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Database: UniProt/TrEMBL
Entry: B5YCM2_DICT6
LinkDB: B5YCM2_DICT6
Original site: B5YCM2_DICT6 
ID   B5YCM2_DICT6            Unreviewed;       537 AA.
AC   B5YCM2;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Alkaline phosphatase III {ECO:0000313|EMBL:ACI18383.1};
DE            EC=3.1.3.1 {ECO:0000313|EMBL:ACI18383.1};
GN   OrderedLocusNames=DICTH_0398 {ECO:0000313|EMBL:ACI18383.1};
OS   Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12).
OC   Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae;
OC   Dictyoglomus.
OX   NCBI_TaxID=309799 {ECO:0000313|EMBL:ACI18383.1, ECO:0000313|Proteomes:UP000001733};
RN   [1] {ECO:0000313|EMBL:ACI18383.1, ECO:0000313|Proteomes:UP000001733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35947 / DSM 3960 / H-6-12
RC   {ECO:0000313|Proteomes:UP000001733};
RX   PubMed=24558247;
RA   Coil D.A., Badger J.H., Forberger H.C., Riggs F., Madupu R., Fedorova N.,
RA   Ward N., Robb F.T., Eisen J.A.;
RT   "Complete Genome Sequence of the Extreme Thermophile Dictyoglomus
RT   thermophilum H-6-12.";
RL   Genome Announc. 2:e00109-e00114(2014).
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; CP001146; ACI18383.1; -; Genomic_DNA.
DR   RefSeq; WP_012547015.1; NC_011297.1.
DR   AlphaFoldDB; B5YCM2; -.
DR   STRING; 309799.DICTH_0398; -.
DR   PaxDb; 309799-DICTH_0398; -.
DR   KEGG; dth:DICTH_0398; -.
DR   eggNOG; COG1785; Bacteria.
DR   HOGENOM; CLU_008539_5_0_0; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000001733; Chromosome.
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; 1.10.60.40; -; 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; 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:ACI18383.1};
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        101
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         52
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         52
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         281
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         290
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         481
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   537 AA;  60083 MW;  8D12869AF31F3270 CRC64;
     MRFDRVFSKV LLIFILVLGF VFFSSSFGVA LQSSSSLYKG KPVKYIFWFI GDGMGLNHVY
     LTEAFLGRKS NSPSIEKLSF TQFPNVGLMT TYAADSYITD SASAITAMAA GKKTNDGVIN
     MDPTLKFKYK SVAEEARDLG YKVGVLTSVS IDHATPAGMY AHQPSRNNYY AIALELFESN
     FDYFGGGGFL QPQGKDGKQK DVYEIAKEKG YKIVDKIEDF LKLRKGDNKI VAINPILDSS
     KALPYAINRL RGANLGLSLA DFTKKAIELL DNPKGFFIMV EGGKIDWAAH ANDAGSVIYD
     VLDFNEAIKV ALEFYKKRPF ETVIIVTADH ETGGLSIGYA GTRYEVYLDV LSRQKISYDE
     FTKVVNEYKS KVKREEAKLS DLLPQIKEYY GLEILSPEVR KELENRAKAG DKEAKIRLQL
     ALNESEIEEL EKAFKLSMMD PKERPNDAKS YLLYGGYDPL TITVTRILNQ KAGISWTSYS
     HTGMPVPVYA IGAGSYIFNG YYDNTDLYKK LMSLIGKDPY KDNVLSSAEV RELVFSK
//
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