EMBL:AWK71323.1, ECO:0000313|Proteomes:UP000245711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2-17 {ECO:0000313|EMBL:AWK71323.1,
RC ECO:0000313|Proteomes:UP000245711};
RA Lee Y., Kim K.H., Chun B.H., Jung H.S., Jeon C.O.;
RT "Isolation of Rhodococcus sp. S2-17 biodegrading of BP-3.";
RL Submitted (MAY-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};
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DR EMBL; CP021354; AWK71323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2BRV2; -.
DR KEGG; roz:CBI38_06775; -.
DR OrthoDB; 8828485at2; -.
DR Proteomes; UP000245711; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR CDD; cd09140; PLDc_vPLD1_2_like_bac_1; 1.
DR CDD; cd09143; PLDc_vPLD1_2_like_bac_2; 1.
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; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000245711}.
FT DOMAIN 130..157
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 346..373
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 448..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 55730 MW; 8F8E26BBB7555833 CRC64;
MSDESPILAP GDTCWQVTHA DRLACIVDAA DYFRHAKSAM LQARHRIILI GWDFDTRIKF
EPDEKTLEGP NRLGRFLVWL TRKRPDLEIY LLKWNIGAFA AIGRGMTPVF MVNCVTDRRL
HFEIDGAHPV GSAHHQKIVV IDDTLAFCGG IDMTVDRWDT SDHRDDNHYR TQPNGNRYGP
WHDATTAVDG DAAKAVSEQA RARWKTATGK ELPALDDTAH TTPWPDGLEP TMHSVDVGIA
RTLPELADRG EVREIEALYL AAIAGAARSL YIESQYLASR TIAEAIATRL REPDGPEIML
VLPRNADGWL ERLAMDGARR RLLHLLWDAD AGGKLGVYYP VTAGGNPIYV HAKILVMDDR
LLRVGSSNLN NRSMGFDSEC DLAVEVRADT ANGDRLRDTI VGIRRQLLCE HLDVASDTFD
DLLTEKGSLL ATVEALRGDG RTLMPFEPDT VEGEDSPLAE SELMDPERTP PSIWERTNWT
RFRRRLVRRR KAAGSLQS
//
