ID Q1LFX4_CUPMC Unreviewed; 467 AA. AC Q1LFX4; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 27-MAR-2024, entry version 93. DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ABF10952.1}; DE EC=3.1.3.1 {ECO:0000313|EMBL:ABF10952.1}; GN Name=phoA2 {ECO:0000313|EMBL:ABF10952.1}; GN OrderedLocusNames=Rmet_4085 {ECO:0000313|EMBL:ABF10952.1}; OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / OS CH34) (Ralstonia metallidurans). OG Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429}. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF10952.1, ECO:0000313|Proteomes:UP000002429}; RN [1] {ECO:0000313|Proteomes:UP000002429} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34 RC {ECO:0000313|Proteomes:UP000002429}; RC PLASMID=Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429}; RX PubMed=20463976; DOI=10.1371/journal.pone.0010433; RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A., RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C., RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.; RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a RT master survivalist in harsh and anthropogenic environments."; RL PLoS ONE 5:E10433-E10433(2010). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000353; ABF10952.1; -; Genomic_DNA. DR AlphaFoldDB; Q1LFX4; -. DR KEGG; rme:Rmet_4085; -. DR eggNOG; COG1785; Bacteria. DR HOGENOM; CLU_008539_4_1_4; -. DR Proteomes; UP000002429; Plasmid megaplasmid CH34. 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; 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 Hydrolase {ECO:0000313|EMBL:ABF10952.1}; KW Magnesium {ECO:0000256|PIRSR:PIRSR601952-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Plasmid {ECO:0000313|EMBL:ABF10952.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002429}; KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}. FT SIGNAL 1..26 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 27..467 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004193455" FT ACT_SITE 83 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1" FT BINDING 39 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 39 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 157 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 159 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 302 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 307 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 311 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 348 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 349 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 431 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" SQ SEQUENCE 467 AA; 48616 MW; C40F6C051F3798B9 CRC64; MKITTRIGML AAAAASACLT MPAAQAAGEA KNVIFFLGDG MGPATVTASR IYKYGESGKL TMESLKRTAR IKTFSNDAQT TDSAPSMAAY MTGVKMNNEV ISMSPDTKAT APGTDVNGNK TINNCLPTNG TSVPTLLELA KARGKATGAI TTTELTHATP AATYSHICHR DAQYDIAAQA VPGGAGFNTA LGDGVDVLMG GGRNHWTPFD ATANKKGRAD GRNLLTEFAA KGYAVAATRD QMMQASGNKL IGLFSTTSHL EYEIDRVAGK GEGATQPSLA DMTAKAIELL SKNGNGYFLM VEGGRIDHAL HGTNAKRALE DTIAFDDAIK RALSMVDLSN TIIVVTADHD HTMTINGYSH RGNPILATAT DYKTKKTALA ADGLPYTTLV FGNGGTPRKA TRDNPSLVDT TANDYLQEVG VNLGSPGAET HGGGDVMLFS TGPGSAPLKG TLDNTKVFGV VKSALGL //