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P55859 (PNPH_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Purine nucleoside phosphorylase

Short name=PNP
EC=2.4.2.1
Alternative name(s):
Inosine phosphorylase
Gene names
Name:PNP
Synonyms:NP
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate.

Subunit structure

Homotrimer.

Subcellular location

Cytoplasmcytoskeleton By similarity.

Sequence similarities

Belongs to the PNP/MTAP phosphorylase family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processnucleoside metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpurine-nucleoside phosphorylase activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289Purine nucleoside phosphorylase
PRO_0000184535

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue951N6-acetyllysine By similarity

Experimental info

Sequence conflict21A → Q AA sequence Ref.1
Sequence conflict251P → S in AAX46392. Ref.2

Secondary structure

................................................. 289
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P55859 [UniParc].

Last modified February 5, 2008. Version 3.
Checksum: 7ECF84CCA494DEED

FASTA28932,037
        10         20         30         40         50         60 
MANGYTYEDY QDTAKWLLSH TEQRPQVAVI CGSGLGGLVN KLTQAQTFDY SEIPNFPEST 

        70         80         90        100        110        120 
VPGHAGRLVF GILNGRACVM MQGRFHMYEG YPFWKVTFPV RVFRLLGVET LVVTNAAGGL 

       130        140        150        160        170        180 
NPNFEVGDIM LIRDHINLPG FSGENPLRGP NEERFGVRFP AMSDAYDRDM RQKAHSTWKQ 

       190        200        210        220        230        240 
MGEQRELQEG TYVMLGGPNF ETVAECRLLR NLGADAVGMS TVPEVIVARH CGLRVFGFSL 

       250        260        270        280 
ITNKVIMDYE SQGKANHEEV LEAGKQAAQK LEQFVSLLMA SIPVSGHTG 

« Hide

References

« Hide 'large scale' references
[1]"Calf spleen purine nucleoside phosphorylase: purification, sequence and crystal structure of its complex with an N(7)-acycloguanosine inhibitor."
Bzowska A., Luic M., Schroeder W., Shugar D., Saenger W., Koellner G.
FEBS Lett. 367:214-218(1995) [PubMed: 7607309] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Spleen.
[2]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Uterus.
[4]"Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15-A resolution."
Koellner G., Luic M., Shugar D., Saenger W., Bzowska A.
J. Mol. Biol. 265:202-216(1997) [PubMed: 9020983] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
Tissue: Spleen.
[5]Mao C., Zhou M., Ealick S., Federov A.A., Almo S.C.
Submitted (JUL-1995) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
[6]"Calf spleen purine nucleoside phosphorylase complexed with substrates and substrate analogues."
Mao C., Cook W.J., Zhou M., Federov A.A., Almo S.C., Ealick S.E.
Biochemistry 37:7135-7146(1998) [PubMed: 9585525] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Tissue: Spleen.
[7]"The high resolution crystal structure of bovine spleen purine nucleoside phosphorylase in complex forms with phosphate and 9-deazainosine."
Pugmire M.J., Mao C., Ealick S.E.
Submitted (MAR-1998) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
Tissue: Spleen.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT021545 mRNA. Translation: AAX46392.1.
BC103291 mRNA. Translation: AAI03292.2.
IPIIPI00717573.
PIRS66203.
UniGeneBt.65253.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A9OX-ray2.00A3-289[»]
1A9PX-ray2.40A3-289[»]
1A9QX-ray2.00A3-282[»]
1A9RX-ray2.00A3-282[»]
1A9SX-ray2.00A3-289[»]
1A9TX-ray2.00A1-284[»]
1B8NX-ray2.00A3-284[»]
1B8OX-ray1.50A3-284[»]
1FXUX-ray2.20A3-289[»]
1LV8X-ray2.30A/B/C/D/E/F3-289[»]
1LVUX-ray2.05A/B/C/D/E/F3-289[»]
1PBNX-ray2.00A1-289[»]
1V48X-ray2.20A3-289[»]
1VFNX-ray2.15A4-284[»]
2AI1X-ray2.00A3-289[»]
2AI2X-ray1.70A3-289[»]
2AI3X-ray1.70A3-289[»]
2QPLX-ray2.10A3-284[»]
3FUCX-ray1.45A/B/C3-284[»]
3PNPX-ray1.60A1-289[»]
4PNPX-ray1.80A1-289[»]
ProteinModelPortalP55859.
SMRP55859. Positions 3-282.
ModBaseSearch...

Protein-protein interaction databases

STRINGP55859.

Proteomic databases

PRIDEP55859.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000016346; ENSBTAP00000016346; ENSBTAG00000012317.

Phylogenomic databases

eggNOGmaNOG14333.
HOVERGENHBG002460.
InParanoidP55859.
OrthoDBEOG4CZBGH.

Enzyme and pathway databases

BRENDA2.4.2.1. 908.

Family and domain databases

InterProIPR011268. InoGua/Xao_phosphorylase.
IPR000845. Nucleoside_phosphorylase_d.
IPR011270. Pur_Nuc_Pase_Ino/Guo-sp.
IPR001369. Purine_phosphorylase-2.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERPTHR11904. Mtap_PNP. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
PIRSFPIRSF000477. PurNPase. 1 hit.
TIGRFAMsTIGR01700. PNPH. 1 hit.
TIGR01697. PNPH-PUNA-XAPA. 1 hit.
PROSITEPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP55859.

Entry information

Entry namePNPH_BOVIN
AccessionPrimary (citable) accession number: P55859
Secondary accession number(s): Q3ZBH6, Q58DQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 5, 2008
Last modified: November 16, 2011
This is version 92 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families