ALPH_SPHSX
ID ALPH_SPHSX Reviewed; 559 AA.
AC A1YYW7;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Alkaline phosphatase PhoK;
DE EC=3.1.3.1;
DE AltName: Full=SPAP protein;
DE Flags: Precursor;
GN Name=phoK {ECO:0000312|EMBL:ABL96598.1};
OS Sphingomonas sp.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=28214;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABL96598.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=BSAR-1 {ECO:0000269|PubMed:18641147};
RX PubMed=18641147; DOI=10.1128/aem.00107-08;
RA Nilgiriwala K.S., Alahari A., Rao A.S., Apte S.K.;
RT "Cloning and overexpression of alkaline phosphatase PhoK from Sphingomonas
RT sp. strain BSAR-1 for bioprecipitation of uranium from alkaline
RT solutions.";
RL Appl. Environ. Microbiol. 74:5516-5523(2008).
RN [2] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=BSAR-1 {ECO:0000269|Ref.2};
RA Nilgiriwala K.S., Apte S.K.;
RT "PhoK alkaline phosphatase.";
RL Submitted (SEP-2009) to UniProtKB.
RN [3] {ECO:0000305}
RP CRYSTALLIZATION.
RC STRAIN=BSAR-1;
RX PubMed=19724132; DOI=10.1107/s1744309109031133;
RA Nilgiriwala K.S., Bihani S.C., Das A., Prashar V., Kumar M., Ferrer J.L.,
RA Apte S.K., Hosur M.V.;
RT "Crystallization and preliminary X-ray crystallographic analysis of PhoK,
RT an extracellular alkaline phosphatase from Sphingomonas sp. BSAR-1.";
RL Acta Crystallogr. F 65:917-919(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ZINC AND SUBSTRATE,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, AND DISULFIDE
RP BONDS.
RC STRAIN=BSAR-1;
RX PubMed=21829507; DOI=10.1371/journal.pone.0022767;
RA Bihani S.C., Das A., Nilgiriwala K.S., Prashar V., Pirocchi M., Apte S.K.,
RA Ferrer J.L., Hosur M.V.;
RT "X-ray structure reveals a new class and provides insight into evolution of
RT alkaline phosphatases.";
RL PLoS ONE 6:E22767-E22767(2011).
CC -!- FUNCTION: Alkaline phosphatase with broad substrate specificity.
CC Precipitates uranium from alkaline solutions.
CC {ECO:0000269|PubMed:18641147, ECO:0000269|PubMed:21829507}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC Evidence={ECO:0000269|PubMed:18641147, ECO:0000269|PubMed:21829507};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:21829507};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000269|PubMed:21829507};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:18641147};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21829507}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18641147}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:18641147}.
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DR EMBL; EF143994; ABL96598.1; -; Genomic_DNA.
DR PDB; 3Q3Q; X-ray; 1.95 A; A=1-559.
DR PDB; 5XWI; X-ray; 1.87 A; A=1-559.
DR PDB; 5XWK; X-ray; 1.90 A; A=1-559.
DR PDBsum; 3Q3Q; -.
DR PDBsum; 5XWI; -.
DR PDBsum; 5XWK; -.
DR AlphaFoldDB; A1YYW7; -.
DR SMR; A1YYW7; -.
DR BRENDA; 3.1.3.1; 10569.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR CDD; cd16016; AP-SPAP; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR026263; Alkaline_phosphatase_prok.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR Pfam; PF01663; Phosphodiest; 1.
DR PIRSF; PIRSF031924; Pi-irrepressible_AP; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hydrolase; Metal-binding; Phosphoprotein;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..559
FT /note="Alkaline phosphatase PhoK"
FT /id="PRO_0000392472"
FT ACT_SITE 89
FT /note="Phosphothreonine intermediate"
FT /evidence="ECO:0000305|PubMed:21829507"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21829507"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21829507"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21829507"
FT BINDING 171..173
FT /ligand="substrate"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21829507"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21829507"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21829507"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21829507"
FT BINDING 491
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21829507"
FT DISULFID 90..126
FT /evidence="ECO:0000269|PubMed:21829507"
FT DISULFID 231..314
FT /evidence="ECO:0000269|PubMed:21829507"
FT DISULFID 545..556
FT /evidence="ECO:0000269|PubMed:21829507"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:5XWK"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 264..280
FT /evidence="ECO:0007829|PDB:5XWI"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 311..333
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:5XWI"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 372..378
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 391..402
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 419..424
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:5XWI"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 496..499
FT /evidence="ECO:0007829|PDB:5XWI"
FT STRAND 500..506
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 524..531
FT /evidence="ECO:0007829|PDB:5XWI"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:5XWI"
SQ SEQUENCE 559 AA; 59982 MW; 0A7A0F7838E1A186 CRC64;
MLKHVAAALL LATAMPVVAQ SPAPAAAPAP AARSIAATPP KLIVAISVDQ FSADLFSEYR
QYYTGGLKRL TSEGAVFPRG YQSHAATETC PGHSTILTGS RPSRTGIIAN NWFDLDAKRE
DKNLYCAEDE SQPGSSSDKY EASPLHLKVP TLGGRMKAAN PATRVVSVAG KDRAAIMMGG
ATADQVWWLG GPQGYVSYKG VAPTPLVTQV NQAFAQRLAQ PNPGFELPAQ CVSKDFPVQA
GNRTVGTGRF ARDAGDYKGF RISPEQDAMT LAFAAAAIEN MQLGKQAQTD IISIGLSATD
YVGHTFGTEG TESCIQVDRL DTELGAFFDK LDKDGIDYVV VLTADHGGHD LPERHRMNAM
PMEQRVDMAL TPKALNATIA EKAGLPGKKV IWSDGPSGDI YYDKGLTAAQ RARVETEALK
YLRAHPQVQT VFTKAEIAAT PSPSGPPESW SLIQEARASF YPSRSGDLLL LLKPRVMSIP
EQAVMGSVAT HGSPWDTDRR VPILFWRKGM QHFEQPLGVE TVDILPSLAA LIKLPVPKDQ
IDGRCLDLVA GKDDSCAGQ
