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Database: UniProt
Entry: F8GSV2_CUPNN
LinkDB: F8GSV2_CUPNN
Original site: F8GSV2_CUPNN 
ID   F8GSV2_CUPNN            Unreviewed;       753 AA.
AC   F8GSV2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Phospholipase D {ECO:0000313|EMBL:AEI79871.1};
DE            EC=3.1.4.4 {ECO:0000313|EMBL:AEI79871.1};
GN   OrderedLocusNames=CNE_2c09000 {ECO:0000313|EMBL:AEI79871.1};
OS   Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS   / N-1) (Ralstonia eutropha).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI79871.1, ECO:0000313|Proteomes:UP000006798};
RN   [1] {ECO:0000313|EMBL:AEI79871.1, ECO:0000313|Proteomes:UP000006798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1
RC   {ECO:0000313|Proteomes:UP000006798};
RX   PubMed=21742890; DOI=10.1128/JB.05660-11;
RA   Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT   "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL   J. Bacteriol. 193:5017-5017(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; CP002878; AEI79871.1; -; Genomic_DNA.
DR   RefSeq; WP_013952581.1; NC_015723.1.
DR   AlphaFoldDB; F8GSV2; -.
DR   KEGG; cnc:CNE_2c09000; -.
DR   HOGENOM; CLU_011094_0_0_4; -.
DR   Proteomes; UP000006798; Chromosome 2.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR   CDD; cd09140; PLDc_vPLD1_2_like_bac_1; 1.
DR   CDD; cd09143; PLDc_vPLD1_2_like_bac_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   InterPro; IPR032816; VTT_dom.
DR   PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   Pfam; PF09335; SNARE_assoc; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEI79871.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        506..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        559..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        590..610
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        630..655
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        667..690
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        696..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          151..178
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          372..394
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   753 AA;  81707 MW;  FA6EDBDD3BCF0176 CRC64;
     MRQHNPPGTT APPATGPPHD CQAPLGFTPE PGRNCWRVES CQRFAMLVDA DAYFRALREA
     LPRAEHTIFI LGWDIDSRME LVPQGAQDGL PAGLRDFLCA LADQRPELRI YILSWDYAMV
     MAMEREWLPS ASAHWQAHRH LSFRLDGNHP PGASHHQKVV VIDNKLAFVG GLDLTLRRWD
     DSCHAPGAPL RVAEGKPYPP FHDVQCALDG PAAAALGTLC AARWLRASGS QPRPVAATSS
     DPWPPGLAPE LTDVRVAIAR TMPMCEDEPG VSEIRMLLRD AIASARHSIY MENQYFSSHE
     IAKALEARLG HEDGPVIVLV SRRNESGWLE AHSMGVLRAR LYRRLRAADT QERFCLYCPS
     IPGLMPECVN VHSKVTVIDD DLITIGSSNL SNRSLGLDTE CNIVVMSGGD PRVQAAIAAM
     RARLLGEHLD VAPEAFQAEV AATRSVLAAI RNLQRADGRS LEAYEPPLPD DVDAASPAAS
     LLDPIEPIDS DQVLAEFVSH EARPRVLGRV GMMVALALLL AGLAFAWRHT PLREWADFRA
     LLSVVEQLDE MPLAPLAMIG VYLAGAVTML PVTLLILVTV VIFGPLYGAA LALCGTVLST
     GAGYLAGRLL GRNAVRRFGG RRLNRVSHQL GKHGVVAMVV LRLVPIAPFA LVNLVIGASR
     ISLRDCLLGT ALGMLPSIVV AACLVNRVAA AARDPGLFTF ALLALVLLVP ASLLLVLRRR
     RRRRAEGGAA RPQDDPPGPR GRLARLAALR RQA
//
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