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Database: UniProt
Entry: G4RDA6_PELHB
LinkDB: G4RDA6_PELHB
Original site: G4RDA6_PELHB 
ID   G4RDA6_PELHB            Unreviewed;       486 AA.
AC   G4RDA6;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AEQ50732.1};
GN   OrderedLocusNames=KKY_693 {ECO:0000313|EMBL:AEQ50732.1};
OS   Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 /
OS   B2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Devosiaceae; Pelagibacterium.
OX   NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ50732.1, ECO:0000313|Proteomes:UP000008850};
RN   [1] {ECO:0000313|EMBL:AEQ50732.1, ECO:0000313|Proteomes:UP000008850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2
RC   {ECO:0000313|Proteomes:UP000008850};
RX   PubMed=22156395; DOI=10.1128/JB.06343-11;
RA   Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., Zhu X.F.,
RA   Liu Y.F., Li P.F., Ni P.X., Wu M.;
RT   "Complete genome sequence of Pelagibacterium halotolerans B2T.";
RL   J. Bacteriol. 194:197-198(2012).
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}.
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DR   EMBL; CP003075; AEQ50732.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4RDA6; -.
DR   STRING; 1082931.KKY_693; -.
DR   KEGG; phl:KKY_693; -.
DR   PATRIC; fig|1082931.4.peg.688; -.
DR   eggNOG; COG1785; Bacteria.
DR   HOGENOM; CLU_008539_4_1_5; -.
DR   Proteomes; UP000008850; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000008850};
KW   Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        105
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         55
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         55
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         166
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         306
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         352
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
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         447
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   486 AA;  51193 MW;  C9D30D494E9D242F CRC64;
     MSTLSIALCA STALGQDVVQ AQSDYFTAGQ DLLAERVAAQ PNTNQAMNVI LFVADGMGIG
     TNYGIRVFQG QEMGLLGEEH NLPYDLYPHS AIIKTYNINA QTPDSAPTAG AMNTGVKQVF
     NTINMADTVV HNDCSTEAPL TLFSELVSEA GKSVGVVSTA RITHATGAAV YAKTANRNWE
     NNAPEGCTDI ATQLIDQMEA GVIDIALGGG ARSFAPEGTE LEVGTGNRPD DVNLIDRAAE
     IGAQVVYNSE DLAAADLSAP VLGLFTNSDM NYEHDRPEGE PSLADMTTAA IESLQGDEDG
     FYLMVEAGRV DHASHGGNAH RAFTDGVALA EAVAAAQEMV DLENTLIIVT ADHEHVMSFN
     GYCGRGTPIT GLCMGVAAGQ VEHSGEPVTA ADGKPYTVVS YTNGAGSVLI EQEDGTYSGE
     RPDLTQEEAQ DPDYLQQALI PMGSETHSGV DVGLWANGPW SHLFGGTMDQ EMIFHVMNHA
     VFGAAE
//
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