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Database: UniProt
Entry: A0A1H2Z925_9FLAO
LinkDB: A0A1H2Z925_9FLAO
Original site: A0A1H2Z925_9FLAO 
ID   A0A1H2Z925_9FLAO        Unreviewed;       602 AA.
AC   A0A1H2Z925;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:SDX13354.1};
GN   ORFNames=SAMN04487892_3338 {ECO:0000313|EMBL:SDX13354.1};
OS   Allomuricauda zhangzhouensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=1073328 {ECO:0000313|EMBL:SDX13354.1, ECO:0000313|Proteomes:UP000199592};
RN   [1] {ECO:0000313|Proteomes:UP000199592}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25030 {ECO:0000313|Proteomes:UP000199592};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNMY01000008; SDX13354.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2Z925; -.
DR   STRING; 1073328.SAMN05216294_3343; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000199592; Unassembled WGS sequence.
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   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   InterPro; IPR001952; Alkaline_phosphatase.
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.
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        336
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         389
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         496
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         500
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         538
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         539
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   602 AA;  66340 MW;  D870B8787650D1E5 CRC64;
     MSLLTQTLRK SSFLSWRHVL SLIVFLVILQ GVYAQSTYKI HSHNDYAQEL PFWFAYSNGA
     SSIEADLFLK DNVLYVTHAE DEINPKHTFK KLYLDRLQGL EADGELGEIQ LLIDLKSEAY
     TTLAKLVKLL GDYPTLIESG KVKFVISGNR PEPGHYKNYP DFIWFDHQNL EELNRNDLTK
     VALVSVSFKN YSVWNGYGRM TAPDLEAVTN AIEKAKSAGK PFRFWATPDT KTAWARLAKM
     GVDYINTDHP ALAKQYLDKL DANTFHMEQK NEVYAPKFLY DEKSTPKNII LMIGDGNGLA
     QISSAMIANR GNLTVTGLKN IGLVKIASAD DLITDSAAGA SAMATGTKTN NRAIGVDPKA
     KAMTNLVDVL GGRGYNTAIV TTDAIFGATP SSFYAHRIER DDTPGLIEDL NKSQLDFFIA
     GGKNEKGTID KVFTEKTLEI FEDFKKPTAI YLGDNKAPTM ENDRGGVFPS AIRKSLEVLE
     SSEAPFLLMV EGAQIDNGGH SNSTKDIVQE MLDFDLAIAE ALKFADANKN TLVVITADHE
     TSGFGIVGGS LELGTVQGDF LTVDHTGIMV PLFAYGPQAD NFSGVYENTE IFEKILEALD
     KK
//
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