ID R1G3I8_9PSEU Unreviewed; 400 AA.
AC R1G3I8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=H480_23467 {ECO:0000313|EMBL:EOD66048.1};
OS Amycolatopsis vancoresmycina DSM 44592.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD66048.1, ECO:0000313|Proteomes:UP000014139};
RN [1] {ECO:0000313|EMBL:EOD66048.1, ECO:0000313|Proteomes:UP000014139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD66048.1,
RC ECO:0000313|Proteomes:UP000014139};
RA Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL Submitted (FEB-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:EOD66048.1}.
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DR EMBL; AOUO01000344; EOD66048.1; -; Genomic_DNA.
DR RefSeq; WP_003094034.1; NZ_AOUO01000344.1.
DR AlphaFoldDB; R1G3I8; -.
DR PATRIC; fig|1292037.4.peg.4447; -.
DR eggNOG; COG1502; Bacteria.
DR OrthoDB; 3740959at2; -.
DR Proteomes; UP000014139; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR025202; PLD-like_dom.
DR PANTHER; PTHR43856; CARDIOLIPIN HYDROLASE; 1.
DR PANTHER; PTHR43856:SF1; MITOCHONDRIAL CARDIOLIPIN HYDROLASE; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..400
FT /note="phospholipase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004360181"
FT DOMAIN 67..176
FT /note="Phospholipase D-like"
FT /evidence="ECO:0000259|Pfam:PF13091"
FT DOMAIN 276..387
FT /note="Phospholipase D-like"
FT /evidence="ECO:0000259|Pfam:PF13091"
SQ SEQUENCE 400 AA; 42722 MW; CB4448E7D4AD46E4 CRC64;
MGSRFKAFTV AAGALLALAG SGIAHAAPSV AADATGMEAI FNNPPENGDR DHSIETRLVQ
LTNGTPAGAE IHISLYSWTR PAMAEALKAA QARGVKVRIA LDGGADDDPA NTAMPILKGA
GLTQLVFCGT GGDNTGCIAH DGSPHSINHD KLWMFSETEG KKDVVVIGSY NLTTVQGNLF
NNALLTYGDP DLYAFYLGHV QKMLAQKKNN NYFADAGYHK TLTTMVTSYL SPRADSHGGT
SEEFATDTWA QLLKYVTKYE TGCSLNVVQA NIADSRTPVV DELVRIAKLG CKVRIVYDDM
GTAALAALKG KANVTLKRFN TTVNDREISV HSKYMLYTGN YSEKAGRQLV FTGSHNVSGA
ALRDNDEILI KVENAAISAA YQDNFSTILA RAKCTAPAVC
//