ID X8CKN2_MYCIT Unreviewed; 484 AA.
AC X8CKN2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Phospholipase D family protein {ECO:0000313|EMBL:EUA56008.1};
GN ORFNames=I550_4166 {ECO:0000313|EMBL:EUA56008.1};
OS Mycobacterium intracellulare 1956.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1299331 {ECO:0000313|EMBL:EUA56008.1, ECO:0000313|Proteomes:UP000020825};
RN [1] {ECO:0000313|EMBL:EUA56008.1, ECO:0000313|Proteomes:UP000020825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1956 {ECO:0000313|EMBL:EUA56008.1,
RC ECO:0000313|Proteomes:UP000020825};
RA Zelazny A., Olivier K., Holland S., Lenaerts A., Ordway D., DeGroote M.A.,
RA Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL Submitted (DEC-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EUA56008.1}.
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DR EMBL; JAOG01000002; EUA56008.1; -; Genomic_DNA.
DR AlphaFoldDB; X8CKN2; -.
DR PATRIC; fig|1299331.3.peg.4066; -.
DR Proteomes; UP000020825; Unassembled WGS sequence.
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}.
FT DOMAIN 132..159
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 345..372
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 484 AA; 53905 MW; AD03E63EF5707DAF CRC64;
MHDDRLLSPG QTCWRTARAD KFAPIVDAAD YFKHAKAAML RARRRIMLIG WDFDSRVTFE
RGRKTLPGPN QLGTFLYWML WKRPGLDIYL LKSNLRLLPA FDGLWYGLAP VSLVNQISSK
RMHFAIDGAH PLGSVHHQKI VVVDDAVAFC GGIDLTLDRW DTRAHEHVNR HRRTARRSYG
PRHDVAAAVD GAAARALGEQ ALARWQTATK QALAPVEARH SAWPGKLEPT LRNVDIGIAL
TLPELDDRPE VREVEALNLA AIAAARDTIY VENQYLASRT LADALAARLR EADGPEIVIV
LARKGNNPLE RGTMDSARHL LLHQLWEADE HDRLGIYWPV TDRGAPIYIH SKVLVVDDRL
LRIGSSNFNN RSLGFDSECD VAIEAPPASS DDDVRREIAS VRNGLVAEHL GVSPGELNRA
IAEHRSVHKA VEALRGDGKT LQPFTERTVA DEAGPLAENE LMDPDHVPRS LSRSVQRFIT
GLRG
//
