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Database: UniProt
Entry: A0A257C6Z5_9BURK
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Original site: A0A257C6Z5_9BURK 
ID   A0A257C6Z5_9BURK        Unreviewed;       679 AA.
AC   A0A257C6Z5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:OYT84967.1};
GN   ORFNames=CFE46_18795 {ECO:0000313|EMBL:OYT84967.1};
OS   Burkholderiales bacterium PBB6.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=2015568 {ECO:0000313|EMBL:OYT84967.1, ECO:0000313|Proteomes:UP000216978};
RN   [1] {ECO:0000313|EMBL:OYT84967.1, ECO:0000313|Proteomes:UP000216978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBB6 {ECO:0000313|EMBL:OYT84967.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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}.
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:OYT84967.1}.
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DR   EMBL; NKIH01000008; OYT84967.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257C6Z5; -.
DR   Proteomes; UP000216978; 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; 2.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF72; 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   Reference proteome {ECO:0000313|Proteomes:UP000216978};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..679
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012287724"
FT   ACT_SITE        213
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
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         274
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         453
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         458
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         462
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         500
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         501
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         628
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   679 AA;  72831 MW;  0DFE09C5CC7FD019 CRC64;
     MSHPRLSRTL FMAPLGCLFI AATAAQAAPV VSRLTPPSEL FSSGQPEPVI ARFLPGQRFD
     LQATLRPDGG QRITEARFEV DGKRVAGDVA LRDCETGCLK GVPQNAAIAT LRAVTVTAPG
     RHEFRVLARQ ADGQSVVARG NFDVVPFQTP SGQKVRNIII LLGDGMGASH RTAARIVQGR
     YAQGKVSSPL AMDTFPATAL VKTSSLNSVV TDSSPGMTAY VLGNKNNNNE EGVFPDDTVD
     AFDNPRIEYL SEYLHRLQGK ALGIVTTADV FDSTPAGNAV HTSSRGAGTG IVDQFLDDRH
     ATGLQVLMGG GRRWFLPAGT VGSSRDERTD YAFSSTEPHT AEIVRRWGVS AGAVDTGRDL
     IADFQQAGFR YAANRQAMDT LPVDTDKVLG LFAFSNMNVA LDKIDGRRGR RTGVSGTVVD
     DFGLPDQPML DEMATVALRA LSRQPKGFVL MVEGASIDKQ AHNMDTERWM LDTLEFDRAV
     KVAQDYARQH ADTLVIVTAD HECSGAAVIG GSRVSDQALQ ELIKAGGPEN LRDKVVGVYE
     QAGFPRYQLA ADGYPETTNI DRRVLVGYAA NADRYEDWRT NPLPLRSGGA PFVQVEPLKL
     YPAGPLQRDD AEGRFLITGQ VPGDSAVHTA TDVPLSAYGP GALTFTGVID NTDVFFKLAQ
     AAMRGTVAPA DASGSKKPR
//
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