ID A0A0F6A6Z8_9GAMM Unreviewed; 537 AA.
AC A0A0F6A6Z8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Alkaline phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=N479_20675 {ECO:0000313|EMBL:KKE81935.1};
OS Pseudoalteromonas luteoviolacea S4054.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE81935.1, ECO:0000313|Proteomes:UP000033434};
RN [1] {ECO:0000313|EMBL:KKE81935.1, ECO:0000313|Proteomes:UP000033434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4054 {ECO:0000313|EMBL:KKE81935.1,
RC ECO:0000313|Proteomes:UP000033434};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KKE81935.1}.
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; AUXW01000173; KKE81935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F6A6Z8; -.
DR PATRIC; fig|1129367.4.peg.4208; -.
DR Proteomes; UP000033434; 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; 1.10.1200.140; Alkaline phosphatase, crown domain; 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 InterPro; IPR042085; Ap_crown.
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; PS51257; PROKAR_LIPOPROTEIN; 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 Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT ACT_SITE 101
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 537 AA; 58378 MW; 6A4482CF630033A8 CRC64;
MLLGLKKLLP LSVVLPLSLC GCKLIESNAY QEKISSPQIK NVILLIGDGM GPQQVGLLEE
YATRAPQSVY QGESSAIAKL ANQGVTGLSL HGPADKLVVD SACSATQLAT GVASGSEMIG
LNRAGHKVPT ILQKAKAFGK STGLVSDTRL THATPAAFAS HQIHRSMENA IAEQMVLSDS
VDVMLSGGLR HFIPKAYVLS AQQTVLETKL ANSGLSLKSK RQDSNNILQQ AENQGYELVF
TKSQLLEAQR GRILGLFANS AMVDGIEASN KRYLGQPSLR DMTEVAIKKL SKNPKGFFLM
VEGGQIDWAG HNNDAGTLLH EMLKFDSAVE SVLQWANGRD DTVVIVTADH ETGGFGFSYS
GMNLPQAVQL DNLNRDVYKP NYNFGELAIL DKLYLQKRSY AEMWKAAKGG KAHPEAEQLV
EIVNQNSEFK IDNTDANAIL AEQKNAFFKR GHKSLGLKTA GKINDFAPFY VYLNERPLNL
IGRALAAKQN IVWSTGTHTH TPVGVFALGP SYAIEQFNGL HTHVELGKIM QRVLFGY
//
