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Database: UniProt
Entry: A0A0P6WNX4_9SPHN
LinkDB: A0A0P6WNX4_9SPHN
Original site: A0A0P6WNX4_9SPHN 
ID   A0A0P6WNX4_9SPHN        Unreviewed;       561 AA.
AC   A0A0P6WNX4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:KPL68584.1};
GN   ORFNames=SZ64_11000 {ECO:0000313|EMBL:KPL68584.1};
OS   Erythrobacter sp. SG61-1L.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL68584.1, ECO:0000313|Proteomes:UP000049978};
RN   [1] {ECO:0000313|EMBL:KPL68584.1, ECO:0000313|Proteomes:UP000049978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG61-1L {ECO:0000313|EMBL:KPL68584.1,
RC   ECO:0000313|Proteomes:UP000049978};
RA   Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA   Pandey G.;
RT   "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT   from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT   of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL   Appl. Environ. Microbiol. 0:0-0(2015).
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:KPL68584.1}.
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DR   EMBL; JXQC01000003; KPL68584.1; -; Genomic_DNA.
DR   RefSeq; WP_054530863.1; NZ_JXQC01000003.1.
DR   AlphaFoldDB; A0A0P6WNX4; -.
DR   STRING; 1603897.SZ64_11000; -.
DR   PATRIC; fig|1603897.4.peg.2130; -.
DR   OrthoDB; 327733at2; -.
DR   Proteomes; UP000049978; Unassembled WGS sequence.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd07389; MPP_PhoD; 1.
DR   Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR   Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR018946; PhoD-like_MPP.
DR   InterPro; IPR038607; PhoD-like_sf.
DR   InterPro; IPR032093; PhoD_N.
DR   InterPro; IPR008963; Purple_acid_Pase-like_N.
DR   PANTHER; PTHR43606; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR   PANTHER; PTHR43606:SF2; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR   Pfam; PF09423; PhoD; 1.
DR   Pfam; PF16655; PhoD_N; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000049978};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          42..128
FT                   /note="Phospholipase D N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16655"
FT   DOMAIN          140..527
FT                   /note="PhoD-like phosphatase metallophosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF09423"
SQ   SEQUENCE   561 AA;  61425 MW;  AF13EA0315E9752B CRC64;
     MAFAAPVTRR TTLAGLAGTT FLATLPWRAA AHDLSANPVF RHGVASGDPD GTSVVLWTRV
     TAEGTPEVRW QLAEDLAFEK IVQQGTATTG ADRDYTVKLL AGGLKPGRTY YYRFQLGDAI
     SPVGRARTLP EGPLDRLGIA LASCSNYPFG FFNAYDAIAR DADVDFVLHT GDYIYEYGQD
     GWGDDVGRAI GRRHEPAHEI VSLSDYRTRH AQYKTDAGSL AMLAAHTLLA CWDDHESANN
     PWTGGAQNHQ PETEGDWKAR RAASIQAYFE WMPVREPEWL AQKGRSRMQF WRSYSFGDLA
     TLFTLETRHT ARAEQIDYLD YATTLASSDD ARHLVEDVIG APGRTMLAPE LEADLSAALE
     QSVAGGQPWR LIGNPMPIAR TNVPDVVSLG LLAQPAADAS LEAQALAWKG KWNLPFYPDT
     WDGYEWARER LYDLSRKAGA GDLVFLTGDS HSFWANQLAD GAGRPAGVEL GTAGITSPGD
     FISSGFGPEL SVKLDQAFTD HNPEVVWTDN MHQGYVRLEL TRGGGEASFV AVDTILRPDY
     RTLVLNRFAL ARKDGAVVLQ G
//
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