ID A0A172UHA9_9MYCO Unreviewed; 480 AA.
AC A0A172UHA9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phospholipase {ECO:0000313|EMBL:ANE78552.1};
GN ORFNames=A7U43_03650 {ECO:0000313|EMBL:ANE78552.1};
OS Mycobacterium adipatum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1682113 {ECO:0000313|EMBL:ANE78552.1, ECO:0000313|Proteomes:UP000077143};
RN [1] {ECO:0000313|EMBL:ANE78552.1, ECO:0000313|Proteomes:UP000077143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC-RL4 {ECO:0000313|EMBL:ANE78552.1,
RC ECO:0000313|Proteomes:UP000077143};
RA Ren L., Fan S., Ruth N., Jia Y., Wang J., Qiao C.;
RT "Complete genome sequence of a phthalic acid esters degrading Mycobacterium
RT sp. YC-RL4.";
RL Submitted (MAY-2016) 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; CP015596; ANE78552.1; -; Genomic_DNA.
DR RefSeq; WP_067991254.1; NZ_CP015596.1.
DR AlphaFoldDB; A0A172UHA9; -.
DR STRING; 1682113.A7U43_03650; -.
DR KEGG; madi:A7U43_03650; -.
DR OrthoDB; 8828485at2; -.
DR Proteomes; UP000077143; 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:UP000077143}.
FT DOMAIN 134..161
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 343..370
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 480 AA; 52582 MW; 4AC74ACC97DB2DC2 CRC64;
MASTADRILV AGRTCWQVPT ADRFAVIIDG ADYLRHVKAA MLRAQRRIIL VGWDFDAGTT
FEQGQTTLPG PNQLGAFLYW LLWKRAGLQI YVLKSNLRLL PLFDDLWYGI TPVSLLNRFS
GRRIRFAVDG AHPAGAVHHQ KIIVIDDAVA FCGGIDLTIG RWDTSDHLDD NPLRTAYGPR
HEVATAMDGA AAGALGELAR DRWRAATGQN MPALDVAHSP WPRGLEPQLR DVEVGIARTL
PALPENDEVR EVEALNLAAI EAAEHTIYLE NQYLASRTLV EALIRRLGER GGPEIVIILP
RRSESALEIQ SMDSARSALI AELWSADTHG HLGIYWPVTG NGTPIYVHSK VIVVDDRLLR
IGSSNLNNRS MGFDSECDVA IEADSDAGRE LIAQIRRVLI SEHLGVPVAD FYAAVPDNGS
FLTAVETLRG DGRTLEPMTA DVVADEAGPL AENDLMDPDH VPSSLTGSVR RLLNELAGWQ
//
