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Database: UniProt
Entry: A0A098S4V9_9BACT
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ID   A0A098S4V9_9BACT        Unreviewed;       376 AA.
AC   A0A098S4V9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Alkaline phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=IX84_15290 {ECO:0000313|EMBL:KGE87364.1};
OS   Phaeodactylibacter xiamenensis.
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Haliscomenobacteraceae;
OC   Phaeodactylibacter.
OX   NCBI_TaxID=1524460 {ECO:0000313|EMBL:KGE87364.1, ECO:0000313|Proteomes:UP000029736};
RN   [1] {ECO:0000313|EMBL:KGE87364.1, ECO:0000313|Proteomes:UP000029736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KD52 {ECO:0000313|EMBL:KGE87364.1,
RC   ECO:0000313|Proteomes:UP000029736};
RX   PubMed=25052393; DOI=10.1099/ijs.0.063909-0;
RA   Chen Z.Jr., Lei X., Lai Q., Li Y., Zhang B., Zhang J., Zhang H., Yang L.,
RA   Zheng W., Tian Y., Yu Z., Xu H.Jr., Zheng T.;
RT   "Phaeodactylibacter xiamenensis gen. nov., sp. nov., a member of the family
RT   Saprospiraceae isolated from the marine alga Phaeodactylum tricornutum.";
RL   Int. J. Syst. Evol. Microbiol. 64:3496-3502(2014).
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}.
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:KGE87364.1}.
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DR   EMBL; JPOS01000037; KGE87364.1; -; Genomic_DNA.
DR   RefSeq; WP_044222228.1; NZ_JPOS01000037.1.
DR   AlphaFoldDB; A0A098S4V9; -.
DR   STRING; 1524460.IX84_15290; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000029736; 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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000029736};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        85
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         44
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         258
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         267
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   376 AA;  41797 MW;  0F3D6B0FB71180A9 CRC64;
     MKFQLHYLLF LLLLPFGCKS PENLNLELLE REPPARNIIL LIGDGMGIGQ ISAGMYSHKK
     PLNIEQFNII GLQKTYAADD LITDSAAGAT AFATGHKTNK SALGLDASGN VVSNIFEQAK
     EREYALGLLT TSSIVHATPA GFFAHVPLRS QYEDIAEQLT NKEIDFFMGG GMRYFNNRDT
     DGRDLISDMR KNGYNIYDAY ETELYTITPD FSRGFGYFTA KEDPPKNKDG RKYLPPATRI
     GTRFLQKRSS RGFIFMVEGA QIDWAGHAND QEYMITEMLD FDEAVGEALA FAKRNKETLV
     IVTADHETGG YAIQPGSTRD SLIAGWTADN HTASLVPVFA YGPRAELFRG IYENTAIYDK
     MVQALGWGEE TAAEEK
//
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