ID A0A0S8K6P8_9BACE Unreviewed; 744 AA.
AC A0A0S8K6P8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=AMS26_02070 {ECO:0000313|EMBL:KPL17132.1};
OS Bacteroides sp. SM23_62.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL17132.1, ECO:0000313|Proteomes:UP000050819};
RN [1] {ECO:0000313|EMBL:KPL17132.1, ECO:0000313|Proteomes:UP000050819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_62 {ECO:0000313|EMBL:KPL17132.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPL17132.1}.
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DR EMBL; LJUP01000009; KPL17132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8K6P8; -.
DR PATRIC; fig|1703352.3.peg.4914; -.
DR Proteomes; UP000050819; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR043744; DUF5689.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR43856; CARDIOLIPIN HYDROLASE; 1.
DR PANTHER; PTHR43856:SF1; MITOCHONDRIAL CARDIOLIPIN HYDROLASE; 1.
DR Pfam; PF18942; DUF5689; 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;
FT DOMAIN 405..439
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 583..616
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 744 AA; 81180 MW; 56D7D6D917E76F34 CRC64;
MMKSALVTVL FSFGILSLEA QLVSIREARS APMGTEVTLT GIVTCDVIGN PSIRYFQDPT
GGMAVYDHNF ADDVKKGDSI TVTGILKDYQ SLIELEPVRG YTIHSCGHSL PHPLLITPGQ
LHDSIQGMLV QIKNVVFDDA GGSFGSGEYQ YTAIDERGTV YVHPDNPLAG VSIPGSPVTM
TGIASTYNQN HQVIVRDYGD LVASGSIWLT TPMVVTNIST QGFDLAWTTN IKGSTALRYG
NTPAMELGVL AGTADSTWHL VSVTGADPSE LFYAQAISVA GADTAWSGVN AYITKSSSTG
VMKAYFNRTV DNSVSSGTDA VHLHLSMDDT LAAYVNRAKY SIDLAIYSYN TSGIADITAA
LNEAHDRGVR VRVVADWHTR EQKRWEILDP DIGIMISPQD DYDASTGIMH NKFLIIDAVS
PDPADAYVWT GSGNITEDQL HHHANNVIII QDQSLATVYQ LEFEEMFGSS GSQPDHSASK
FGTSKKDNTP HELVIGNIPV ECYFSPTNRV NQIISDNISQ ADHELYVNTM LITRDFLAEA
IVERNDAGVV SQVIINDEND PADNEYVMGI LKDLGQNFRQ NGEGSILHHK TMIIDQGYPA
ADPLVLTGSH NWSSSADTRN DENTLIIHDG TLANIYYQEF SERFRNGEIT GNTSVDATGT
AGRQELFIYP NPNSGSFILI SPFLMDVRAD LEIFTSDGRL IWSSRTGLVP GENPVTLPTK
PERGLYILQL RHNGGMERCL FISQ
//
