ID A0A0U2VJ81_9GAMM Unreviewed; 529 AA.
AC A0A0U2VJ81;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ALS34512.1};
GN Name=phoA {ECO:0000313|EMBL:ALS34512.1};
GN ORFNames=PTRA_a3556 {ECO:0000313|EMBL:ALS34512.1};
OS Pseudoalteromonas translucida KMM 520.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1315283 {ECO:0000313|EMBL:ALS34512.1};
RN [1] {ECO:0000313|EMBL:ALS34512.1, ECO:0000313|Proteomes:UP000065261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMM 520 {ECO:0000313|EMBL:ALS34512.1,
RC ECO:0000313|Proteomes:UP000065261};
RA Murphy D.;
RL Submitted (MAR-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|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; CP011034; ALS34512.1; -; Genomic_DNA.
DR RefSeq; WP_058374445.1; NZ_CP011034.1.
DR AlphaFoldDB; A0A0U2VJ81; -.
DR KEGG; ptn:PTRA_a3556; -.
DR PATRIC; fig|1315283.4.peg.3103; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000065261; Chromosome I.
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 Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..529
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006833031"
FT ACT_SITE 116
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 490
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 529 AA; 56171 MW; F5DC4A20741BD993 CRC64;
MKIKKVAAAI ALTFAFNAAS YADVLPQSQK DSSWYSAAQT KLTTKTTQAQ SVKATKAKNI
ILFVGDGMGV STLTAARILQ GQRNNQSGEE GYLSFETFPY SAQVKTYNVD AQTPDSAGTM
TAMISGVKTD VGVIGVNENI ERGVCSTVAG NELLTATELA EIKGLATGVI STARITHATP
AATYAKSADR NWEDISDMPE DAIAAGCEDI ASQLINFEKN LEARFVGTDI DGLDVVMGGG
RRHFLPKDAA ANSTDAVSAI EGDRTDNRNL ISEWQAQYPT ATYVMDQTGF DNIADDATKV
FGLFNESHMQ YEADRANDIA GEPSLTDMTT KAIEVLGKND KGFFLTVESG RIDHAHHAGN
AYNALNDTIE LAKAVQAAVD NTNPEETLIL VTADHSHVFT IAGYPKRGNP ILGQVVAVGE
RAPSLAADNK PYTTVGYANG LGFRNLGDET DADASYASAA VAGRVELQGI DTTTPGFHQE
TTVPLASETH AGEDISLHAK GPGAQLAQGV IEQNVVFHII NQALELTQQ
//
