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A1YYW7

- ALPH_SPHSX

UniProt

A1YYW7 - ALPH_SPHSX

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Protein

Alkaline phosphatase PhoK

Gene

phoK

Organism
Sphingomonas sp.
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Alkaline phosphatase with broad substrate specificity. Precipitates uranium from alkaline solutions.2 Publications

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.2 Publications

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn(2+) ions.1 Publication

pH dependencei

Optimum pH is 9.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi49 – 491Zinc 11 Publication
Active sitei89 – 891Phosphothreonine intermediate1 Publication
Metal bindingi89 – 891Zinc 11 Publication
Binding sitei110 – 1101Substrate1 Publication
Metal bindingi300 – 3001Zinc 21 Publication
Metal bindingi304 – 3041Zinc 2; via tele nitrogen1 Publication
Metal bindingi345 – 3451Zinc 11 Publication
Metal bindingi346 – 3461Zinc 1; via tele nitrogen1 Publication
Metal bindingi491 – 4911Zinc 2; via tele nitrogen1 Publication

GO - Molecular functioni

  1. alkaline phosphatase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB
  3. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alkaline phosphatase PhoK (EC:3.1.3.1)
Alternative name(s):
SPAP protein
Gene namesi
Name:phoKImported
OrganismiSphingomonas sp.
Taxonomic identifieri28214 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingomonas

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 559540Alkaline phosphatase PhoKPRO_0000392472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi90 ↔ 1261 Publication
Disulfide bondi231 ↔ 3141 Publication
Disulfide bondi545 ↔ 5561 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Expressioni

Inductioni

Constitutively expressed.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
559
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 488Combined sources
Helixi53 – 597Combined sources
Helixi60 – 623Combined sources
Helixi66 – 738Combined sources
Beta strandi74 – 818Combined sources
Helixi89 – 968Combined sources
Helixi102 – 1054Combined sources
Beta strandi109 – 1135Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi123 – 1253Combined sources
Helixi152 – 1598Combined sources
Beta strandi165 – 1717Combined sources
Helixi172 – 1798Combined sources
Beta strandi184 – 1896Combined sources
Helixi205 – 21814Combined sources
Helixi229 – 2346Combined sources
Beta strandi238 – 2403Combined sources
Beta strandi243 – 2464Combined sources
Helixi257 – 2615Combined sources
Helixi264 – 28017Combined sources
Turni281 – 2844Combined sources
Beta strandi285 – 2884Combined sources
Beta strandi290 – 2967Combined sources
Helixi298 – 3069Combined sources
Beta strandi308 – 3103Combined sources
Helixi311 – 33323Combined sources
Beta strandi338 – 3436Combined sources
Helixi352 – 3554Combined sources
Turni356 – 3594Combined sources
Helixi368 – 3703Combined sources
Helixi372 – 38312Combined sources
Beta strandi391 – 40212Combined sources
Helixi408 – 42417Combined sources
Beta strandi428 – 4336Combined sources
Helixi434 – 4385Combined sources
Helixi447 – 4493Combined sources
Helixi452 – 4587Combined sources
Turni462 – 4643Combined sources
Beta strandi467 – 4726Combined sources
Beta strandi476 – 4794Combined sources
Helixi496 – 4994Combined sources
Beta strandi500 – 5078Combined sources
Helixi521 – 5233Combined sources
Helixi524 – 5318Combined sources
Helixi538 – 5403Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q3QX-ray1.95A1-559[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni171 – 1733Substrate binding

