Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9SE00

- PPAF1_IPOBA

UniProt

Q9SE00 - PPAF1_IPOBA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

Protein has several cofactor binding sites:

Absorptioni

Abs(max)=560 nm2 Publications

Kineticsi

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

pH dependencei

Optimum pH is 4.5.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi172 – 1721IronBy similarity
Metal bindingi201 – 2011IronBy similarity
Metal bindingi201 – 2011Manganese
Metal bindingi204 – 2041IronBy similarity
Metal bindingi238 – 2381Manganese
Binding sitei238 – 2381SubstrateBy similarity
Metal bindingi323 – 3231Manganese
Active sitei333 – 3331Proton donorBy similarity
Metal bindingi360 – 3601Manganese
Metal bindingi362 – 3621IronBy 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-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi382 – 382InterchainBy similarity
Glycosylationi433 – 4331N-linked (GlcNAc...)Sequence Analysis

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 – 454Combined sources
Helixi52 – 543Combined sources
Beta strandi64 – 707Combined sources
Beta strandi72 – 765Combined sources
Beta strandi78 – 869Combined sources
Turni89 – 924Combined sources
Beta strandi93 – 986Combined sources
Beta strandi105 – 1084Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi123 – 1297Combined sources
Beta strandi137 – 1426Combined sources
Helixi145 – 1473Combined sources
Beta strandi149 – 1546Combined sources
Beta strandi165 – 1706Combined sources
Helixi177 – 18812Combined sources
Beta strandi194 – 1985Combined sources
Helixi205 – 2073Combined sources
Helixi209 – 2113Combined sources
Helixi214 – 22714Combined sources
Helixi238 – 2403Combined sources
Helixi245 – 2473Combined sources
Helixi254 – 2596Combined sources
Helixi265 – 2673Combined sources
Beta strandi274 – 2796Combined sources
Beta strandi282 – 2865Combined sources
Helixi298 – 30912Combined sources
Turni312 – 3143Combined sources
Beta strandi317 – 3215Combined sources
Turni332 – 3376Combined sources
Helixi338 – 35013Combined sources
Beta strandi354 – 3585Combined sources
Beta strandi360 – 3678Combined sources
Beta strandi369 – 3713Combined sources
Beta strandi392 – 3965Combined sources
Beta strandi417 – 4215Combined sources
Beta strandi425 – 4317Combined sources
Beta strandi433 – 44311Combined sources
Beta strandi452 – 4587Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XZWX-ray2.50A/B39-464[»]
ProteinModelPortaliQ9SE00.
SMRiQ9SE00. Positions 39-464.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9SE00.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni360 – 3623Substrate bindingBy 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

« Hide

        10         20         30         40         50
MRLVVVGLWC LILGLILNPT KFCDAGVTSS YVRKSLSALP NAEDVDMPWD
60 70 80 90 100
SDVFAVPSGY NAPQQVHITQ GDYEGRGVII SWTTPYDKAG ANKVVYWSEN
110 120 130 140 150
SKSQKRAMGT VVTYKYYNYT SAFIHHCTIK DLEYDTKYYY RLGFGDAKRQ
160 170 180 190 200
FWFVTPPKPG PDVPYVFGLI GDIGQTHDSN TTLTHYEQNS AKGQAVLFMG
210 220 230 240 250
DLSYSNRWPN HDNNRWDTWG RFSERSVAYQ PWIWTAGNHE IDYAPDIGEY
260 270 280 290 300
QPFVPFTNRY PTPHEASGSG DPLWYAIKRA SAHIIVLSSY SGFVKYSPQY
310 320 330 340 350
KWFTSELEKV NRSETPWLIV LVHAPLYNSY EAHYMEGEAM RAIFEPYFVY
360 370 380 390 400
YKVDIVFSGH VHSYERSERV SNVAYNIVNA KCTPVSDESA PVYITIGDGG
410 420 430 440 450
NSEGLASEMT QPQPSYSAFR EASFGHGIFD IKNRTHAHFS WHRNQDGASV
460 470
EADSLWLLNR YWASEDASSM SAM
Length:473
Mass (Da):53,815
Last modified:May 1, 2000 - v1
Checksum:iBAE4B807DADD95A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF200825 mRNA. Translation: AAF19821.1.
PIRiA59200.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF200825 mRNA. Translation: AAF19821.1 .
PIRi A59200.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 63 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