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Database: UniProt
Entry: A0A0Q5HGP3_9BURK
LinkDB: A0A0Q5HGP3_9BURK
Original site: A0A0Q5HGP3_9BURK 
ID   A0A0Q5HGP3_9BURK        Unreviewed;       466 AA.
AC   A0A0Q5HGP3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:KQQ87432.1};
GN   ORFNames=ASF77_17885 {ECO:0000313|EMBL:KQQ87432.1};
OS   Massilia sp. Leaf139.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ87432.1, ECO:0000313|Proteomes:UP000051760};
RN   [1] {ECO:0000313|EMBL:KQQ87432.1, ECO:0000313|Proteomes:UP000051760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ87432.1,
RC   ECO:0000313|Proteomes:UP000051760};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ87432.1, ECO:0000313|Proteomes:UP000051760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ87432.1,
RC   ECO:0000313|Proteomes:UP000051760};
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   -!- 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:KQQ87432.1}.
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DR   EMBL; LMOJ01000025; KQQ87432.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q5HGP3; -.
DR   STRING; 1736272.ASF77_17885; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000051760; 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   Reference proteome {ECO:0000313|Proteomes:UP000051760};
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..466
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006251542"
FT   ACT_SITE        87
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         43
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         160
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         162
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         351
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         352
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         430
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   466 AA;  49533 MW;  346135BD2C12354F CRC64;
     MTRTLLSTLL LAACCGAATA QTANTMRLAP KAQAKNIIFF LGDGMGPTTI TAARIFKAGE
     DGLLDFERLD RTARIKTYSA DAQVTDSAPS MGAYMTGVKI NNDVISLKDA KPVAPGKDGN
     GNPSIDRCGT GNGTAPMTIL ELAKAAGKSV GAITTTELTH ATPASTFSHV CDRDMAYNIA
     EQLVPGGAGF NPRLKDGVDV LMGGGRNHFT PYEAKRNPKG RGDGRDLVAE LEKQGYFIAN
     TRADMASGRP GQKFLGLYSA ESHLDYASKR RPEQPTLAEM TAKSIELLST NPKGFFLMVE
     GGKIDHALHD TNARNALIET VAFDEAIQTA VERMRAIDPG LDNTLIVVTA DHDHTMVLNG
     YPKRGNPVLD IVRGYRDGEP TRDADGKTYT TLVFGNGPNR PDVRADVDSA KALAADYHQE
     TGVKWSSESH GGGDVKLYAA GAGSAPFRGT IENTHVFTLM KAAAGL
//
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