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Database: UniProt
Entry: A3NQR7_BURP0
LinkDB: A3NQR7_BURP0
Original site: A3NQR7_BURP0 
ID   A3NQR7_BURP0            Unreviewed;       467 AA.
AC   A3NQR7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Alkaline phosphatase family protein {ECO:0000313|EMBL:ABN90676.1};
GN   OrderedLocusNames=BURPS1106A_0405 {ECO:0000313|EMBL:ABN90676.1};
OS   Burkholderia pseudomallei (strain 1106a).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=357348 {ECO:0000313|EMBL:ABN90676.1, ECO:0000313|Proteomes:UP000006738};
RN   [1] {ECO:0000313|EMBL:ABN90676.1, ECO:0000313|Proteomes:UP000006738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1106a {ECO:0000313|EMBL:ABN90676.1,
RC   ECO:0000313|Proteomes:UP000006738};
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (FEB-2007) 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; CP000572; ABN90676.1; -; Genomic_DNA.
DR   RefSeq; WP_004522963.1; NC_009076.1.
DR   AlphaFoldDB; A3NQR7; -.
DR   GeneID; 56527395; -.
DR   KEGG; bpl:BURPS1106A_0405; -.
DR   HOGENOM; CLU_008539_4_1_4; -.
DR   Proteomes; UP000006738; Chromosome I.
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..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..467
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002655936"
FT   ACT_SITE        84
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         158
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         350
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         431
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;  48616 MW;  E00C0EA8CCBEB264 CRC64;
     MSTIKRIAAA AFAAAALSGG FGHAAHAAGQ AKNVIFFLGD GMGPATVTAS RLYKVGEAGQ
     LTMEKLPRTA RIKTFSNDAQ TTDSAPSMAA YMTGVKMNNE VLSMSPDTRA IAPGSDANGN
     KTVNRCGVGN GTPATTLLEL AKARGKAVGA ITTTELTHAT PAATYSHICH RDAQYDIAAQ
     AVPGGAGYNA ALGDGVDVLM GGGRNHWTPY DPLANRRGRA DGRNLLAELQ AKGYAVVATK
     DQLAQAGAGK LIGLFSTTSH LEYELDRVAG KGEGATQPSL AEMTAKAIDV LRKNPNGYFL
     MVEGGRIDHA LHGTNAKRAL EDTVAFDEAI RTALAKVDLS DTLIVVTADH DHTMTINGYS
     KRGNPVLDIS RNYRDGQPNK DADGNPYTTL VFGNGANRPN VRVPVDSSTA TNDAYLQEVG
     VRMGSAGSET HGGGDVMLFA DGAGAKAFKG TLDNTKVFGL VKAAFGF
//
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