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
//