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Database: UniProt
Entry: Q1ZSX3_PHOAS
LinkDB: Q1ZSX3_PHOAS
Original site: Q1ZSX3_PHOAS 
ID   Q1ZSX3_PHOAS            Unreviewed;       473 AA.
AC   Q1ZSX3;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:EAS64854.1};
GN   ORFNames=VAS14_04023 {ECO:0000313|EMBL:EAS64854.1};
OS   Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS   CCUG 15956)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS64854.1, ECO:0000313|Proteomes:UP000001603};
RN   [1] {ECO:0000313|EMBL:EAS64854.1, ECO:0000313|Proteomes:UP000001603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S14 {ECO:0000313|EMBL:EAS64854.1,
RC   ECO:0000313|Proteomes:UP000001603};
RX   PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA   Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA   DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA   Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA   Robb F.T., Kjelleberg S., Cavicchioli R.;
RT   "The genomic basis of trophic strategy in marine bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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   -!- 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:EAS64854.1}.
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DR   EMBL; AAOJ01000002; EAS64854.1; -; Genomic_DNA.
DR   RefSeq; WP_005368280.1; NZ_CH902600.1.
DR   AlphaFoldDB; Q1ZSX3; -.
DR   GeneID; 61227503; -.
DR   eggNOG; COG1785; Bacteria.
DR   HOGENOM; CLU_008539_6_2_6; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000001603; 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; 1.10.60.40; -; 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..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..473
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004199130"
FT   ACT_SITE        82
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         34
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
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         135
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         274
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         314
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         433
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   473 AA;  51199 MW;  F2F6BE72D76E27D1 CRC64;
     MSILKPTLIA SSLLLSLGAH AADAPKYVFF MIGDGMGTAQ RQISEYYLQQ QNGDETQRLA
     INAMPVAGII TTHSANTLVT DSAAAGTALA TGVKTDNGVI AMDPEGHKLR STLDAAKDKG
     MATGIVTTTR LTHATPATFV AKNISRDNEN EIANDYLASN VDFFAGGGYR HFINGEGSKR
     KDGKNLVDGF KQKGYHTFIG ADSSADFLAF HPTNSQKVFA SFASSHLPYE IDRKKDLNTP
     SLAQMTSKAI ETLKYDPDGF FMLVEGGRID HAAHANDVST VIQDTIAFDQ AVKAAVDFYE
     HHKDETLIIV AGDHETGGMG LGLGENYFVQ LDKLKGVDES IEDKLQGVYK GDRKAFMKHI
     DEHFGLKLLT KEEQQTLNHA MDIDDELRAK NITDFDGYST HNDATYGGYD PVAIAVAHIT
     SQRAGVYWTS YAHTATQLPL SAVGVGAEKF GNFEDNTQVA KTLATLMNVK IGS
//
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