GenomeNet

Database: UniProt
Entry: A0A0P0D6W2_9FLAO
LinkDB: A0A0P0D6W2_9FLAO
Original site: A0A0P0D6W2_9FLAO 
ID   A0A0P0D6W2_9FLAO        Unreviewed;       580 AA.
AC   A0A0P0D6W2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ALJ06673.1};
GN   ORFNames=APS56_00580 {ECO:0000313|EMBL:ALJ06673.1};
OS   Pseudalgibacter alginicilyticus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Pseudalgibacter.
OX   NCBI_TaxID=1736674 {ECO:0000313|EMBL:ALJ06673.1, ECO:0000313|Proteomes:UP000057981};
RN   [1] {ECO:0000313|EMBL:ALJ06673.1, ECO:0000313|Proteomes:UP000057981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HZ-22 {ECO:0000313|Proteomes:UP000057981};
RA   Gilbert D.G.;
RL   Submitted (OCT-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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP012898; ALJ06673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P0D6W2; -.
DR   STRING; 1736674.APS56_00580; -.
DR   KEGG; ahz:APS56_00580; -.
DR   PATRIC; fig|1736674.3.peg.124; -.
DR   Proteomes; UP000057981; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd16012; ALP; 1.
DR   CDD; cd08577; PI-PLCc_GDPD_SF_unchar3; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   InterPro; IPR039559; AIM6_PI-PLC-like_dom.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR   Pfam; PF00245; Alk_phosphatase; 3.
DR   Pfam; PF13653; GDPD_2; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 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:UP000057981};
KW   Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        310
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         269
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         363
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         469
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         474
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         478
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         516
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         517
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   580 AA;  64732 MW;  FDA838E3DD8F0978 CRC64;
     MGQEIGLPYK IHSHNDYKQK VPFWTAYSCG LNSIEIDVIL KNDTLFVAHD EVDITSFNTI
     ENLYLDPIQK TFQLTPQSYQ QIQLLIDIKT EAIATLKTLI NTLKLYPDIT NSEHISFIVS
     GNQPKPESYN NYPSFIKFDY QNLKPLSEEA LNKVGLISLP FSKFSNWNGK GRLTKEDHKK
     VSEIINKAHS FNKPFRFWGC PDSKTAWKAF AELGVDYINT DMPYTASTYI HSLSDRIHRN
     TFYSTVYKPT FHSIKKNQGV KNIILMIGDG YGLSQISAAA LSNHGELTLT QLKSIGLLKT
     QAADDFTTDS AAAGTAIATG EKTYNRSIGM NINRVPIENM TELLNKKNYN TGFITTDVIT
     GATPSAFYAH QLDRDMTKEI ASDLIKSNIS LFMGGGASSY SDIFVNSNFT ILNSLNEIAS
     SKKKKVGYFL SEKGVPSINS GRDHILAEAT KTGLEYFSNQ NKPFFLMIEA AQIDSFGHRN
     DISGIVTEAI DFDKAITEAI KYADTHKNTL VIITADHETS GLSIPQGNLE SNKVEGDFST
     YDHTGVMVPI FAYGPKSEVF TGVYENNEVF HKIKDVLNIK
//
DBGET integrated database retrieval system