Q980Q4 (UPP_SULSO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uracil phosphoribosyltransferase
EC=2.4.2.9

Alternative name(s):
UMP pyrophosphorylase
UPRTase

Gene names

Name:	upp
Ordered Locus Names:	SSO0231

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	216 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. Ref.2
Catalytic activity	UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.2
Cofactor	Binds 1 Mg2+ ion per subunit. The magnesium is bound as Mg-PRPP By similarity.
Enzyme regulation	Allosterically activated by GTP. Inhibited by CTP and UMP in combination. Ref.2
Pathway	Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1. HAMAP MF_01218_A
Subunit structure	Homotetramer. Ref.2
Sequence similarities	Belongs to the UPRTase family.
Biophysicochemical properties	Kinetic parameters: KM=55 µM for 5-phospho-alpha-D-ribose 1-diphosphate (in the presence of 1 mM GTP) Ref.2 KM=19 µM for 5-phospho-alpha-D-ribose 1-diphosphate (without GTP) KM=27 µM for uracil (in the presence of 1 mM GTP) KM=1.4 µM for uracil (without GTP) Vmax=15.8 µmol/min/mg enzyme (in the presence of 1 mM GTP) Vmax=0.92 µmol/min/mg enzyme (without GTP) pH dependence: Optimum pH is 5.0-5.6 at 60 degrees Celsius.

Ontologies

Keywords
Ligand	GTP-binding Magnesium Nucleotide-binding
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nucleoside metabolic process Inferred from electronic annotation. Source: InterPro uracil salvage Inferred from electronic annotation. Source: InterPro
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW uracil phosphoribosyltransferase 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 – 216

216

Uracil phosphoribosyltransferase HAMAP MF_01218_A

PRO_0000120927

Regions

Nucleotide binding

29 – 30

2

CTP HAMAP MF_01218_A

Nucleotide binding

30 – 34

5

GTP HAMAP MF_01218_A

Nucleotide binding

87 – 96

10

CTP HAMAP MF_01218_A

Region

140 – 148

9

5-phospho-alpha-D-ribose 1-diphosphate binding HAMAP MF_01218_A

Region

208 – 210

3

Uracil binding HAMAP MF_01218_A

Sites

Binding site

37

1

CTP

Binding site

80

1

5-phospho-alpha-D-ribose 1-diphosphate

Binding site

105

1

5-phospho-alpha-D-ribose 1-diphosphate

Binding site

203

1

Uracil; via amide nitrogen

Binding site

209

1

5-phospho-alpha-D-ribose 1-diphosphate

Secondary structure

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216

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Helix

9 – 19

11

Helix

25 – 44

20

Beta strand

50 – 55

6

Beta strand

61 – 66

6

Helix

68 – 71

4

Beta strand

72 – 79

8

Turn

80 – 82

3

Helix

83 – 92

10

Beta strand

97 – 105

9

Beta strand

119 – 125

7

Turn

131 – 133

3

Beta strand

135 – 139

5

Beta strand

141 – 146

6

Helix

147 – 156

10

Helix

157 – 159

3

Beta strand

162 – 167

6

Beta strand

169 – 172

4

Helix

173 – 182

10

Beta strand

186 – 197

12

Beta strand

203 – 206

4

Helix

210 – 215

6

Sequences

	Sequence		Length	Mass (Da)
	Q980Q4 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 08F934237C3FD158	FASTA	216	24,150
	10 20 30 40 50 60 MPLYVIDKPI TLHILTQLRD KYTDQINFRK NLVRLGRILG YEISNTLDYE IVEVETPLGV 70 80 90 100 110 120 KTKGVDITDL NNIVIINILR AAVPLVEGLL KAFPKARQGV IGASRVEVDG KEVPKDMDVY 130 140 150 160 170 180 IYYKKIPDIR AKVDNVIIAD PMIATASTML KVLEEVVKAN PKRIYIVSII SSEYGVNKIL 190 200 210 SKYPFIYLFT VAIDPELNNK GYILPGLGDA GDRAFG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"Allosteric properties of the GTP activated and CTP inhibited uracil phosphoribosyltransferase from the thermoacidophilic archaeon Sulfolobus solfataricus." Jensen K.F., Arent S., Larsen S., Schack L. FEBS J. 272:1440-1453(2005) [PubMed: 15752360] [Abstract] Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, KINETIC ANALYSIS, ENZYME REGULATION, REACTION MECHANISM. Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[3]	"Allosteric regulation and communication between subunits in uracil phosphoribosyltransferase from Sulfolobus solfataricus." Arent S., Harris P., Jensen K.F., Larsen S. Biochemistry 44:883-892(2005) [PubMed: 15654744] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH UMP AND CTP, REACTION MECHANISM.
[4]	"Structural and kinetic studies of the allosteric transition in Sulfolobus solfataricus uracil phosphoribosyltransferase: Permanent activation by engineering of the C-terminus." Christoffersen S., Kadziola A., Johansson E., Rasmussen M., Willemoes M., Jensen K.F. J. Mol. Biol. 393:464-477(2009) [PubMed: 19683539] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEXES WITH GTP; 5-PHOSPHO-ALPHA-D-RIBOSE 1-DIPHOSPHATE; RIBOSE-5-PHOSPHATE AND DIPHOSPHATE, REACTION MECHANISM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE006641 Genomic DNA. Translation: AAK40574.1.

PIR

G90164.

RefSeq

NP_341784.1. NC_002754.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VST	X-ray	2.80	A	1-216	[»]
1XTT	X-ray	1.80	A/B/C/D	1-216	[»]
1XTU	X-ray	2.80	A/B/C/D/E/F/G/H	1-216	[»]
1XTV	X-ray	2.60	A/B/C/D/E/F/G/H	1-216	[»]
3G6W	X-ray	2.90	A/B/C/D	1-216	[»]

ProteinModelPortal

Q980Q4.

SMR

Q980Q4. Positions 2-216.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1455384.

GenomeReviews

Gene locus SSO0231 in contig AE006641_GR.

KEGG

sso:SSO0231.

NMPDR

fig|273057.1.peg.207.

Phylogenomic databases

HOGENOM

HBG326432.

OMA

VYVLDPM.

ProtClustDB

PRK00129.

Enzyme and pathway databases

BioCyc

SSOL273057:SSO0231-MONOMER.

Family and domain databases

HAMAP

MF_01218_A. Upp_A.
[Tree]

InterPro

IPR000836. PRibTrfase.
IPR005765. Ura_phspho_trans.
[Graphical view]

KO

K00761.

Pfam

PF00156. Pribosyltran. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01091. Upp. 1 hit.

ProtoNet

Search...

Entry information

Entry name

UPP_SULSO

Accession

Primary (citable) accession number: Q980Q4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	October 1, 2001
Last modified:	November 16, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program