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Database: UniProt
Entry: A0A0M1NIG5_9BACL
LinkDB: A0A0M1NIG5_9BACL
Original site: A0A0M1NIG5_9BACL 
ID   A0A0M1NIG5_9BACL        Unreviewed;       444 AA.
AC   A0A0M1NIG5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:KOR82058.1};
GN   ORFNames=AM231_21075 {ECO:0000313|EMBL:KOR82058.1};
OS   Paenibacillus solani.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1705565 {ECO:0000313|EMBL:KOR82058.1, ECO:0000313|Proteomes:UP000036932};
RN   [1] {ECO:0000313|Proteomes:UP000036932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-22460 {ECO:0000313|Proteomes:UP000036932};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (AUG-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:KOR82058.1}.
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DR   EMBL; LIUT01000005; KOR82058.1; -; Genomic_DNA.
DR   RefSeq; WP_054404381.1; NZ_LIUT01000005.1.
DR   AlphaFoldDB; A0A0M1NIG5; -.
DR   PATRIC; fig|1705565.3.peg.136; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000036932; 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   Reference proteome {ECO:0000313|Proteomes:UP000036932};
KW   Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        88
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         48
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         48
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         139
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         263
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         268
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="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         310
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         399
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   444 AA;  48089 MW;  A534200C5A8A8709 CRC64;
     MKVRISFISI SVLVLVCSIL GFQTNLISEA AASNSRAKAK NVIFMIPDGF SPAYAANYRL
     YKGEPSVMDS MLVGMVRTYS ADSALTDSAA AATAMATGYK TNNGMIGRTP DGIERKTILE
     AAREQGKAIG LVATSSITDA TPAAFSSHVF SRKDESDIAQ QQLQLADVLL GGGKLFFLPE
     TMGGKQSSRN LLEEAKQRGY RVVENRAQLE SASGNQVLGL FADGDMAPEL DREHTNEPSL
     KEMTGKAIDI LRRGKDGFFL LVEGSQIDSA GHYNDAAWAM KDTESFEEAV GLARKFAEED
     GNTLVVIAGD HDTGGMTVGG YDQTDAKLEV LRQVHASGLY MTKELKNDRS NVKEVLKAYA
     GIDVTTEEEI AIINAADAMQ AINHVISKRS LVGWHTYLHT GVDVPLYAFG PGSELFRGLH
     NNTDLPHLVS RAMNIDFGDE KYKK
//
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