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Q9SE00

- PPAF1_IPOBA

UniProt

Q9SE00 - PPAF1_IPOBA

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Protein

Purple acid phosphatase 1

Gene
PAP1
Organism
Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.1 Publication

Cofactori

Binds 1 iron ion per subunit By similarity.2 Publications
Binds 1 manganese ion per subunit. Can also use zinc, copper and magnesium ions.2 Publications

Absorptioni

Abs(max)=560 nm2 Publications

Kineticsi

  1. KM=95 µM for p-NPP (at pH 4.9 and 25 degrees Celsius)
  2. KM=120 µM for ATP (at pH 4.9 and 25 degrees Celsius)
  3. KM=180 µM for ADP (at pH 4.9 and 25 degrees Celsius)
  4. KM=360 µM for AMP (at pH 4.9 and 25 degrees Celsius)
  5. KM=75 µM for pyrophosphate (at pH 4.9 and 25 degrees Celsius)
  6. KM=490 µM for beta-glycerophosphate (at pH 4.9 and 25 degrees Celsius)
  7. KM=44 µM for 4-nitrophenol phosphate (at pH 3.5)
  8. KM=68 µM for 4-nitrophenol phosphate (at pH 4)
  9. KM=68 µM for 4-nitrophenol phosphate (at pH 4.5)
  10. KM=93 µM for 4-nitrophenol phosphate (at pH 5)
  11. KM=330 µM for 4-nitrophenol phosphate (at pH 6)
  12. KM=930 µM for 4-nitrophenol phosphate (at pH 6.5)
  13. KM=1800 µM for 4-nitrophenol phosphate (at pH 7)
  14. KM=5000 µM for 4-nitrophenol phosphate (at pH 8)

pH dependencei

Optimum pH is 4.5.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi172 – 1721Iron By similarity
Metal bindingi201 – 2011Iron By similarity
Metal bindingi201 – 2011Manganese
Metal bindingi204 – 2041Iron By similarity
Metal bindingi238 – 2381Manganese
Binding sitei238 – 2381Substrate By similarity
Metal bindingi323 – 3231Manganese
Active sitei333 – 3331Proton donor By similarity
Metal bindingi360 – 3601Manganese
Metal bindingi362 – 3621Iron By similarity

GO - Molecular functioni

  1. acid phosphatase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15153.

Names & Taxonomyi

Protein namesi
Recommended name:
Purple acid phosphatase 1 (EC:3.1.3.2)
Alternative name(s):
Manganese(II) purple acid phosphatase 1
Gene namesi
Name:PAP1
OrganismiIpomoea batatas (Sweet potato) (Convolvulus batatas)
Taxonomic identifieri4120 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesConvolvulaceaeIpomoeeaeIpomoea

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3838 Reviewed predictionAdd
BLAST
Chaini39 – 473435Purple acid phosphatase 1PRO_5000057351Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi118 – 1181N-linked (GlcNAc...) Reviewed prediction
Glycosylationi180 – 1801N-linked (GlcNAc...) Reviewed prediction
Glycosylationi311 – 3111N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi382 – 382Interchain By similarity
Glycosylationi433 – 4331N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer; disulfide-linked By similarity.

Structurei

Secondary structure

1
473
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi42 – 454
Helixi52 – 543
Beta strandi64 – 707
Beta strandi72 – 765
Beta strandi78 – 869
Turni89 – 924
Beta strandi93 – 986
Beta strandi105 – 1084
Beta strandi110 – 1123
Beta strandi123 – 1297
Beta strandi137 – 1426
Helixi145 – 1473
Beta strandi149 – 1546
Beta strandi165 – 1706
Helixi177 – 18812
Beta strandi194 – 1985
Helixi205 – 2073
Helixi209 – 2113
Helixi214 – 22714
Helixi238 – 2403
Helixi245 – 2473
Helixi254 – 2596
Helixi265 – 2673
Beta strandi274 – 2796
Beta strandi282 – 2865
Helixi298 – 30912
Turni312 – 3143
Beta strandi317 – 3215
Turni332 – 3376
Helixi338 – 35013
Beta strandi354 – 3585
Beta strandi360 – 3678
Beta strandi369 – 3713
Beta strandi392 – 3965
Beta strandi417 – 4215
Beta strandi425 – 4317
Beta strandi433 – 44311
Beta strandi452 – 4587

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XZWX-ray2.50A/B39-464[»]
ProteinModelPortaliQ9SE00.
SMRiQ9SE00. Positions 39-464.

