ID A0A031LWU2_9GAMM Unreviewed; 487 AA.
AC A0A031LWU2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=CL42_04500 {ECO:0000313|EMBL:EZQ11578.1};
OS Acinetobacter sp. Ver3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=466088 {ECO:0000313|EMBL:EZQ11578.1, ECO:0000313|Proteomes:UP000023816};
RN [1] {ECO:0000313|EMBL:EZQ11578.1, ECO:0000313|Proteomes:UP000023816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ver3 {ECO:0000313|EMBL:EZQ11578.1,
RC ECO:0000313|Proteomes:UP000023816};
RA Kurth D.G., Ordonez O.F., Albarracin V.H., Revale S., Farias M.E.;
RT "Polyextremophylic features in the genome of Acinetobacter sp. Ver3
RT isolated from a high altitude andean lake.";
RL Submitted (MAR-2014) 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};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EZQ11578.1}.
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DR EMBL; JFYL01000009; EZQ11578.1; -; Genomic_DNA.
DR RefSeq; WP_035265572.1; NZ_JFYL01000009.1.
DR AlphaFoldDB; A0A031LWU2; -.
DR eggNOG; COG1502; Bacteria.
DR Proteomes; UP000023816; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd09129; PLDc_unchar2_1; 1.
DR CDD; cd09130; PLDc_unchar2_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR025202; PLD-like_dom.
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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 81..264
FT /note="Phospholipase D-like"
FT /evidence="ECO:0000259|Pfam:PF13091"
FT DOMAIN 309..450
FT /note="Phospholipase D-like"
FT /evidence="ECO:0000259|Pfam:PF13091"
SQ SEQUENCE 487 AA; 55555 MW; BEB96031A25B18E2 CRC64;
MRLFKRIHQK LNWSNRRYVG LILGMLTIGY LASALYHIYK PLPEGLNYSG KLRHANVKFL
ADQTYIDTAG QRQQHQIFDE ILNLIEQAQT TIVLDMFLFN PETGQSQNQH RALTRELTQA
LIKKKRLTPN IEIKLITDPI NSVYGGIIPE HYRQLRQAGI DVIETDLSPL RASNPLWSGI
WYFCCQSLGN NAEKGWLSNP FGEEKITIRS YLNLFNFKAN HRKTIIVDTS EGWKTLVTSM
NPHDGSSRHS NVALVVEGHT AVDILKTEQS VALFSKANIP MVIVGDVPED KQLQQVQVLT
EKAIYDELLK LIESAQGADA KIDLAMFYLS ERKIIEALIE AHQRGVEVRV LLDPNKDAFG
RTKNGIPNRP VATELYKAGI DVRWCNTQGE QCHSKMIIKR SSDQVELILG SANFTARNLK
NYNLETDLRV IGSSNQQVFK DAVQYFDTAW MNLEGKQMSV DYSEYAEDSK MKYAIYRFME
WSGLSTF
//
