ID A0A158D663_9BURK Unreviewed; 761 AA.
AC A0A158D663;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Phospholipase D/transphosphatidylase {ECO:0000313|EMBL:SAK89706.1};
GN ORFNames=AWB77_04931 {ECO:0000313|EMBL:SAK89706.1};
OS Caballeronia fortuita.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1777138 {ECO:0000313|EMBL:SAK89706.1, ECO:0000313|Proteomes:UP000054903};
RN [1] {ECO:0000313|Proteomes:UP000054903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Oliw E.H.;
RL Submitted (JAN-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; FCNX02000013; SAK89706.1; -; Genomic_DNA.
DR RefSeq; WP_061137000.1; NZ_FCNX02000013.1.
DR AlphaFoldDB; A0A158D663; -.
DR STRING; 1777138.AWB77_04931; -.
DR OrthoDB; 8828485at2; -.
DR Proteomes; UP000054903; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0006796; P:phosphate-containing compound 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};
KW Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 497..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 543..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 571..593
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 653..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 684..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 132..159
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 357..379
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 714..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 84100 MW; 0FBED7871D4C9BE3 CRC64;
MDHANEESFF QPGRNCASVR HADRFSLLID GADYFRVLRE ALTRAERTVF ILGWDIDSRM
KLTPEGADDG YPEALGDFLH ALAGDKRRLR IYILAWDFAM LYAFEREWLP VYKMGWRTNR
RIAFQMDGKH PLGGSQHQKI VVIDDRVAFV GGLDLTRSRW DTTAHAPDEP LRRDANGAPY
QPFHDVHSMF DGDAAREIGQ LARERWARAC GKRLAIRAHR ANLRHDPWPP SRRVDLEDVD
IAISLTEPDY LGREPVRQIR TQYLDAIARA RRSIYIENQY FTSGTIGAAL AESLAREDGP
DLAIVVPRNQ SGWLQEVTMG VLRARLHTLL KNADTHGRYR LLFPSVPKLG DEIVNVHSKL
MIVDDELLIV GSANLNNRSM VLDSECNVSI DAGADARIRR AIATMRDTLL AEHLGCKVDD
VVRETQARNG MNAAIQALLR NRDEHRTMVP LDPQVSTELD QVIPPEALID PETPIAAGEL
VDQFVPKEKT RPLIGRFALL GVFALLVVVV AGLWNWTPLG EYVNLKSLTN ATRHIDSLPL
APLWIVLCYV LAAVIAVPIT LLIATSGIVF GAYWGGAYAF VGTTIAAAIS YSLGNWLGRD
AVRRLAGARV NRLSERVAKR GIVAVVALRL LPVAPFAIVN LVAGASHIRM RDFIIGTMLG
MGPGIVLTVA FAHQLVASLH RPTVGSFAVL IGIGAALLGV SLLLQRFLGG AKHQEAHEGA
PGDADKPRAS DEAKRASELR ESGTMPRETP ARNERPDEVN S
//