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.720.10. 2 hits.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR026263. Alkaline_phosphatase_prok.
IPR002591. Phosphodiest/P_Trfase.
[Graphical view]
PfamiPF01663. Phosphodiest. 1 hit.
[Graphical view]
PIRSFiPIRSF031924. Pi-irrepressible_AP. 1 hit.
SUPFAMiSSF53649. SSF53649. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A1YYW7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKHVAAALL LATAMPVVAQ SPAPAAAPAP AARSIAATPP KLIVAISVDQ
60 70 80 90 100
FSADLFSEYR QYYTGGLKRL TSEGAVFPRG YQSHAATETC PGHSTILTGS
110 120 130 140 150
RPSRTGIIAN NWFDLDAKRE DKNLYCAEDE SQPGSSSDKY EASPLHLKVP
160 170 180 190 200
TLGGRMKAAN PATRVVSVAG KDRAAIMMGG ATADQVWWLG GPQGYVSYKG
210 220 230 240 250
VAPTPLVTQV NQAFAQRLAQ PNPGFELPAQ CVSKDFPVQA GNRTVGTGRF
260 270 280 290 300
ARDAGDYKGF RISPEQDAMT LAFAAAAIEN MQLGKQAQTD IISIGLSATD
310 320 330 340 350
YVGHTFGTEG TESCIQVDRL DTELGAFFDK LDKDGIDYVV VLTADHGGHD
360 370 380 390 400
LPERHRMNAM PMEQRVDMAL TPKALNATIA EKAGLPGKKV IWSDGPSGDI
410 420 430 440 450
YYDKGLTAAQ RARVETEALK YLRAHPQVQT VFTKAEIAAT PSPSGPPESW
460 470 480 490 500
SLIQEARASF YPSRSGDLLL LLKPRVMSIP EQAVMGSVAT HGSPWDTDRR
510 520 530 540 550
VPILFWRKGM QHFEQPLGVE TVDILPSLAA LIKLPVPKDQ IDGRCLDLVA

GKDDSCAGQ
Length:559
Mass (Da):59,982
Last modified:February 6, 2007 - v1
Checksum:i0A7A0F7838E1A186
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF143994 Genomic DNA. Translation: ABL96598.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF143994 Genomic DNA. Translation: ABL96598.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3Q3Q X-ray 1.95 A 1-559 [» ]
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.720.10. 2 hits.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR026263. Alkaline_phosphatase_prok.
IPR002591. Phosphodiest/P_Trfase.
[Graphical view ]
Pfami PF01663. Phosphodiest. 1 hit.
[Graphical view ]
PIRSFi PIRSF031924. Pi-irrepressible_AP. 1 hit.
SUPFAMi SSF53649. SSF53649. 2 hits.
ProtoNeti Search...

Publicationsi

  1. "Cloning and overexpression of alkaline phosphatase PhoK from Sphingomonas sp. strain BSAR-1 for bioprecipitation of uranium from alkaline solutions."
    Nilgiriwala K.S., Alahari A., Rao A.S., Apte S.K.
    Appl. Environ. Microbiol. 74:5516-5523(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION.
    Strain: BSAR-11 Publication.
  2. "PhoK alkaline phosphatase."
    Nilgiriwala K.S., Apte S.K.
    Submitted (SEP-2009) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: BSAR-11 Publication.
  3. "Crystallization and preliminary X-ray crystallographic analysis of PhoK, an extracellular alkaline phosphatase from Sphingomonas sp. BSAR-1."
    Nilgiriwala K.S., Bihani S.C., Das A., Prashar V., Kumar M., Ferrer J.L., Apte S.K., Hosur M.V.
    Acta Crystallogr. F 65:917-919(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
    Strain: BSAR-1.
  4. "X-ray structure reveals a new class and provides insight into evolution of alkaline phosphatases."
    Bihani S.C., Das A., Nilgiriwala K.S., Prashar V., Pirocchi M., Apte S.K., Ferrer J.L., Hosur M.V.
    PLoS ONE 6:E22767-E22767(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ZINC AND SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, DISULFIDE BONDS.
    Strain: BSAR-1.

Entry informationi

Entry nameiALPH_SPHSX
AccessioniPrimary (citable) accession number: A1YYW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: February 6, 2007
Last modified: November 26, 2014
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3