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Database: UniProt
Entry: A0A0F2PSR3_9FIRM
LinkDB: A0A0F2PSR3_9FIRM
Original site: A0A0F2PSR3_9FIRM 
ID   A0A0F2PSR3_9FIRM        Unreviewed;       460 AA.
AC   A0A0F2PSR3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:KJS17248.1};
GN   ORFNames=VR69_05840 {ECO:0000313|EMBL:KJS17248.1};
OS   Peptococcaceae bacterium BRH_c4b.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629717 {ECO:0000313|EMBL:KJS17248.1, ECO:0000313|Proteomes:UP000033446};
RN   [1] {ECO:0000313|EMBL:KJS17248.1, ECO:0000313|Proteomes:UP000033446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c4b {ECO:0000313|EMBL:KJS17248.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-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:KJS17248.1}.
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DR   EMBL; LADO01000022; KJS17248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2PSR3; -.
DR   STRING; 1629717.VR69_05840; -.
DR   PATRIC; fig|1629717.3.peg.1907; -.
DR   Proteomes; UP000033446; 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..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..460
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002456643"
FT   ACT_SITE        110
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         51
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         51
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         163
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         322
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         327
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         331
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         372
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         373
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   460 AA;  49641 MW;  19D869C4BFEB1C1F CRC64;
     MISVKTLKKN ALSMVLAGSL VFAQTSGIAM AQGSVAPDKP IAKNIIVMIS DGCGYNQIDA
     ANLYRYGKTG VQPYEHFPVK YGMSTYSVGS YNPQQAWGSF DYVKEGATDS AAAATAMSTG
     FKTYDAAIGV DNDKQPLKNV LERAEELGKA TGVITSVQFS HATPAGFVAH NESRNNYSEI
     ANEMLQKSST DVIMSAGHPL YDNDGKKASK TNYKYVGGES TWQGLLDGSL QVADADGDGK
     ADPWTLIQER KDFQKLMSGE TPTRVCGVAQ VASTLQQSRS GDDKANPYVV PLNETVPMLE
     EMTKGALNVL DNDKDGFFLM VEGGAIDWAG HANQSGRMIE EENEFNKSVE AVNNWVEKNS
     NWGETLLIVT GDHECGYLTG PGSGQAAGSQ PVWNPLKNNG AGNLPGMQWN SPEHTNSLIP
     FFAKGDAARI FKSYADEKDP VRGSYIDNTE IAKVIFDIME
//
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