ID   A0A0Q4BRS7_9SPHN        Unreviewed;       566 AA.
AC   A0A0Q4BRS7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Alkaline phosphatase {ECO:0000256|PIRNR:PIRNR031924};
DE            EC=3.1.3.1 {ECO:0000256|PIRNR:PIRNR031924};
GN   ORFNames=ASE49_11560 {ECO:0000313|EMBL:KQM14790.1};
OS   Novosphingobium sp. Leaf2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM14790.1, ECO:0000313|Proteomes:UP000050893};
RN   [1] {ECO:0000313|EMBL:KQM14790.1, ECO:0000313|Proteomes:UP000050893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf2 {ECO:0000313|EMBL:KQM14790.1,
RC   ECO:0000313|Proteomes:UP000050893};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM14790.1, ECO:0000313|Proteomes:UP000050893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf2 {ECO:0000313|EMBL:KQM14790.1,
RC   ECO:0000313|Proteomes:UP000050893};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Alkaline phosphatase with broad substrate specificity.
CC       {ECO:0000256|PIRNR:PIRNR031924}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR031924};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR031924};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRNR:PIRNR031924};
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:KQM14790.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMJY01000019; KQM14790.1; -; Genomic_DNA.
DR   RefSeq; WP_056774308.1; NZ_LMJY01000019.1.
DR   AlphaFoldDB; A0A0Q4BRS7; -.
DR   STRING; 1735670.ASE49_11560; -.
DR   OrthoDB; 9766127at2; -.
DR   Proteomes; UP000050893; Unassembled WGS sequence.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd16016; AP-SPAP; 1.
DR   Gene3D; 3.30.1360.150; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR026263; Alkaline_phosphatase_prok.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR10151:SF126; PHOSPHODIESTERASE; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   PIRSF; PIRSF031924; Pi-irrepressible_AP; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR031924};
KW   Phosphoprotein {ECO:0000256|PIRSR:PIRSR031924-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050893};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRNR:PIRNR031924}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..566
FT                   /note="Alkaline phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006212844"
FT   ACT_SITE        97
FT                   /note="Phosphothreonine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031924-50"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031924-51"
FT   BINDING         179..181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031924-51"
SQ   SEQUENCE   566 AA;  59594 MW;  D79E74BB931FAF41 CRC64;
     MRLSFSSLAV ALVLGASVPA MAQTAAPAAP VAPQAAQPAP ATPAPATPPK LIVAISVDQY
     SADLFSQYRQ HYSKGLARLL QGAVFPSGFQ SHAATETCPG HSTLLTGVHP NRTGIIANNW
     FVPGIARADK QVYCVEDETN PASNSEDSVV ATAHLKAPTL GDLLKRKNPA SLNVAVSAKD
     RAVVMMSGHT ADAAYWVKGK GFATFADRKL SPAAIAENAA LASRVDAGMG PLPVPDWCGA
     VDHATPLGNF SIGTYRFPLT GGDYKGFVNS PRVDAATTEM AIRLLDEMPL GRGPAPDVLS
     VSYSATDKVG HAYGMEGVEM CIQMNELDQT IGTLLTALDA RGIDYVVVLT ADHGGTDVPE
     RMRLQGVPDA ARLDPALIDK ALSASVGKAT GITVKDGPLL YGAGGSGDIW LNAGLNPKQR
     KAVIRELVAE LKANPQVSGV YTADELKAVK VPSGHPQDWT QIERVAASFD PARSGEVLMM
     TRRAVVPGVK PVPGYVSTHG SAWDYDRRVP MLFWRKGMVP MEQAQPVETV DIAPTLAALV
     GLSEPAGTWD GRCLDIYAGE SDSCSR
//