ID   D5B9Z3_ZUNPS            Unreviewed;       567 AA.
AC   D5B9Z3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ADF52291.1};
GN   OrderedLocusNames=ZPR_1966 {ECO:0000313|EMBL:ADF52291.1};
OS   Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS   profunda).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Zunongwangia.
OX   NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF52291.1, ECO:0000313|Proteomes:UP000001654};
RN   [1] {ECO:0000313|EMBL:ADF52291.1, ECO:0000313|Proteomes:UP000001654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC   {ECO:0000313|Proteomes:UP000001654};
RX   PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA   Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA   Zhou B.C., Yu J., Zhang Y.Z.;
RT   "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT   to the deep-sea environment and ecological role in sedimentary organic
RT   nitrogen degradation.";
RL   BMC Genomics 11:247-247(2010).
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; CP001650; ADF52291.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5B9Z3; -.
DR   STRING; 655815.ZPR_1966; -.
DR   KEGG; zpr:ZPR_1966; -.
DR   eggNOG; COG1785; Bacteria.
DR   HOGENOM; CLU_445393_0_0_10; -.
DR   Proteomes; UP000001654; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd16012; ALP; 1.
DR   CDD; cd08577; PI-PLCc_GDPD_SF_unchar3; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   InterPro; IPR039559; AIM6_PI-PLC-like_dom.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR018299; Alkaline_phosphatase_AS.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR   Pfam; PF00245; Alk_phosphatase; 2.
DR   Pfam; PF13653; GDPD_2; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        304
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         263
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         263
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="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         458
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         463
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         467
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         505
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         506
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   567 AA;  63419 MW;  FB752892C34C0832 CRC64;
     MAQSNYKFHS HNDYAQDFPF WKAYIHGASS IEADIFLKND ELYVTHSEDE IQADFTLENL
     YLKPLADLAK AGKLRNLQLL IDLKSESKTS LKKLVEVLNS YPELTQSDKI SFVISGNRPR
     PNEYKDYPGF IEFDHQDLSD LEKTDLTKVA LISQNFRDYS VWNGLGRITA PELKKVETAI
     KKAHDAGKPF RFWGAPDTKT AWSRFAEMGV DFINTDKPDE ASKYLETLQT RKFELKTPIS
     VYQPKFDYDK STSPKNIILM IGDGNGLSQI SSAVFANRGE LTLTQLKNIG LVKTSSFDDL
     VTDSAAGGTA MATGTKTNNR AIGTDKDGKD LSNLTEILAK KGFLNGIMTT DFVTGATPSS
     FFAHVVERDD SESILEDLNK SKIDFFMAAG ARDFEKIKDN FIQEDFSDFN DLENRTAVFL
     SENMLADASV RGDQFPKYVK KALQNLERQD KPYFLMIEAA KIDKNGHTNN ASGIIEEMLD
     FDKTIAEVLK VADKNKNTLV VITADHETSG FGIMQGDLEK GKIEGGFLTH DHTGAMIPLF
     SYGPGSELFN GVYENTAVFH RILKALE
//