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Database: UniProt/TrEMBL
Entry: A0A0U4W148_9BACT
LinkDB: A0A0U4W148_9BACT
Original site: A0A0U4W148_9BACT 
ID   A0A0U4W148_9BACT        Unreviewed;       517 AA.
AC   A0A0U4W148;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:BAU22877.1};
GN   ORFNames=THC_0483 {ECO:0000313|EMBL:BAU22877.1};
OS   Caldimicrobium thiodismutans.
OC   Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC   Thermodesulfobacteriales; Thermodesulfobacteriaceae; Caldimicrobium.
OX   NCBI_TaxID=1653476 {ECO:0000313|EMBL:BAU22877.1, ECO:0000313|Proteomes:UP000068196};
RN   [1] {ECO:0000313|EMBL:BAU22877.1, ECO:0000313|Proteomes:UP000068196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF1 {ECO:0000313|EMBL:BAU22877.1,
RC   ECO:0000313|Proteomes:UP000068196};
RX   PubMed=26842785; DOI=10.1099/ijsem.0.000947;
RA   Kojima H., Umezawa K., Fukui M.;
RT   "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT   bacterium isolated from a hot spring, and emended description of the genus
RT   Caldimicrobium.";
RL   Int. J. Syst. Evol. Microbiol. 66:1828-1831(2016).
RN   [2] {ECO:0000313|Proteomes:UP000068196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF1 {ECO:0000313|Proteomes:UP000068196};
RA   Kojima H., Umezawa K., Fukui M.;
RT   "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT   bacterium isolated from a hot spring.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2016).
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; AP014945; BAU22877.1; -; Genomic_DNA.
DR   RefSeq; WP_068512809.1; NZ_AP014945.1.
DR   AlphaFoldDB; A0A0U4W148; -.
DR   STRING; 1653476.THC_0483; -.
DR   KEGG; cthi:THC_0483; -.
DR   PATRIC; fig|1653476.3.peg.498; -.
DR   OrthoDB; 9794455at2; -.
DR   Proteomes; UP000068196; 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; 1.10.1200.140; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000068196};
KW   Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   COILED          376..403
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        96
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         46
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         147
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         149
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         446
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   517 AA;  58829 MW;  FB12C3CDFCD5A634 CRC64;
     MLGRRDFLKL SLASFITLVA PSREIFARVN FSEGSATKGI IFLVGDGWPL GVMKVMTEFM
     TMKFKEESNL SILLRNLNTR VLLQNTSSLS SVVTDSAPAS VAWATGSKTV NRSLSSLPDG
     RKLTTIFELA RQKGIAYGFV TTTRVTHATP AAWYSHNPNR DDEDNIALDL LNSNVMVAMG
     GGDRHFNGTI RKDRRDLYGM FREKGFRVVR TREELVASLN DENPILGIFA SSHMSYFVDR
     VNDKRLRESE PSLPEMTAVA LQKLSKNKKG FILQIEAGRI DHACHSNDMY GAMMDCYELD
     KTLAVILEFM EKNPNVLLIV TSDHGNSGYG INGTGPEYND STEALLSYNN KASFEYMKRL
     MRGQDAKNIR DIFENYTGQK ISLEEAEEIY RKLNEKKTVV INDIWYEPDY TMGRILAKSV
     YKYENENLFK PAIERRGNVG FTSTNHTAED QIVIIYGEQI PQMRVKSHID NTELFQIICN
     YLRIYHINPK MKKEEAIAFI KSITKEEWKK HLELHIA
//
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