ID Q0K9P2_CUPNH Unreviewed; 462 AA. AC Q0K9P2; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 93. DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:CAJ93279.1}; DE EC=3.1.3.1 {ECO:0000313|EMBL:CAJ93279.1}; GN OrderedLocusNames=H16_A2182 {ECO:0000313|EMBL:CAJ93279.1}; OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 OS / H16 / Stanier 337) (Ralstonia eutropha). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ93279.1, ECO:0000313|Proteomes:UP000008210}; RN [1] {ECO:0000313|EMBL:CAJ93279.1, ECO:0000313|Proteomes:UP000008210} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier RC 337 {ECO:0000313|Proteomes:UP000008210}; RX PubMed=16964242; DOI=10.1038/nbt1244; RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., RA Eitinger T., Ewering C., Potter M., Schwartz E., Strittmatter A., Voss I., RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.; RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia RT eutropha H16."; RL Nat. Biotechnol. 24:1257-1262(2006). 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; AM260479; CAJ93279.1; -; Genomic_DNA. DR RefSeq; WP_011615543.1; NZ_CP039287.1. DR AlphaFoldDB; Q0K9P2; -. DR STRING; 381666.H16_A2182; -. DR GeneID; 57644312; -. DR KEGG; reh:H16_A2182; -. DR PATRIC; fig|381666.6.peg.2590; -. DR eggNOG; COG1785; Bacteria. DR HOGENOM; CLU_008539_4_1_4; -. DR OrthoDB; 9794455at2; -. DR Proteomes; UP000008210; Chromosome 1. 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:CAJ93279.1}; 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:UP000008210}; KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}. FT SIGNAL 1..25 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 26..462 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004174704" FT ACT_SITE 82 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1" FT BINDING 38 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 38 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 297 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 302 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 306 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 343 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 344 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 426 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" SQ SEQUENCE 462 AA; 48120 MW; 6B12FE210BD357E5 CRC64; MKLIIRTGLS ALAAACACIA LPAQAAGEAK NVIFFLGDGM GPTTVTASRI YKYGETGKLN MESLKRTARV KTYSNDAQTT DSAPSMAAYM TGVKMNNEVI SMSADTKASD GTGKAYVTSA GDSTCPSGNG APVVTVLELA KAAGKSVGAV TTTRVTHATP AATFSHVCHR DGENNIAAQA TPGNAGYNTA LKDGLDVLLG GGRRQFLPDS VTGGKRTDGV DLTTQFPGYT YVTTGTAFKA VDPASTSKLL GLFNMDHLNY ELDRVKNNVD EPSLADMTEK AIRILQKNGN GYFLMVEGGR IDHALHGTNA KRALEDTIAF DDAIKRALSM VDLSNTMIVV TADHDHTMTI NGYSHRGNPI LGTATDIKTR QPATAADGLP YTTLVFGNGG GPRKTPRDNP ALVDTTADGY LQEVGVNLGS PGSETHGGGD VMLFSTGPGN AALKGTIDNT KVFSVVKSAL GL //