ID F2RKQ4_STRVP Unreviewed; 428 AA.
AC F2RKQ4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN OrderedLocusNames=SVEN_2006 {ECO:0000313|EMBL:CCA55293.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA55293.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA55293.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA55293.1};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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; FR845719; CCA55293.1; -; Genomic_DNA.
DR RefSeq; WP_015033211.1; NZ_JABVZO010000101.1.
DR AlphaFoldDB; F2RKQ4; -.
DR STRING; 953739.SVEN_2006; -.
DR GeneID; 69864164; -.
DR KEGG; sve:SVEN_2006; -.
DR PATRIC; fig|953739.5.peg.4162; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_047394_1_0_11; -.
DR OrthoDB; 3740959at2; -.
DR Proteomes; UP000006854; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..428
FT /note="phospholipase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003285405"
FT DOMAIN 70..217
FT /note="Phospholipase D-like"
FT /evidence="ECO:0000259|Pfam:PF13091"
FT DOMAIN 285..418
FT /note="Phospholipase D-like"
FT /evidence="ECO:0000259|Pfam:PF13091"
SQ SEQUENCE 428 AA; 45520 MW; BEC117B156A9AC35 CRC64;
MISIKSKFRT TVTALAVGAS LLVAPSASAE PVLAVTTGPV FNDPNSADAS ARGRILSHLA
GLVDGAEPGS SIRISLYLYQ SVYLAEKLGA AHRRGVTVQV VVDADSRSTG LDTLKSRLAD
PTGSPDSWVR TCKAEEACLA LDPGTTAADP NGTYDNVNHN KFFLFSRTKG KGTVPVDDVV
VQGSGNLTSN DTDDWWNDAL TVAGNTELFA AYTRYFDDQA AAAAGQAPQV ADYPHDTQAG
KAKVYFFPRS GTDTVVNILG TVAPVGTPDS CAGNSAGYGT PDGRTKIRIA QGHITRTEVA
RKLWELAEAG CDIEIVYRSL DNWTADDKPM GQVANWLTRP VTGKGRITLH QLDNDKRGGS
DSHTKYLLVE GTYNGGVNKK IVFTGSHTYT TTALKYNDEA LLKYEDAAVF DAYVGNFEAQ
RAAALAGL
//
