ID A0A1C4LMF4_9ACTN Unreviewed; 577 AA.
AC A0A1C4LMF4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=GA0115240_122312 {ECO:0000313|EMBL:SCD74929.1};
OS Streptomyces sp. DvalAA-14.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839759 {ECO:0000313|EMBL:SCD74929.1, ECO:0000313|Proteomes:UP000199020};
RN [1] {ECO:0000313|EMBL:SCD74929.1, ECO:0000313|Proteomes:UP000199020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DvalAA-14 {ECO:0000313|EMBL:SCD74929.1,
RC ECO:0000313|Proteomes:UP000199020};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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};
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DR EMBL; FMCH01000209; SCD74929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4LMF4; -.
DR Proteomes; UP000199020; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR CDD; cd09128; PLDc_unchar1_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006644; Cadg.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43856; CARDIOLIPIN HYDROLASE; 1.
DR PANTHER; PTHR43856:SF1; MITOCHONDRIAL CARDIOLIPIN HYDROLASE; 1.
DR Pfam; PF05345; He_PIG; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR SMART; SM00736; CADG; 1.
DR SUPFAM; SSF49313; Cadherin-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000199020};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..577
FT /note="phospholipase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008697128"
FT DOMAIN 115..142
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 263..294
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 577 AA; 59132 MW; BE697F961E5BCA77 CRC64;
MSSTRRLIRT LAAGAVASAA ALVPTTAHAA SAYSLVVLPD QGESAIYSFV NSATTSIDMT
IYELRDTTLV NDLVSKQKAG VRVRVILDSQ QTSVNGAAYS ALSAAGAGVT YSSSAYVYTH
QKTITVDGAK SYISTGNFDT TYYSTSRDYG VFDSTSADVA AIEKVFNADY AKTAITPGDG
ADLVWSPTDS QSHLLSLISG AQHSLDVQQE EFGDTALVNA IVADAKRGVA VRVVAENESS
SYTTQLNQVT AAGGKVTTYT SSTGYYIHAK AIVADYGTST AKVFAGSENF SDNSLNHNRE
LGLITTDSGV LSGIEAAFTA DFNHHTTTGV TVAGPGDQTG TVGAAASVQI SATDTAGGTL
SYTASALPAG LSINAATGLI KGTPTTAGTS TVTVTATDST GPSGSTTFSW TVNPASSGGC
APAQLLGNPG FETGSAAPWT ASTGLIGNSA AEPAHSGSWD ARLDGHGTTH TDTLSQTVTL
PSGCSSYQLG FWLHIDTAET STGTAYDTLS AQVLNSSGTV LGTLAGYSNR DHNTGYTQHT
FNLSAYAGKT VTVKFTGSED YELQTTFVLD DAAVTVS
//
