ID M3GCY8_LEPBO Unreviewed; 448 AA.
AC M3GCY8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=LEP1GSC123_3149 {ECO:0000313|EMBL:EMF98786.1};
OS Leptospira borgpetersenii str. 200701203.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193007 {ECO:0000313|EMBL:EMF98786.1, ECO:0000313|Proteomes:UP000011783};
RN [1] {ECO:0000313|EMBL:EMF98786.1, ECO:0000313|Proteomes:UP000011783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200701203 {ECO:0000313|EMBL:EMF98786.1,
RC ECO:0000313|Proteomes:UP000011783};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL Submitted (JAN-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:EMF98786.1}.
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DR EMBL; AKWO02000078; EMF98786.1; -; Genomic_DNA.
DR AlphaFoldDB; M3GCY8; -.
DR BioCyc; LBOR1193007:G11KN-740-MONOMER; -.
DR Proteomes; UP000011783; 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; cd09172; PLDc_Nuc_like_unchar1_1; 1.
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; 2.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000011783}.
FT DOMAIN 128..155
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 289..316
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 448 AA; 51376 MW; 7AB69B1A6C4C9145 CRC64;
MRKISNAFVL IFLYIWFFLS LATCSSRHDS DFFWLEWAKT RNVEASFSYP GRYVHTFKRR
NVRDKILRLI ESAGFAIDLW VYSFEDPEIL NALKKANTRG VQIRIVADPE REYMDEFKNL
GVFRKWERSG LQHSKILIVD RKKVFLGSGN FTWYGLENDL NGYVSFDLFD SEIENFYAFL
EEDSGITSLN IPPFQFYISP EKGRLIQNLI LREVDRAQRD IRYLIFDHFD SVLTSRLALA
DRRGVNVKGI YDSPVDEEGK YLANVFENPG SEIAADGNEE VIESGSFGKG GLLHHKTMIV
DGKTLISGSY NFSISARDNN REILFKTTNP YLVAVYVEEW ERIRVNSIVY KATSFGTENG
SNGIYFGYSG NSIPIGVEQT ICRTDTAKEE SFYLESGNAF LKSILEYTFL PTESCKDVSN
FTPPSSGFTG KKPIIRSRRK VLGKKGFY
//