Miscellaneous databases

EvolutionaryTraceiQ9SE00.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni360 – 3623Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.380. 1 hit.
3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR008963. Purple_acid_Pase-like_N.
IPR015914. Purple_acid_Pase_N.
IPR025733. Purple_acid_PPase_C_dom.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
PF14008. Metallophos_C. 1 hit.
[Graphical view]
SUPFAMiSSF49363. SSF49363. 1 hit.
SSF56300. SSF56300. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9SE00-1 [UniParc]FASTAAdd to Basket

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MRLVVVGLWC LILGLILNPT KFCDAGVTSS YVRKSLSALP NAEDVDMPWD    50
SDVFAVPSGY NAPQQVHITQ GDYEGRGVII SWTTPYDKAG ANKVVYWSEN 100
SKSQKRAMGT VVTYKYYNYT SAFIHHCTIK DLEYDTKYYY RLGFGDAKRQ 150
FWFVTPPKPG PDVPYVFGLI GDIGQTHDSN TTLTHYEQNS AKGQAVLFMG 200
DLSYSNRWPN HDNNRWDTWG RFSERSVAYQ PWIWTAGNHE IDYAPDIGEY 250
QPFVPFTNRY PTPHEASGSG DPLWYAIKRA SAHIIVLSSY SGFVKYSPQY 300
KWFTSELEKV NRSETPWLIV LVHAPLYNSY EAHYMEGEAM RAIFEPYFVY 350
YKVDIVFSGH VHSYERSERV SNVAYNIVNA KCTPVSDESA PVYITIGDGG 400
NSEGLASEMT QPQPSYSAFR EASFGHGIFD IKNRTHAHFS WHRNQDGASV 450
EADSLWLLNR YWASEDASSM SAM 473
Length:473
Mass (Da):53,815
Last modified:May 1, 2000 - v1
Checksum:iBAE4B807DADD95A7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF200825 mRNA. Translation: AAF19821.1.
PIRiA59200.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF200825 mRNA. Translation: AAF19821.1 .
PIRi A59200.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XZW X-ray 2.50 A/B 39-464 [» ]
ProteinModelPortali Q9SE00.
SMRi Q9SE00. Positions 39-464.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-15153.

Miscellaneous databases

EvolutionaryTracei Q9SE00.

Family and domain databases

Gene3Di 2.60.40.380. 1 hit.
3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR008963. Purple_acid_Pase-like_N.
IPR015914. Purple_acid_Pase_N.
IPR025733. Purple_acid_PPase_C_dom.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
PF14008. Metallophos_C. 1 hit.
[Graphical view ]
SUPFAMi SSF49363. SSF49363. 1 hit.
SSF56300. SSF56300. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Binuclear metal centers in plant purple acid phosphatases: Fe-Mn in sweet potato and Fe-Zn in soybean."
    Schenk G., Ge Y., Carrington L.E., Wynne C.J., Searle I.R., Carroll B.J., Hamilton S., de Jersey J.
    Arch. Biochem. Biophys. 370:183-189(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: cv. Golden.
  2. "Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase."
    Schenk G., Gahan L.R., Carrington L.E., Mitic N., Valizadeh M., Hamilton S.E., de Jersey J., Guddat L.W.
    Proc. Natl. Acad. Sci. U.S.A. 102:273-278(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-464 IN COMPLEX WITH SUBSTRATE AND COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiPPAF1_IPOBA
AccessioniPrimary (citable) accession number: Q9SE00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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