ID A0A136A6Z0_9ALTE Unreviewed; 234 AA.
AC A0A136A6Z0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=undecaprenyl-diphosphate phosphatase {ECO:0000256|ARBA:ARBA00012374};
DE EC=3.6.1.27 {ECO:0000256|ARBA:ARBA00012374};
DE AltName: Full=Undecaprenyl pyrophosphate phosphatase {ECO:0000256|ARBA:ARBA00032707};
GN ORFNames=AX660_00625 {ECO:0000313|EMBL:KXI30999.1};
OS Paraglaciecola hydrolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1799789 {ECO:0000313|EMBL:KXI30999.1, ECO:0000313|Proteomes:UP000070299};
RN [1] {ECO:0000313|EMBL:KXI30999.1, ECO:0000313|Proteomes:UP000070299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S66 {ECO:0000313|EMBL:KXI30999.1,
RC ECO:0000313|Proteomes:UP000070299};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-
CC trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate;
CC Xref=Rhea:RHEA:28094, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58405, ChEBI:CHEBI:60392; EC=3.6.1.27;
CC Evidence={ECO:0000256|ARBA:ARBA00000759};
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:KXI30999.1}.
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DR EMBL; LSNE01000001; KXI30999.1; -; Genomic_DNA.
DR RefSeq; WP_068370954.1; NZ_LSNE01000001.1.
DR AlphaFoldDB; A0A136A6Z0; -.
DR STRING; 1799789.AX660_00625; -.
DR OrthoDB; 9780918at2; -.
DR Proteomes; UP000070299; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd03392; PAP2_like_2; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 2.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR14969:SF13; AT30094P; 1.
DR PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000070299};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 108..219
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 234 AA; 26365 MW; C3B3D73B08084C0C CRC64;
MQIKPNNPAL TSLVKFSTIL WLSLFCVLAW LFIELALLVN SGSPLSWDRS IMLAMRNPLD
LGDPIGPAWF EELMRDVTAL GGTGILSLLT LLTCAYLFMQ KNSTLAWFVL ITIGTGMLCS
FALKYGFSRP RPELVAHGSY VYTSSFPSGH SMMSAVVYFI LTGVLLQTQT RRRIKIFMLS
CTAMVVVLIG LSRVYLGVHW PTDVLAGWSA GCFWALCSYR FLRYWQKRQS RKTH
//
