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Database: UniProt
Entry: B4VRB8_9CYAN
LinkDB: B4VRB8_9CYAN
Original site: B4VRB8_9CYAN 
ID   B4VRB8_9CYAN            Unreviewed;       542 AA.
AC   B4VRB8;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN   ORFNames=MC7420_1243 {ECO:0000313|EMBL:EDX75325.1};
OS   Coleofasciculus chthonoplastes PCC 7420.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Coleofasciculus.
OX   NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX75325.1, ECO:0000313|Proteomes:UP000003835};
RN   [1] {ECO:0000313|EMBL:EDX75325.1, ECO:0000313|Proteomes:UP000003835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX75325.1,
RC   ECO:0000313|Proteomes:UP000003835};
RA   Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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; DS989849; EDX75325.1; -; Genomic_DNA.
DR   RefSeq; WP_006101036.1; NZ_DS989849.1.
DR   AlphaFoldDB; B4VRB8; -.
DR   STRING; 118168.MC7420_1243; -.
DR   eggNOG; COG1502; Bacteria.
DR   eggNOG; COG1555; Bacteria.
DR   HOGENOM; CLU_038899_0_0_3; -.
DR   OrthoDB; 155099at2; -.
DR   Proteomes; UP000003835; Unassembled WGS sequence.
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   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; SSF160975; AF1531-like; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50035; PLD; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000003835}.
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   542 AA;  60231 MW;  6EF51CE0B8D76FA3 CRC64;
     MTQSYWHQGI IWLIVLTLSA CQPPPVQVHR PPPLPQDPFV QVYFNHSPST TYKEPYRLVT
     RPGDNLEQII TQAIATAQST VDVAVQELRL PQIAQALVKR HQAGVRVRVI VENTYNRPWS
     EVSAQDIANL PPRERDRARE NLRLIDRNND GKLTPAEINQ RDALVILRNA GVPILDDTAD
     GSQGSGLMHH KFVVVDGYTV IVTSANFTTS DIHGDFQAPD SRGNANNLLK IESVELANSF
     TEEFNQMWGD GPGGVPDSRF GVKKSQRPIQ KVTLGDTTLA VKFSPTSPTQ PWSQSSNGFI
     EQILQSATQT IELALFVFSE QRLADQLQTV HEQGVQVQAL IDPSFAYRYY SEGLDLLGVA
     LSNQCRYEAR NRPWQNPIAT VGVPQLPSGD LLHHKFGVVD REIVITGSHN WSASANTQND
     ETLLVIDSHL VAAHFEREFE RLYTNAILGV PVAVQRRIQN QQQSCDQITQ ANDPNAPSFR
     GIVNLNTATQ DELETLPGIG PKLAERIITA RSQKPFTSLA DLDRVSGIGP HLLQQLDGRV
     TW
//
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