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Database: UniProt
Entry: A0A1I1Q8T2_9BURK
LinkDB: A0A1I1Q8T2_9BURK
Original site: A0A1I1Q8T2_9BURK 
ID   A0A1I1Q8T2_9BURK        Unreviewed;       456 AA.
AC   A0A1I1Q8T2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:SFD18521.1};
GN   ORFNames=SAMN05216204_11881 {ECO:0000313|EMBL:SFD18521.1};
OS   Massilia yuzhufengensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1164594 {ECO:0000313|EMBL:SFD18521.1, ECO:0000313|Proteomes:UP000198639};
RN   [1] {ECO:0000313|EMBL:SFD18521.1, ECO:0000313|Proteomes:UP000198639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12041 {ECO:0000313|EMBL:SFD18521.1,
RC   ECO:0000313|Proteomes:UP000198639};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FOLD01000018; SFD18521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1Q8T2; -.
DR   STRING; 1164594.SAMN05216204_11881; -.
DR   Proteomes; UP000198639; 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; 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   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..456
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011503931"
FT   ACT_SITE        77
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         33
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         290
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         341
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         342
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         420
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   456 AA;  48410 MW;  5DBB4E77377A16B5 CRC64;
     MKKRLPLLLA ATVFSASAIA APKAKNIIFF LGDGMGPTTI TAARIYRHGE DGLLSFERLE
     RTARIKTYSN DFQTTDSAPS MGAYMTGVKI NQDGISMKDA RAIDPLKDAN GNQTLDQCGD
     NNGSIAPTIL ELAKARGKAV GAVTTTELTH ATPASTFSHV CHRDAAYTIA RQLVPGGAGY
     NPALGDGVDV LMGGGRHHFT PYDKAGNPQG RADGRDLLAE LAAQGYAVAN TRAGMMSARP
     GRKFVGIYSA DDHMDYALAR RPEQPTLGEM ALKAIDLLSK DPDGFFLMVE GGKIDHALHD
     NNAKNALADT VAFDEAIQAA IERMRALDPG LENTLVVVTA DHDHTMVLSG YPKRGSKVLD
     IVHDYANGQP KKDADGKSFT ALVFGNGKVR PDVRTDVDSA VALGDKYQQE AGVHTVYESH
     GGGDVKLYAV GAGSAPFKGT IENTQVFHLM KAAAGL
//
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