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Database: UniProt
Entry: A0A0W1L3H3_9GAMM
LinkDB: A0A0W1L3H3_9GAMM
Original site: A0A0W1L3H3_9GAMM 
ID   A0A0W1L3H3_9GAMM        Unreviewed;       529 AA.
AC   A0A0W1L3H3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:KTF14029.1};
GN   ORFNames=ATS75_12955 {ECO:0000313|EMBL:KTF14029.1};
OS   Pseudoalteromonas sp. H105.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1348393 {ECO:0000313|EMBL:KTF14029.1, ECO:0000313|Proteomes:UP000054685};
RN   [1] {ECO:0000313|EMBL:KTF14029.1, ECO:0000313|Proteomes:UP000054685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H105 {ECO:0000313|EMBL:KTF14029.1,
RC   ECO:0000313|Proteomes:UP000054685};
RA   Duhaime M.B., Sullivan M.B., Wichels A.;
RT   "Six Pseudoalteromonas strains isolated from surface waters of Kabeltonne
RT   offshore Helgoland, North Sea.";
RL   Submitted (DEC-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:KTF14029.1}.
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DR   EMBL; LOFH01000007; KTF14029.1; -; Genomic_DNA.
DR   RefSeq; WP_058560843.1; NZ_LOFH01000007.1.
DR   AlphaFoldDB; A0A0W1L3H3; -.
DR   STRING; 1348393.ATS75_12955; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000054685; 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..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..529
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006925010"
FT   ACT_SITE        116
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         66
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         179
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         348
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         394
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         395
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         490
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   529 AA;  56403 MW;  15DFC4CF8A64460F CRC64;
     MKINKIATAI GFTLVLSAAA NAGVLPQSQT QSQWYESAQT TLATKQSQAQ EEQLTKAKNV
     ILFVGDGMGV STLTAARILA GQRDGQLGEE GLLSFEAFPY SAQVKTYNVD AQTPDSAGTM
     TAMASGVKTD VGVIGVNENI QRGDCSTVFG NELITTTELA EIKGLATGVI STARITHATP
     AATYAKSADR NWEDVSDMPE GAVTAGCEDI ASQLVNFEKN LEARFLGTDV DGIDVVMGGG
     RRHFLPKDAT FNSADAMSEV EGDRTDERDL TAEWQANYPD GQYVMDKAGF EAISADTKQV
     LALFNESHMQ YEADRENDIA GEPSLSEMTE KAINILDNNE KGFFLTVESG RIDHAHHAGN
     AYNALNDTIE FAKAVQAAVD NTNPEETLIL VTADHSHVFT IAGYPKRGNP ILGKVVAVGK
     EDPSLAADGM PYTTVGYANG LGFRDLGDET NADAAYLEGP NVGRHDLTTI DTTRAGFHQE
     ATVPLGSETH AGEDITLHAK GPGAQLAQGV VEQNVVFHLV NQALELIKQ
//
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