ID   A0ZCG9_NODSP            Unreviewed;       541 AA.
AC   A0ZCG9;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN   ORFNames=NSP_37350 {ECO:0000313|EMBL:AHJ30038.1};
OS   Nodularia spumigena CCY9414.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC   Nodularia.
OX   NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ30038.1, ECO:0000313|Proteomes:UP000019325};
RN   [1] {ECO:0000313|EMBL:AHJ30038.1, ECO:0000313|Proteomes:UP000019325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ30038.1};
RX   PubMed=23555932;
RA   Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA   Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA   Stal L.J., Hess W.R.;
RT   "Insights into the physiology and ecology of the brackish-water-adapted
RT   Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT   analysis.";
RL   PLoS ONE 8:E60224-E60224(2013).
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; CP007203; AHJ30038.1; -; Genomic_DNA.
DR   RefSeq; WP_006195149.1; NZ_CP007203.1.
DR   AlphaFoldDB; A0ZCG9; -.
DR   STRING; 313624.NSP_37350; -.
DR   GeneID; 78017931; -.
DR   PATRIC; fig|313624.11.peg.3751; -.
DR   eggNOG; COG1502; Bacteria.
DR   eggNOG; COG1555; Bacteria.
DR   HOGENOM; CLU_038899_0_0_3; -.
DR   Proteomes; UP000019325; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR   CDD; cd09116; PLDc_Nuc_like; 1.
DR   CDD; cd09173; PLDc_Nuc_like_unchar1_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   Gene3D; 1.10.150.320; Photosystem II 12 kDa extrinsic protein; 1.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR010994; RuvA_2-like.
DR   PANTHER; PTHR43856; CARDIOLIPIN HYDROLASE; 1.
DR   PANTHER; PTHR43856:SF1; MITOCHONDRIAL CARDIOLIPIN HYDROLASE; 1.
DR   Pfam; PF12836; HHH_3; 1.
DR   Pfam; PF13091; PLDc_2; 2.
DR   SMART; SM00278; HhH1; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50035; PLD; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..541
FT                   /note="phospholipase D"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002631813"
FT   DOMAIN          184..211
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          388..415
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   541 AA;  61009 MW;  53C5B8DE24D28D52 CRC64;
     MQIFPPRKYF LIFFLIFAIA CQKAQPQNQL LAALPQDSLV QVYFNHSQAS EYKEPYRQQT
     RLGDNLEQQI IDAISQAQST VDVAIQELRL PKISQALAQR QKAGVKVRVI LEDNYSRPLS
     SLTPAEVQKL TPREQARYQE FRNFVDLNQD NQLSPEEINQ RDALIILNNA KIPWIDDRAD
     GSAGSNLMHH KFVIVDNRWV IKTSANFTLS DIHGDYTNLS SLGNANNFLK IDSPELAVLF
     TEEFNIMWGD GPGGKPDSRF GLQKPMRAPQ NITLGDTKIT VHFSPTSSTQ PWNKSSNGLM
     GETLKSATKS IDMALFVFSE QRLANIIKTR HQKNVSIRAL IDSQFAYRYY SDAMDMMGVA
     LSNNCKYELD NNPWQNPLTT VGVPTLARGD LLHHKFGVID QQTVITGSHN WSKAANHGND
     ETVLIVENPT IAAHYVREFN RLYADAKLGV PLSVQQKISA EEKQCPQIIS QTSSKFLEIK
     PVNINTATLE ELVTLPGIGE QLAQKIIIAR QQQKFTSLAD LTRVSGISTK STEKWRDRII
     W
//