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Database: UniProt
Entry: A0A255ZB74_9FLAO
LinkDB: A0A255ZB74_9FLAO
Original site: A0A255ZB74_9FLAO 
ID   A0A255ZB74_9FLAO        Unreviewed;       471 AA.
AC   A0A255ZB74;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:OYQ38154.1};
GN   ORFNames=CHU92_06405 {ECO:0000313|EMBL:OYQ38154.1};
OS   Flavobacterium cyanobacteriorum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2022802 {ECO:0000313|EMBL:OYQ38154.1, ECO:0000313|Proteomes:UP000216605};
RN   [1] {ECO:0000313|EMBL:OYQ38154.1, ECO:0000313|Proteomes:UP000216605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH021 {ECO:0000313|EMBL:OYQ38154.1,
RC   ECO:0000313|Proteomes:UP000216605};
RA   Cai H.;
RT   "Flavobacterium cyanobacteriorum sp. nov., isolated from cyanobacterial
RT   aggregates in a eutrophic lake.";
RL   Submitted (JUL-2017) 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:OYQ38154.1}.
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DR   EMBL; NOXV01000232; OYQ38154.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255ZB74; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000216605; 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:UP000216605};
KW   Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        100
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         50
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         151
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         279
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         284
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         288
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
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         431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   471 AA;  51665 MW;  4EE7B426ADF87995 CRC64;
     MDRRKFFRNG SLFTLGATLL NPFESRALLP ATGEAYKNKK AKNIIFLVSD GMSSGTLNMA
     DLYLSRKTGK GSNWLQLYKD QRVSRALMDT ASANSVVTDS SAGSSAWGGG VRVNNGSLNV
     GPSGEKYLPI WQKFKKAGKM AGCVTTVPVT HATPAGFCVN NNSRGAQEEI AEEYHAIGFD
     VMMGGGNNYF SAAVRKDKKD VYAAYKAKGW QVVRNRNEMM AADNNKPLLG VFADDALPYS
     IDRRSSRELT DTTPTLAEMT GKAIDRMKGH KNGFVLQVEA GKVDWGAHAN DIAAVLYDQV
     AFDEAIKVAV DFAEKDKETL VIITTDHGNA NPGIIYGRDA NANFDSIQNY THTNEWILNQ
     VKPGSTVAQV REMISSANGA PVSEENAKVI LSYYDGLQKE EGLYNYKKLP FRAFAEMQKA
     TNSVGWISMD HSADYVELAM FGPGSELLKP FVKNTDLHYL MLQAAEVENK F
//
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