P0A9M2 (HPRT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hypoxanthine phosphoribosyltransferase
Short name=HPRT
EC=2.4.2.8

Gene names

Name:	hpt
Ordered Locus Names:	b0125, JW5009

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	178 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts preferentially on hypoxanthine; has very low activity towards guanine. Inactive towards xanthine. Ref.4
Catalytic activity	IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.4
Cofactor	Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein By similarity. Ref.4
Pathway	Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Subunit structure	Homotetramer. Ref.4
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Ontologies

Keywords
Biological process	Purine salvage
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding Nucleotide-binding
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GMP salvage Inferred from direct assay Ref.4. Source: EcoliWiki IMP salvage Inferred from direct assay Ref.4. Source: EcoliWiki adenine salvage Inferred from Biological aspect of Ancestor. Source: RefGenome guanine salvage Inferred from Biological aspect of Ancestor. Source: RefGenome hypoxanthine metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome purine ribonucleoside salvage Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	guanine phosphoribosyltransferase activity Inferred from electronic annotation. Source: EC hypoxanthine phosphoribosyltransferase activity Inferred from direct assay Ref.4. Source: EcoCyc magnesium ion binding Inferred from direct assay PubMed 692401. Source: EcoCyc nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 178

178

Hypoxanthine phosphoribosyltransferase

PRO_0000139632

Regions

Nucleotide binding

99 – 108

10

IMP

Nucleotide binding

158 – 159

2

IMP

Sites

Active site

103

1

Proton acceptor Probable

Metal binding

159

1

Magnesium By similarity

Binding site

131

1

IMP

Binding site

153

1

IMP; via carbonyl oxygen

Secondary structure

1

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178

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

11 – 29

19

Turn

30 – 32

3

Beta strand

36 – 42

7

Turn

43 – 45

3

Helix

46 – 53

8

Beta strand

61 – 67

7

Beta strand

82 – 84

3

Beta strand

93 – 104

12

Helix

106 – 116

11

Beta strand

120 – 130

11

Helix

132 – 134

3

Beta strand

143 – 147

5

Beta strand

153 – 155

3

Beta strand

160 – 162

3

Beta strand

168 – 173

6

Sequences

	Sequence		Length	Mass (Da)
	P0A9M2 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: E1A75EB68231DC32	FASTA	178	20,115
	10 20 30 40 50 60 MKHTVEVMIP EAEIKARIAE LGRQITERYK DSGSDMVLVG LLRGSFMFMA DLCREVQVSH 70 80 90 100 110 120 EVDFMTASSY GSGMSTTRDV KILKDLDEDI RGKDVLIVED IIDSGNTLSK VREILSLREP 130 140 150 160 170 KSLAICTLLD KPSRREVNVP VEFIGFSIPD EFVVGYGIDY AQRYRHLPYI GKVILLDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Crystal structures of free, IMP-, and GMP-bound Escherichia coli hypoxanthine phosphoribosyltransferase." Guddat L.W., Vos S., Martin J.L., Keough D.T., de Jersey J. Protein Sci. 11:1626-1638(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEXES WITH IMP; GMP AND MAGNESIUM, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, COFACTOR, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00096 Genomic DNA. Translation: AAC73236.2.
AP009048 Genomic DNA. Translation: BAB96700.2.

RefSeq

NP_414667.4. NC_000913.2.
YP_488428.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G9S	X-ray	2.80	A/B	1-178	[»]
1G9T	X-ray	2.80	A/B	1-178	[»]
1GRV	X-ray	2.90	A/B	1-178	[»]

ProteinModelPortal

P0A9M2.

SMR

P0A9M2. Positions 1-177.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47994N.

STRING

511145.b0125.

2D gel databases

SWISS-2DPAGE

P0A9M2.

Proteomic databases

PaxDb

P0A9M2.

PRIDE

P0A9M2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73236; AAC73236; b0125.
BAB96700; BAB96700; BAB96700.

GeneID

12932685.
946624.

KEGG

ecj:Y75_p0122.
eco:b0125.

PATRIC

32115353. VBIEscCol129921_0128.

Organism-specific databases

EchoBASE

EB4143.

EcoGene

EG20098. hpt.

Phylogenomic databases

eggNOG

COG0634.

HOGENOM

HOG000236520.

KO

K00760.

OMA

SIKIVTL.

ProtClustDB

PRK15423.

Enzyme and pathway databases

BioCyc

EcoCyc:HYPOXANPRIBOSYLTRAN-MONOMER.
ECOL316407:JW5009-MONOMER.
MetaCyc:HYPOXANPRIBOSYLTRAN-MONOMER.

UniPathway

UPA00591; UER00648.

Gene expression databases

Genevestigator

P0A9M2.

Family and domain databases

InterPro

IPR005904. Hxn_phspho_trans.
IPR000836. PRibTrfase_dom.
[Graphical view]

Pfam

PF00156. Pribosyltran. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01203. HGPRTase. 1 hit.

PROSITE

PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A9M2.

Entry information

Entry name

HPRT_ECOLI

Accession

Primary (citable) accession number: P0A9M2
Secondary accession number(s): P36766

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program