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Database: UniProt
Entry: A0A1K1PNV5_9PSEU
LinkDB: A0A1K1PNV5_9PSEU
Original site: A0A1K1PNV5_9PSEU 
ID   A0A1K1PNV5_9PSEU        Unreviewed;       398 AA.
AC   A0A1K1PNV5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:SFW49201.1};
GN   ORFNames=SAMN04489730_0825 {ECO:0000313|EMBL:SFW49201.1};
OS   Amycolatopsis australiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=546364 {ECO:0000313|EMBL:SFW49201.1, ECO:0000313|Proteomes:UP000182740};
RN   [1] {ECO:0000313|EMBL:SFW49201.1, ECO:0000313|Proteomes:UP000182740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44671 {ECO:0000313|EMBL:SFW49201.1,
RC   ECO:0000313|Proteomes:UP000182740};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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|ARBA:ARBA00005984, ECO:0000256|RuleBase:RU003946}.
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DR   EMBL; FPJG01000006; SFW49201.1; -; Genomic_DNA.
DR   RefSeq; WP_072474982.1; NZ_FPJG01000006.1.
DR   AlphaFoldDB; A0A1K1PNV5; -.
DR   STRING; 546364.SAMN04489730_0825; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000182740; 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; IPR018299; Alkaline_phosphatase_AS.
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.
DR   PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, 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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..398
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013244644"
FT   ACT_SITE        84
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         137
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         279
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         283
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         321
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         322
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   398 AA;  41378 MW;  FD6D361A4699EA7D CRC64;
     MRSGVLVAAL VLFGSGVAAS AAEPAAAHAR NVIYIQGDGL GPGQRELIRL ATVGRHGDLA
     MNRLPVTGLV HTDPDDPEEV VTDSAAAATA LATGHKTRNG AVGVDPAGRP LRTVLEDAKR
     AGKATGLVTT AQVTGASPAA FAAHVPSRDA QSDIARQYLV DSRPDVLLGG GEDWWFPKGE
     PGAWPDKPGE ESRSTHGNLV AQAQRTGYTY VRNAQELQRT RASRILGLFA NEDMVDYGPD
     GVGKYAPSVP LVQMAKKALD TLSANPHGFF LFLEEEGIDG MSHENNAHAV IDAGRALDAT
     VAEVLRFVRS HPDTLVIVGG DHETGGLSIE NADGPNEGDE DGPFPVPGTN LAFKVDWTTG
     DHSGASTPVT ATGPGSAALD GTVDNTDVHR AMAQAFGS
//
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