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Alkaline phosphatase PhoK (EC 3.1.3.1) (SPAP protein)

 ALPH_SPHSX              Reviewed;         559 AA.
A1YYW7;
23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 1.
30-AUG-2017, entry version 38.
RecName: Full=Alkaline phosphatase PhoK;
EC=3.1.3.1;
AltName: Full=SPAP protein;
Flags: Precursor;
Name=phoK {ECO:0000312|EMBL:ABL96598.1};
Sphingomonas sp.
Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
Sphingomonadaceae; Sphingomonas.
NCBI_TaxID=28214;
[1] {ECO:0000305, ECO:0000312|EMBL:ABL96598.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND INDUCTION.
STRAIN=BSAR-1 {ECO:0000269|PubMed:18641147};
PubMed=18641147; DOI=10.1128/AEM.00107-08;
Nilgiriwala K.S., Alahari A., Rao A.S., Apte S.K.;
"Cloning and overexpression of alkaline phosphatase PhoK from
Sphingomonas sp. strain BSAR-1 for bioprecipitation of uranium from
alkaline solutions.";
Appl. Environ. Microbiol. 74:5516-5523(2008).
[2] {ECO:0000305}
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=BSAR-1 {ECO:0000269|Ref.2};
Nilgiriwala K.S., Apte S.K.;
"PhoK alkaline phosphatase.";
Submitted (SEP-2009) to UniProtKB.
[3] {ECO:0000305}
CRYSTALLIZATION.
STRAIN=BSAR-1;
PubMed=19724132; DOI=10.1107/S1744309109031133;
Nilgiriwala K.S., Bihani S.C., Das A., Prashar V., Kumar M.,
Ferrer J.L., Apte S.K., Hosur M.V.;
"Crystallization and preliminary X-ray crystallographic analysis of
PhoK, an extracellular alkaline phosphatase from Sphingomonas sp.
BSAR-1.";
Acta Crystallogr. F 65:917-919(2009).
[4]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ZINC AND
SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE
SITE, AND DISULFIDE BONDS.
STRAIN=BSAR-1;
PubMed=21829507; DOI=10.1371/journal.pone.0022767;
Bihani S.C., Das A., Nilgiriwala K.S., Prashar V., Pirocchi M.,
Apte S.K., Ferrer J.L., Hosur M.V.;
"X-ray structure reveals a new class and provides insight into
evolution of alkaline phosphatases.";
PLoS ONE 6:E22767-E22767(2011).
-!- FUNCTION: Alkaline phosphatase with broad substrate specificity.
Precipitates uranium from alkaline solutions.
{ECO:0000269|PubMed:18641147, ECO:0000269|PubMed:21829507}.
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate. {ECO:0000269|PubMed:18641147,
ECO:0000269|PubMed:21829507}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:21829507};
Note=Binds 2 Zn(2+) ions. {ECO:0000269|PubMed:21829507};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 9.0. {ECO:0000269|PubMed:18641147};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21829507}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18641147}.
-!- INDUCTION: Constitutively expressed.
{ECO:0000269|PubMed:18641147}.
-----------------------------------------------------------------------
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EMBL; EF143994; ABL96598.1; -; Genomic_DNA.
PDB; 3Q3Q; X-ray; 1.95 A; A=1-559.
PDBsum; 3Q3Q; -.
SMR; A1YYW7; -.
BRENDA; 3.1.3.1; 10569.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0004035; F:alkaline phosphatase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
CDD; cd16016; AP-SPAP; 1.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core.
InterPro; IPR026263; Alkaline_phosphatase_prok.
InterPro; IPR002591; Phosphodiest/P_Trfase.
Pfam; PF01663; Phosphodiest; 1.
PIRSF; PIRSF031924; Pi-irrepressible_AP; 1.
SUPFAM; SSF53649; SSF53649; 2.
1: Evidence at protein level;
3D-structure; Disulfide bond; Hydrolase; Metal-binding;
Phosphoprotein; Secreted; Signal; Zinc.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 559 Alkaline phosphatase PhoK.
/FTId=PRO_0000392472.
REGION 171 173 Substrate binding.
ACT_SITE 89 89 Phosphothreonine intermediate.
{ECO:0000305|PubMed:21829507}.
METAL 49 49 Zinc 1. {ECO:0000269|PubMed:21829507}.
