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Database: UniProt
Entry: A0A1S8CMQ0_9GAMM
LinkDB: A0A1S8CMQ0_9GAMM
Original site: A0A1S8CMQ0_9GAMM 
ID   A0A1S8CMQ0_9GAMM        Unreviewed;       484 AA.
AC   A0A1S8CMQ0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:OMQ23779.1};
GN   ORFNames=BMI79_09755 {ECO:0000313|EMBL:OMQ23779.1};
OS   Serratia oryzae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=2034155 {ECO:0000313|EMBL:OMQ23779.1, ECO:0000313|Proteomes:UP000216021};
RN   [1] {ECO:0000313|EMBL:OMQ23779.1, ECO:0000313|Proteomes:UP000216021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J11-6 {ECO:0000313|EMBL:OMQ23779.1,
RC   ECO:0000313|Proteomes:UP000216021};
RA   Zhang X.-X., Zhang J.;
RT   "Rahnella oryzae sp. nov., isolated from rice root.";
RL   Submitted (NOV-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}.
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:OMQ23779.1}.
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DR   EMBL; MOXD01000004; OMQ23779.1; -; Genomic_DNA.
DR   RefSeq; WP_076941986.1; NZ_MOXD01000004.1.
DR   AlphaFoldDB; A0A1S8CMQ0; -.
DR   STRING; 2034155.BMI79_09755; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000216021; 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; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR001952; Alkaline_phosphatase.
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; 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        98
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         54
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         172
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         310
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         361
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         447
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   484 AA;  51314 MW;  32D35C0783AB1496 CRC64;
     MKRNVLCRMM LGAIFAVTGC NDSDSVSSTQ SETPTPAPVP LAVPTKNVLF FLGDGMGIAT
     LTAARIYSVG EEGELTIDTL PETAFVHTYS NDAQVTDSAP SMSAYMTGLK TNNEVISMSP
     DTKATNPQGK PYQVNFDSTC PPGNGQAVET LLEQMKAANY GTGIVTTTRV THATPAATYA
     HVCHRDAENT IAAALVPGGQ GFNTKLGDGI DVILGGGASY FTPATAGGTR GDQRNLIAEL
     QAANYRYAAN KQQFEQLPVD GSKLVALFTP NHMSYDLDRD PAQEPSLAEM TEKAIDALAA
     KQKGFFLMVE GGRIDHALHA TNARRALQDT VAFDEAIKMA LDKMQQIDPG LQNTLIVVTA
     DHDHTLQMNG YAQRTGKTQE GNPGVLGVVK NYVNGANSTD VDGNPYTIIG FGNGPAHQAT
     RGPIDENALE SADFLQESVI PLKSETHGGG DVFLAAQGLG AEQFSGTLNN DRVFSLIKQA
     IDLP
//
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