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Database: UniProt/TrEMBL
Entry: C6BHZ9_RALP1
LinkDB: C6BHZ9_RALP1
Original site: C6BHZ9_RALP1 
ID   C6BHZ9_RALP1            Unreviewed;       485 AA.
AC   C6BHZ9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:ACS64595.1};
DE            EC=3.1.3.1 {ECO:0000313|EMBL:ACS64595.1};
GN   OrderedLocusNames=Rpic12D_3331 {ECO:0000313|EMBL:ACS64595.1};
OS   Ralstonia pickettii (strain 12D).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=428406 {ECO:0000313|EMBL:ACS64595.1};
RN   [1] {ECO:0000313|EMBL:ACS64595.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12D {ECO:0000313|EMBL:ACS64595.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Marsh T., Richardson P.;
RT   "Complete sequence chromosome 1 of Ralstonia pickettii 12D.";
RL   Submitted (JUN-2009) 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; CP001644; ACS64595.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6BHZ9; -.
DR   STRING; 428406.Rpic12D_3331; -.
DR   KEGG; rpf:Rpic12D_3331; -.
DR   HOGENOM; CLU_008539_4_1_4; -.
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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ACS64595.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..485
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002962490"
FT   ACT_SITE        98
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         54
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         172
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         310
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         361
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         449
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   485 AA;  50294 MW;  4628561FB13FA071 CRC64;
     MHNHTFTKYA AAAAAALAMA ACGSDGTSTA GGATPDTTPP SATPAKNVVF FLGDGMGLTT
     MTAARIYKVG EDGELTMDTL PETGFVRTFS NNAQVTDSAP SMSAYMTGVK MNNEVISMSP
     DTMAYDAGGK DYLSGADSTC PSGNGKPVTT LLELMKAAGY GTGVVTTTRI THATPAATYS
     HICHRDGENT IAAQLTPAGK GFNAALGDGV DVVFGGGRKH FQPTTAGGAR TDGRDLIAEL
     KAGGYRYASN KAEFDTLQAT DGKVVGLFTS SHMSYDLDRD PSKEPSLGEM TNKAIDVLAA
     KKKGFFLMVE GGRIDHALHE TTARKALQDT VAFDSAIRGA IDKLNTIDPG LKNTLIVVTA
     DHDHTLVLNG YAKRTGPTSD SNPGVLGLLK NYVTGANATD TGGNPFTIIG FGTGENRPAT
     RGALTDAAVY DKNYHQEAVI PVAPGGETHG GTDVFIGARG LGAERFTGTL DNTEVFGLIK
     QAVGL
//
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