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Database: UniProt/TrEMBL
Entry: A0A0U3I6B4_9GAMM
LinkDB: A0A0U3I6B4_9GAMM
Original site: A0A0U3I6B4_9GAMM 
ID   A0A0U3I6B4_9GAMM        Unreviewed;       433 AA.
AC   A0A0U3I6B4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ALU45606.1};
GN   ORFNames=AT705_21960 {ECO:0000313|EMBL:ALU45606.1};
OS   Pseudoalteromonas rubra.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=43658 {ECO:0000313|EMBL:ALU45606.1, ECO:0000313|Proteomes:UP000069015};
RN   [1] {ECO:0000313|EMBL:ALU45606.1, ECO:0000313|Proteomes:UP000069015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 6842 {ECO:0000313|EMBL:ALU45606.1,
RC   ECO:0000313|Proteomes:UP000069015};
RA   Li B., Wang X.;
RT   "Complete genome sequence of Pseudoalteromonas rubra SCSIO 6842, harboring
RT   a conjugative plasmid.";
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|ARBA:ARBA00005984, ECO:0000256|RuleBase:RU003946}.
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DR   EMBL; CP013612; ALU45606.1; -; Genomic_DNA.
DR   RefSeq; WP_058798475.1; NZ_CP013612.1.
DR   AlphaFoldDB; A0A0U3I6B4; -.
DR   KEGG; prr:AT705_21960; -.
DR   Proteomes; UP000069015; Chromosome 2.
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; 1.10.60.40; -; 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; 1.
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   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..433
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006839735"
FT   ACT_SITE        81
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         33
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         132
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         134
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         255
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         397
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   433 AA;  47100 MW;  F179849032240D78 CRC64;
     MTRNISALAF ALGCTLSNSV FAAPKNIIYM IGDGMGPAFT TAYRYMQDDK ATKFVEPTVF
     DSILVGMAHT YPDDDTVVTD SAAGATALST AEKSYNGAIA VDTHKQSLKT MLEIAKEQGM
     TTALVATSQI NHATPASFAA HNESRRNYDE IADDYIDNKI AGKLPVDLLL GGGTKYFIRD
     DRNLVSEFKE AGYQYADAFD KLDSLSRLPA LGLFAEVAFP HAIDSEEPKR LTTMTNKALD
     LLDKNNEKGF FVMIEGSQID WCGHANDIAC AMKEMDDFAG AITAAKAYID KNPDTILVVT
     ADHSTGGLTL GSNGVYQWKT NVVAKAKASV KELTNTISEA KPKQMAKFWT QLTGLPFDED
     TKKALIKAQK DSKEALYKAA NKIINDASYT GWTTKGHTAI DVQVFAYGEG RDAFIGSLNN
     TQIADKLISY IEK
//
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