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Protein

Hypoxanthine phosphoribosyltransferase

Gene

hpt

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Acts preferentially on hypoxanthine; has very low activity towards guanine. Inactive towards xanthine.1 Publication

Catalytic activityi

IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate.1 Publication

Cofactori

Mg2+By similarityNote: 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

Pathwayi: IMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes IMP from hypoxanthine.
Proteins known to be involved in this subpathway in this organism are:
  1. Hypoxanthine phosphoribosyltransferase (hpt)
This subpathway is part of the pathway IMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from hypoxanthine, the pathway IMP biosynthesis via salvage pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei103Proton acceptorCurated1
Binding sitei131IMP1
Binding sitei153IMP; via carbonyl oxygen1
Metal bindingi159MagnesiumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi99 – 108IMP10
Nucleotide bindingi158 – 159IMP2

GO - Molecular functioni

  • guanine phosphoribosyltransferase activity Source: UniProtKB-EC
  • hypoxanthine phosphoribosyltransferase activity Source: EcoCyc
  • magnesium ion binding Source: EcoCyc
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  • GMP salvage Source: EcoliWiki
  • IMP salvage Source: EcoliWiki

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processPurine salvage
LigandMagnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:HYPOXANPRIBOSYLTRAN-MONOMER
MetaCyc:HYPOXANPRIBOSYLTRAN-MONOMER
UniPathwayiUPA00591; UER00648

Names & Taxonomyi

Protein namesi
Recommended name:
Hypoxanthine phosphoribosyltransferase (EC:2.4.2.8)
Short name:
HPRT
Gene namesi
Name:hpt
Ordered Locus Names:b0125, JW5009
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG20098 hpt

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB04566 Inosinic Acid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001396321 – 178Hypoxanthine phosphoribosyltransferaseAdd BLAST178

Proteomic databases

EPDiP0A9M2
PaxDbiP0A9M2
PRIDEiP0A9M2

2D gel databases

SWISS-2DPAGEiP0A9M2

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi4261679, 26 interactors
DIPiDIP-47994N
IntActiP0A9M2, 5 interactors
STRINGi316385.ECDH10B_0105

Structurei

Secondary structure

1178
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi11 – 29Combined sources19
Turni30 – 32Combined sources3
Beta strandi36 – 41Combined sources6
Turni42 – 45Combined sources4
Helixi46 – 54Combined sources9
Beta strandi61 – 67Combined sources7
Turni73 – 76Combined sources4
Beta strandi82 – 84Combined sources3
Beta strandi93 – 104Combined sources12
Helixi106 – 116Combined sources11
Beta strandi121 – 130Combined sources10
Helixi132 – 134Combined sources3
Beta strandi142 – 147Combined sources6
Beta strandi153 – 155Combined sources3
Beta strandi160 – 162Combined sources3
Beta strandi168 – 175Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G9SX-ray2.80A/B1-178[»]
1G9TX-ray2.80A/B1-178[»]
1GRVX-ray2.90A/B1-178[»]
5KNRX-ray2.86A/B1-178[»]
5KNSX-ray2.79A/B1-178[»]
5KNTX-ray2.55A/B1-178[»]
5KNUX-ray2.81A/B1-178[»]
5KNVX-ray2.86A/B1-178[»]
5KNXX-ray2.40A/B1-178[»]
ProteinModelPortaliP0A9M2
SMRiP0A9M2
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9M2

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108UGV Bacteria
COG0634 LUCA
HOGENOMiHOG000236520
InParanoidiP0A9M2
KOiK00760
OMAiTMDWMAV
PhylomeDBiP0A9M2

Family and domain databases

CDDicd06223 PRTases_typeI, 1 hit
InterProiView protein in InterPro
IPR005904 Hxn_phspho_trans
IPR000836 PRibTrfase_dom
IPR029057 PRTase-like
PfamiView protein in Pfam
PF00156 Pribosyltran, 1 hit
SUPFAMiSSF53271 SSF53271, 1 hit
TIGRFAMsiTIGR01203 HGPRTase, 1 hit
PROSITEiView protein in PROSITE
PS00103 PUR_PYR_PR_TRANSFER, 1 hit

Sequencei

Sequence statusi: Complete.

P0A9M2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHTVEVMIP EAEIKARIAE LGRQITERYK DSGSDMVLVG LLRGSFMFMA
60 70 80 90 100
DLCREVQVSH EVDFMTASSY GSGMSTTRDV KILKDLDEDI RGKDVLIVED
110 120 130 140 150
IIDSGNTLSK VREILSLREP KSLAICTLLD KPSRREVNVP VEFIGFSIPD
160 170
EFVVGYGIDY AQRYRHLPYI GKVILLDE
Length:178
Mass (Da):20,115
Last modified:July 19, 2005 - v1
Checksum:iE1A75EB68231DC32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC73236.2
AP009048 Genomic DNA Translation: BAB96700.2
RefSeqiNP_414667.4, NC_000913.3
WP_000683335.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73236; AAC73236; b0125
BAB96700; BAB96700; BAB96700
GeneIDi946624
KEGGiecj:JW5009
eco:b0125
PATRICifig|1411691.4.peg.2157

Similar proteinsi

Entry informationi

Entry nameiHPRT_ECOLI
AccessioniPrimary (citable) accession number: P0A9M2
Secondary accession number(s): P36766
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: March 28, 2018
This is version 105 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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