ID A1SN75_NOCSJ Unreviewed; 436 AA.
AC A1SN75;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN OrderedLocusNames=Noca_3760 {ECO:0000313|EMBL:ABL83260.1};
OS Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL83260.1, ECO:0000313|Proteomes:UP000000640};
RN [1] {ECO:0000313|Proteomes:UP000000640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABL83260.1, ECO:0000313|Proteomes:UP000000640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX PubMed=21551312; DOI=10.1128/JB.05109-11;
RA Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C., Copeland A.,
RA Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A., Hammon N.M., Han S.,
RA Hauser L.J., Israni S., Kim E., Kyrpides N., Land M.L., Lapidus A.,
RA Larimer F.W., Lucas S., Pitluck S., Richardson P., Schmutz J., Tapia R.,
RA Thompson S., Tice H.N., Spain J.C., Gossett J.G., Mattes T.E.;
RT "Genome Sequence of the ethene- and vinyl chloride-oxidizing actinomycete
RT Nocardioides sp. strain JS614.";
RL J. Bacteriol. 193:3399-3400(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; CP000509; ABL83260.1; -; Genomic_DNA.
DR AlphaFoldDB; A1SN75; -.
DR STRING; 196162.Noca_3760; -.
DR KEGG; nca:Noca_3760; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_047394_0_0_11; -.
DR Proteomes; UP000000640; Chromosome.
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; 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 SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000640};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..436
FT /note="phospholipase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002637565"
FT DOMAIN 139..171
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 24..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 436 AA; 49338 MW; A3B9BACFC7B425C6 CRC64;
MRLRITGVLG ALVLVATMLA TSPTGPAEAA SRKRWEPPTG GHFNNPWRDR EAKFRIERQI
VAAINHAHKA SYIRIAVYSF DRVNVAKRLI EAHKRGVHVQ VLHNDHAYTK AMKMLKRALG
TKRSRKSWDY TCKTGCRSQQ GVLHDKIYLF EHTGGARNVV MTGSANLTKN AAVHQFNDLL
VKKDAPKLYD VVLTLFRQLK KDRTAKPLYW HKVLRDYQLW VMPHPRTAAD NDPVMDILRP
VRCRGAKGGT GTNGRTKIRV SMHSWNGDRG AWIARRLRHL YADGCNVKVM WGLAGAKMKD
VMGAQTPRGR VPRHANGYDT DCDELNEVDM YSHQKYFTIS GRYGRDRSAS LVFTGSSNWT
HSGVSGDEMI LRAKGPHLVK QWNNNFSNIW KNWSRPVGHQ GGFRPAPPPC KAERGISARR
ATTHDLSFSG PYWEAD
//
