O67914 (UPP_AQUAE) 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
Synonyms:	uraP
Ordered Locus Names:	aq_2163

Organism

Aquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Aquificae › Aquificae › Aquificales › Aquificaceae › Aquifex › Aquifex aeolicus

Protein attributes

Sequence length	208 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 By similarity. HAMAP-Rule MF_01218
Catalytic activity	UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_01218
Cofactor	Binds 1 Mg2+ ion per subunit. The magnesium is bound as Mg-PRPP By similarity.
Enzyme regulation	Allosterically activated by GTP By similarity. HAMAP-Rule MF_01218
Pathway	Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1. HAMAP-Rule MF_01218
Sequence similarities	Belongs to the UPRTase family.

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	UMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway uracil salvage Inferred from electronic annotation. Source: InterPro
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: HAMAP uracil phosphoribosyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 208

208

Uracil phosphoribosyltransferase HAMAP-Rule MF_01218

PRO_0000120792

Regions

Region

128 – 136

9

5-phospho-alpha-D-ribose 1-diphosphate binding By similarity

Region

196 – 198

3

Uracil binding By similarity

Sites

Binding site

77

1

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

Binding site

102

1

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

Binding site

191

1

Uracil; via amide nitrogen By similarity

Binding site

197

1

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

Secondary structure

1

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208

Helix Strand Turn

Details...

Beta strand

2 – 4

3

Helix

8 – 18

11

Helix

24 – 42

19

Turn

43 – 45

3

Beta strand

49 – 55

7

Beta strand

58 – 64

7

Helix

67 – 69

3

Beta strand

70 – 76

7

Turn

77 – 79

3

Helix

80 – 89

10

Beta strand

97 – 102

6

Turn

104 – 106

3

Beta strand

109 – 115

7

Beta strand

122 – 127

6

Beta strand

129 – 134

6

Helix

135 – 145

11

Beta strand

149 – 159

11

Helix

161 – 170

10

Beta strand

174 – 181

8

Beta strand

183 – 185

3

Beta strand

191 – 194

4

Helix

198 – 203

6

Sequences

	Sequence		Length	Mass (Da)
	O67914 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 87B9CFEFEA9CFF77	FASTA	208	23,533
	10 20 30 40 50 60 MIVELSHPLI KHKVNTARIQ DTSAEKLRKT LKELGFMLVY EALKDILLEE KEVRTWIGNK 70 80 90 100 110 120 RFNYLNEEEI VFVPILRAGL SFLEGALQVV PNAKVGFLGI KRNEETLESH IYYSRLPELK 130 140 150 160 170 180 GKIVVILDPM LATGGTLEVA LREILKHSPL KVKSVHAIAA PEGLKRIEEK FKEVEIFVGN 190 200 VDERLNDKGY IIPGLGDIGD RLYAVSVY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
[2]	"Structure of aq2163 protein from Aquifex aeolicus." RIKEN structural genomics initiative (RSGI) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000657 Genomic DNA. Translation: AAC07880.1.

PIR

F70485.

RefSeq

NP_214483.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E55	X-ray	2.15	A/B/C/D	1-208	[»]

ProteinModelPortal

O67914.

SMR

O67914. Positions 1-208.

ModBase

Search...

Protein-protein interaction databases

STRING

224324.aq_2163.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC07880; AAC07880; aq_2163.

GeneID

1193903.

KEGG

aae:aq_2163.

PATRIC

20961160. VBIAquAeo85532_1671.

Phylogenomic databases

eggNOG

COG0035.

HOGENOM

HOG000262754.

KO

K00761.

OMA

DSPTFRR.

Enzyme and pathway databases

BioCyc

AAEO224324:GJBH-1548-MONOMER.

UniPathway

UPA00574; UER00636.

Family and domain databases

HAMAP

MF_01218_B. Upp_B.

InterPro

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

Pfam

PF00156. Pribosyltran. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01091. upp. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O67914.

Entry information

Entry name

UPP_AQUAE

Accession

Primary (citable) accession number: O67914

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program