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}.
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; 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
//