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Database: UniProt
Entry: W6TQ21_9SPHI
LinkDB: W6TQ21_9SPHI
Original site: W6TQ21_9SPHI 
ID   W6TQ21_9SPHI            Unreviewed;       467 AA.
AC   W6TQ21;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Alkaline phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=N824_28000 {ECO:0000313|EMBL:ETZ21582.1};
OS   Pedobacter sp. V48.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=509635 {ECO:0000313|EMBL:ETZ21582.1, ECO:0000313|Proteomes:UP000019145};
RN   [1] {ECO:0000313|EMBL:ETZ21582.1, ECO:0000313|Proteomes:UP000019145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V48 {ECO:0000313|EMBL:ETZ21582.1,
RC   ECO:0000313|Proteomes:UP000019145};
RX   PubMed=24578271;
RA   Bitzer A.S., Garbeva P., Silby M.W.;
RT   "Draft Genome Sequence of Pedobacter sp. Strain V48, Isolated from a
RT   Coastal Sand Dune in the Netherlands.";
RL   Genome Announc. 2:e00094-e00014(2014).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC       Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2};
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC       {ECO:0000256|RuleBase:RU003946}.
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:ETZ21582.1}.
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DR   EMBL; AWRU01000017; ETZ21582.1; -; Genomic_DNA.
DR   RefSeq; WP_048906193.1; NZ_AWRU01000017.1.
DR   AlphaFoldDB; W6TQ21; -.
DR   STRING; 509635.N824_28000; -.
DR   PATRIC; fig|509635.5.peg.3421; -.
DR   eggNOG; COG1785; Bacteria.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000019145; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   CDD; cd16012; ALP; 1.
DR   Gene3D; 1.10.60.40; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR   Pfam; PF00245; Alk_phosphatase; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        95
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         45
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         146
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         148
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         272
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         277
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         281
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         320
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         423
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   467 AA;  51583 MW;  8E5BC44D26ADB17B CRC64;
     MNRRSLLKGG LLAGISMPFV GLHDVIAKPI GGVKKAKNII MMVSDGMSTG TLNMADLYAN
     RTFGVGSKWL DLYRGNKAVR ALMDTASASS MVTDSAAASS SWGGGMRVRN GSLNVGMRGE
     NPQPILQKFK ENGKKVGCVT TVPITHATPA GFCVNIDNRD GQALIAEMYL ELKFDVMMGG
     GSKYFSSKRK DGSIIPKYLT QGFKVAENRA EMLTLDKLKP VLGLFAEDGL PYEVDRKNDP
     ELMKAVPSIA EMTMKAIELM KDHRNGFALQ VEAGKVDWAA HSNDVAGLIF DQLAFDEAVG
     KVIEFAEKDG ETLVIITTDH GNSNPGLFYA DEADKKFDNL QRFKHSNTWL LTQLNQSFSE
     EKIKEIIKES QGLDMKLEDV KSLVAHFKDI VPGQLYNESN LPFYEYGKIM GKYTDVQWAG
     MNHTGDYVEL TMFGPGSERL TPFIKNYELH NFMLNAAEMP VHFLVKA
//
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