P50389 (PNPH_SULSO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Purine nucleoside phosphorylase
Short name=PNP
EC=2.4.2.1

Alternative name(s):
5'-methylthioadenosine phosphorylase I
Short name=MTA phosphorylase I
Short name=MTAPI

Gene names

Ordered Locus Names:

SSO2706

Organism

Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

Taxonomic identifier

273057 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length	236 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. Cleaves inosine, guanosine, and adenosine with a better efficiency than MTA. Ref.3 Ref.4
Catalytic activity	S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate. Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate.
Pathway	Purine metabolism; purine nucleoside salvage.
Subunit structure	Homohexamer; disulfide-linked. Trimer of homodimers, with three symmetric intersubunit disulfide bonds linking the dimers to one another. Ref.3
Sequence similarities	Belongs to the PNP/UDP phosphorylase family.
Biophysicochemical properties	Kinetic parameters: KM=154 µM for S-methyl-5'-thioadenosine Ref.4 KM=25.4 µM for adenosine KM=84 µM for inosine KM=113.6 µM for guanosine Temperature dependence: Optimum temperature is 120 degrees Celsius. Highly thermostable.

Ontologies

Keywords
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	nucleoside metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	S-methyl-5-thioadenosine phosphorylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 236

236

Purine nucleoside phosphorylase

PRO_0000063195

Regions

Region

86 – 89

4

Phosphate binding

Region

180 – 182

3

Substrate binding

Region

204 – 205

2

Substrate binding

Sites

Binding site

5

1

Substrate; shared with dimeric partner

Binding site

21

1

Phosphate; via amide nitrogen

Binding site

25

1

Phosphate

Binding site

43

1

Phosphate; shared with dimeric partner

Binding site

163

1

Substrate

Amino acid modifications

Disulfide bond

125

Interchain

Secondary structure

1

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236

Helix Strand Turn

Details...

Beta strand

15 – 21

7

Helix

23 – 29

7

Helix

30 – 32

3

Beta strand

33 – 40

8

Helix

42 – 44

3

Beta strand

47 – 52

6

Beta strand

55 – 61

7

Helix

66 – 78

13

Beta strand

83 – 94

12

Beta strand

102 – 110

9

Helix

114 – 120

7

Helix

132 – 144

13

Beta strand

149 – 156

8

Helix

167 – 172

6

Turn

173 – 175

3

Beta strand

176 – 182

7

Helix

183 – 193

11

Beta strand

196 – 207

12

Helix

219 – 234

16

Sequences

	Sequence		Length	Mass (Da)
	P50389 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: F1570ECE8AA3D51B	FASTA	236	25,738
	10 20 30 40 50 60 MNPVHILAKK GEVAERVLVV GDPGRARLLS TLLQNPKLTN ENRGFLVYTG KYNGETVSIA 70 80 90 100 110 120 THGIGGPSIA IVLEELAMLG ANVFIRYGTT GALVPYINLG EYIIVTGASY NQGGLFYQYL 130 140 150 160 170 180 RDNACVASTP DFELTNKLVT SFSKRNLKYY VGNVFSSDAF YAEDEEFVKK WSSRGNIAVE 190 200 210 220 230 MECATLFTLS KVKGWKSATV LVVSDNLAKG GIWITKEELE KSVMDGAKAV LDTLTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Gene cloning and amino acid sequence determination." Cacciapuoti G., Porcelli M., Bertoldo C., Fusco S., De Rosa M., Zappia V. Eur. J. Biochem. 239:632-637(1996) [PubMed: 8774706] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[2]	"The complete genome of the crenarchaeon Sulfolobus solfataricus P2." She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J. Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed: 11427726] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[3]	"Purification and characterization of extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and evidence for intersubunit disulfide bonds." Cacciapuoti G., Porcelli M., Bertoldo C., de Rosa M., Zappia V. J. Biol. Chem. 269:24762-24769(1994) [PubMed: 7929153] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-26, FUNCTION, SUBUNIT.
[4]	"A novel hyperthermostable 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus." Cacciapuoti G., Forte S., Moretti M.A., Brio A., Zappia V., Porcelli M. FEBS J. 272:1886-1899(2005) [PubMed: 15819883] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[5]	"Three-dimensional structure of a hyperthermophilic 5'-deoxy-5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus." Appleby T.C., Mathews I.I., Porcelli M., Cacciapuoti G., Ealick S.E. J. Biol. Chem. 276:39232-39242(2001) [PubMed: 11489901] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH SUBSTRATES AND SUBSTRATE ANALOGS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z50181 Genomic DNA. Translation: CAA90560.1.
AE006641 Genomic DNA. Translation: AAK42818.1.

PIR

S58291.

RefSeq

NP_344028.1. NC_002754.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JDS	X-ray	1.80	A/B/C/D/E/F	1-236	[»]
1JDT	X-ray	2.00	A/B/C	1-236	[»]
1JDU	X-ray	2.50	A/B/C	1-236	[»]
1JDV	X-ray	2.00	A/B/C/D/E/F	1-236	[»]
1JDZ	X-ray	2.00	A/B/C	1-236	[»]
1JE0	X-ray	1.60	A/B/C	1-236	[»]
1JE1	X-ray	1.80	A/B/C/D/E/F	1-236	[»]
1JP7	X-ray	1.80	A/B/C	1-236	[»]
1JPV	X-ray	1.80	A/B/C	1-236	[»]

ProteinModelPortal

P50389.

SMR

P50389. Positions 2-236.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1452737.

GenomeReviews

Gene locus SSO2706 in contig AE006641_GR.

KEGG

sso:SSO2706.

NMPDR

fig|273057.1.peg.2451.

Phylogenomic databases

HOGENOM

HBG617197.

OMA

LAVEMEC.

ProtClustDB

CLSK803477.

Enzyme and pathway databases

BioCyc

SSOL273057:SSO2706-MONOMER.

BRENDA

2.4.2.28. 6163.

Family and domain databases

InterPro

IPR018017. Nucleoside_phosphorylase.
IPR018016. Nucleoside_phosphorylase_CS.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view]

KO

K00772.

PANTHER

PTHR21234. PNP_UDP. 1 hit.

Pfam

PF01048. PNP_UDP_1. 1 hit.
[Graphical view]

PROSITE

PS01232. PNP_UDP_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PNPH_SULSO

Accession

Primary (citable) accession number: P50389

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program