METAL 89 89 Zinc 1. {ECO:0000269|PubMed:21829507}.
METAL 300 300 Zinc 2. {ECO:0000269|PubMed:21829507}.
METAL 304 304 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:21829507}.
METAL 345 345 Zinc 1. {ECO:0000269|PubMed:21829507}.
METAL 346 346 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:21829507}.
METAL 491 491 Zinc 2; via tele nitrogen.
{ECO:0000269|PubMed:21829507}.
BINDING 110 110 Substrate. {ECO:0000269|PubMed:21829507}.
DISULFID 90 126 {ECO:0000269|PubMed:21829507}.
DISULFID 231 314 {ECO:0000269|PubMed:21829507}.
DISULFID 545 556 {ECO:0000269|PubMed:21829507}.
STRAND 41 48 {ECO:0000244|PDB:3Q3Q}.
HELIX 53 59 {ECO:0000244|PDB:3Q3Q}.
HELIX 60 62 {ECO:0000244|PDB:3Q3Q}.
HELIX 66 73 {ECO:0000244|PDB:3Q3Q}.
STRAND 74 81 {ECO:0000244|PDB:3Q3Q}.
HELIX 89 96 {ECO:0000244|PDB:3Q3Q}.
HELIX 102 105 {ECO:0000244|PDB:3Q3Q}.
STRAND 109 113 {ECO:0000244|PDB:3Q3Q}.
STRAND 118 120 {ECO:0000244|PDB:3Q3Q}.
STRAND 123 125 {ECO:0000244|PDB:3Q3Q}.
HELIX 152 159 {ECO:0000244|PDB:3Q3Q}.
STRAND 165 171 {ECO:0000244|PDB:3Q3Q}.
HELIX 172 179 {ECO:0000244|PDB:3Q3Q}.
STRAND 184 189 {ECO:0000244|PDB:3Q3Q}.
HELIX 205 218 {ECO:0000244|PDB:3Q3Q}.
HELIX 229 234 {ECO:0000244|PDB:3Q3Q}.
STRAND 238 240 {ECO:0000244|PDB:3Q3Q}.
STRAND 243 246 {ECO:0000244|PDB:3Q3Q}.
HELIX 257 261 {ECO:0000244|PDB:3Q3Q}.
HELIX 264 280 {ECO:0000244|PDB:3Q3Q}.
TURN 281 284 {ECO:0000244|PDB:3Q3Q}.
STRAND 285 288 {ECO:0000244|PDB:3Q3Q}.
STRAND 290 296 {ECO:0000244|PDB:3Q3Q}.
HELIX 298 306 {ECO:0000244|PDB:3Q3Q}.
STRAND 308 310 {ECO:0000244|PDB:3Q3Q}.
HELIX 311 333 {ECO:0000244|PDB:3Q3Q}.
STRAND 338 343 {ECO:0000244|PDB:3Q3Q}.
HELIX 352 355 {ECO:0000244|PDB:3Q3Q}.
TURN 356 359 {ECO:0000244|PDB:3Q3Q}.
HELIX 368 370 {ECO:0000244|PDB:3Q3Q}.
HELIX 372 383 {ECO:0000244|PDB:3Q3Q}.
STRAND 391 402 {ECO:0000244|PDB:3Q3Q}.
HELIX 408 424 {ECO:0000244|PDB:3Q3Q}.
STRAND 428 433 {ECO:0000244|PDB:3Q3Q}.
HELIX 434 438 {ECO:0000244|PDB:3Q3Q}.
HELIX 447 449 {ECO:0000244|PDB:3Q3Q}.
HELIX 452 458 {ECO:0000244|PDB:3Q3Q}.
TURN 462 464 {ECO:0000244|PDB:3Q3Q}.
STRAND 467 472 {ECO:0000244|PDB:3Q3Q}.
STRAND 476 479 {ECO:0000244|PDB:3Q3Q}.
HELIX 496 499 {ECO:0000244|PDB:3Q3Q}.
STRAND 500 507 {ECO:0000244|PDB:3Q3Q}.
HELIX 521 523 {ECO:0000244|PDB:3Q3Q}.
HELIX 524 531 {ECO:0000244|PDB:3Q3Q}.
HELIX 538 540 {ECO:0000244|PDB:3Q3Q}.
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


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