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Database: UniProt
Entry: H3NSN4_9GAMM
LinkDB: H3NSN4_9GAMM
Original site: H3NSN4_9GAMM 
ID   H3NSN4_9GAMM            Unreviewed;       456 AA.
AC   H3NSN4;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:EHQ57097.1};
GN   ORFNames=OMB55_00008180 {ECO:0000313|EMBL:EHQ57097.1};
OS   gamma proteobacterium HIMB55.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX   NCBI_TaxID=745014 {ECO:0000313|EMBL:EHQ57097.1, ECO:0000313|Proteomes:UP000003408};
RN   [1] {ECO:0000313|EMBL:EHQ57097.1, ECO:0000313|Proteomes:UP000003408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIMB55 {ECO:0000313|EMBL:EHQ57097.1,
RC   ECO:0000313|Proteomes:UP000003408};
RX   PubMed=22493201; DOI=10.1128/JB.00171-12;
RA   Huggett M.J., Rappe M.S.;
RT   "Genome Sequence of Strain HIMB55, a Novel Marine Gammaproteobacterium of
RT   the OM60/NOR5 Clade.";
RL   J. Bacteriol. 194:2393-2394(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}.
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:EHQ57097.1}.
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DR   EMBL; AGIF02000001; EHQ57097.1; -; Genomic_DNA.
DR   AlphaFoldDB; H3NSN4; -.
DR   STRING; 745014.OMB55_00008180; -.
DR   PATRIC; fig|745014.4.peg.835; -.
DR   eggNOG; COG1785; Bacteria.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000003408; 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   Disulfide bond {ECO:0000256|PIRSR:PIRSR601952-3};
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:UP000003408};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..456
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003591025"
FT   ACT_SITE        84
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         35
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         135
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         137
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         321
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         368
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         420
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   DISULFID        150..169
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-3"
SQ   SEQUENCE   456 AA;  48491 MW;  7F9CA417D5B1D122 CRC64;
     MRFFNAPTLL TTLLGIFSAQ SAYADPKSVI LIIGDGFDDV HVTMGRNYLS GQGGTLTLDT
     MPFRGAVQVE TVDDNGTPIY VADSANTATT LATGSVTRIG RVGKDRDDES VTTVLEAAAA
     AGYKTGIVST ASVTDATPAA FAAHVGIRAC ENPVTIRGGE KYGVTFPGCP KDLEENGGAG
     SISEQLATAD VDVILGGGME HFAAQYETQP TALDKATESG ATVLTSAAQL NANYSGRVIG
     LFSEDTMPVQ WQGSDGRSAE DIERSWLNLA HEMIGSITPP ETISCVDNPA FEDMPSLNAM
     TRFALRHLDK ENERGFFLTI ESASIDKKSH VRDPCGSIGE IAQLEQALAA ALEHAANNPD
     TLIIVTADHA QAAQIVPEPT LYTGLPIPVF SPGKVARVET PEGSVMRINY ATNNIQSEEH
     TGANVPLFAN AEGNKVLSPF MRQREIYQAM MQYLEL
//
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