ID A0A1Q2GTV9_9GAMM Unreviewed; 429 AA.
AC A0A1Q2GTV9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AQP98546.1};
GN ORFNames=B0W48_01290 {ECO:0000313|EMBL:AQP98546.1};
OS Pseudoalteromonas aliena.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=247523 {ECO:0000313|EMBL:AQP98546.1, ECO:0000313|Proteomes:UP000188243};
RN [1] {ECO:0000313|EMBL:AQP98546.1, ECO:0000313|Proteomes:UP000188243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EH1 {ECO:0000313|EMBL:AQP98546.1,
RC ECO:0000313|Proteomes:UP000188243};
RA Kim E., Heo E., Kim H., Kim D.;
RT "Complete genome sequence of the cold-active Pseudoalteromonas aliena
RT strain EH1 isolated from Arctic seawater.";
RL Submitted (FEB-2017) 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}.
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; CP019628; AQP98546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2GTV9; -.
DR STRING; 247523.B0W48_01290; -.
DR KEGG; paln:B0W48_01290; -.
DR Proteomes; UP000188243; 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; 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..429
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013360873"
FT ACT_SITE 80
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 429 AA; 46495 MW; 4CCE923B21948016 CRC64;
MKKQFSLLAL LCTASGAYAE SAPKNVIYMI GDGMGPAYTT AYRYFKDDPA TKEIEGTVFD
TILKGMAHTY PDDHTYVTDS AAGATALSSG HKSYNGAIAV DTHKKAVKTM LEIAKERGMT
TALVATSQIN HATPASFASH NESRNNYDAI ANDYIDNKIV GKLPVDLMLG GGTKYFIRDD
RNLVDEFKAA GYQYGDDINN LGQITQIPAL GLYAPKGLPF ALDENPTRLT QLTSKALDLL
DTQNKSGFFV MIEGSQIDWC GHANDIACAM AEMDDFAKSI EKAKAYVDKN KDTILVVTAD
HSTGGLTLGA HGQYKWETEV VKGVKATAGK LTQLLLDAKD LKSVWTTNTS IEFTTENQIK
LEQAKKMGDK ALNLAVKSII SDTSFTGWTT GGHTAVDVQV FAYGKGSEHF IGSQNNTDIA
DKLIGFIER
//
