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Database: UniProt
Entry: W0EQ05_9BACT
LinkDB: W0EQ05_9BACT
Original site: W0EQ05_9BACT 
ID   W0EQ05_9BACT            Unreviewed;       466 AA.
AC   W0EQ05;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AHF12895.1};
GN   ORFNames=BARVI_09245 {ECO:0000313|EMBL:AHF12895.1};
OS   Barnesiella viscericola DSM 18177.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae;
OC   Barnesiella.
OX   NCBI_TaxID=880074 {ECO:0000313|EMBL:AHF12895.1, ECO:0000313|Proteomes:UP000018901};
RN   [1] {ECO:0000313|EMBL:AHF12895.1, ECO:0000313|Proteomes:UP000018901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18177 {ECO:0000313|Proteomes:UP000018901};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-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}.
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DR   EMBL; CP007034; AHF12895.1; -; Genomic_DNA.
DR   RefSeq; WP_025278915.1; NZ_CP007034.1.
DR   AlphaFoldDB; W0EQ05; -.
DR   STRING; 880074.BARVI_09245; -.
DR   KEGG; bvs:BARVI_09245; -.
DR   PATRIC; fig|880074.11.peg.1915; -.
DR   eggNOG; COG1785; Bacteria.
DR   HOGENOM; CLU_008539_5_0_10; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000018901; Chromosome.
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; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR   Pfam; PF00245; Alk_phosphatase; 2.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 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        85
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         36
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         260
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         429
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   466 AA;  52120 MW;  B365125D85FC267B CRC64;
     MKRNAQKWVL TLVILLISTT LLSAKTPKYI FYCIGDGMSF AHVMATQLYY EHGNNPNGKE
     SLAILDFPVR SAIRTYANNS LITCSAAAGT ALATGHRTNI DFVGIDPEGK PLTSIAKQLR
     DKGYAIGIVT SGQIDDATPA AFYASQMRKD AYLIGRDGAD SQFDYLAGSA LKQPYGKDQK
     QPSLYDYYRQ KGYTICRGID GFDAQADKVL LLDADTTLRS WLPYVIERDP EAMGLEFMVK
     TGIDKLSREK GKKGFFMMIE GASIDHASHP CDIATAVKEG AEFDRCVKLT YEFYRQHPDE
     TLIIVTADHE TGGLTLGETS MKPFHWEYVN YQKMSKESLS NLFQRLRKTG EIDTWEKARK
     ILAENTGLWD KIPVNAGEEA KLMQCYYETI VKKNSEQEIT LYSRNEPLVA EAIALLARKI
     GVGWTTFSHT GSFVPLYAIG CQAQQFGTLN DNTEIPNTIR KIMKIK
//
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