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Database: UniProt
Entry: R7ZWT3_9BACT
LinkDB: R7ZWT3_9BACT
Original site: R7ZWT3_9BACT 
ID   R7ZWT3_9BACT            Unreviewed;       469 AA.
AC   R7ZWT3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:EON78474.1};
DE            EC=3.1.3.1 {ECO:0000313|EMBL:EON78474.1};
GN   ORFNames=ADIS_1085 {ECO:0000313|EMBL:EON78474.1};
OS   Lunatimonas lonarensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae.
OX   NCBI_TaxID=1232681 {ECO:0000313|EMBL:EON78474.1, ECO:0000313|Proteomes:UP000013909};
RN   [1] {ECO:0000313|EMBL:EON78474.1, ECO:0000313|Proteomes:UP000013909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK24 {ECO:0000313|EMBL:EON78474.1,
RC   ECO:0000313|Proteomes:UP000013909};
RA   Singh A.;
RT   "A novel strain isolated from Lonar lake, Maharashtra, India.";
RL   Submitted (FEB-2013) 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   -!- 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:EON78474.1}.
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DR   EMBL; AQHR01000035; EON78474.1; -; Genomic_DNA.
DR   RefSeq; WP_010853232.1; NZ_AQHR01000035.1.
DR   AlphaFoldDB; R7ZWT3; -.
DR   STRING; 1232681.ADIS_1085; -.
DR   PATRIC; fig|1288963.3.peg.1084; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000013909; Unassembled WGS sequence.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EON78474.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013909};
KW   Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   ACT_SITE        97
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         148
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         276
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         281
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         285
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         324
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         426
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   469 AA;  50731 MW;  58AB7F2606E259C8 CRC64;
     MKRRDFFRKG VFASLGATAL GTGSAFARHT EDAFRKTAKN VIFLVSDGMS TGTLNMADVL
     LKQKEGRRSR WVGSYQGNIM KRSLMETASS NSVVTDSAAA GSSWGGGMRV PNGSLNIGPN
     GEEPIPILQK FKAAGKSVGC VTSVQIAHAT PAAFCVNEKS RNAMPVIAET YLKLRFDVMF
     GGGDELFNGS KRADKKDLYK DYRAAGFTVA RNREELLKVQ GKGPVLGVFS EGGLPYAIDR
     ENDPEIKKVT PSMAEMVKKA IEILSQNPNG FAMQIEGGKV DWAAHGNDAP ALLYDQIDFD
     EAVGIALDFA ARDGETLVIM TTDHGNANPG LFDGGVKGKF GTLFTATRSN EWILKQLNGD
     NTPDQVIDLI NAYQGITIKP EEAIALLKNY QVVNDEGLYD TGKIPLKLLS EIQMPYTGIG
     WAGTGHSSDH VELGMFGPGS ENLPAFIENY KLHNFMLNAA HVPAMAYAW
//
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