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P0A9M4 (HPRT_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hypoxanthine phosphoribosyltransferase

Short name=HPRT
EC=2.4.2.8
Gene names
Name:hpt
Ordered Locus Names:SF0122, S0124
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Acts preferentially on hypoxanthine; has very low activity towards guanine. Inactive towards xanthine By similarity.

Catalytic activity

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

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.

Pathway

Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Sequence caution

The sequence AAN41785.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAP15666.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processPurine salvage
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
Nucleotide-binding
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processIMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

purine ribonucleoside salvage

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionguanine phosphoribosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

hypoxanthine phosphoribosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 178178Hypoxanthine phosphoribosyltransferase
PRO_0000139636

Regions

Nucleotide binding99 – 10810IMP By similarity
Nucleotide binding158 – 1592IMP By similarity

Sites

Active site1031Proton acceptor By similarity
Metal binding1591Magnesium By similarity
Binding site1311IMP By similarity
Binding site1531IMP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A9M4 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: E1A75EB68231DC32

FASTA17820,115
        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 

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN41785.2. Different initiation.
AE014073 Genomic DNA. Translation: AAP15666.1. Different initiation.
RefSeqNP_706078.4. NC_004337.2.
NP_835861.2. NC_004741.1.

3D structure databases

ProteinModelPortalP0A9M4.
SMRP0A9M4. Positions 1-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF0122.

Proteomic databases

PaxDbP0A9M4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN41785; AAN41785; SF0122.
AAP15666; AAP15666; S0124.
GeneID1024487.
1076555.
KEGGsfl:SF0122.
sfx:S0124.
PATRIC18701190. VBIShiFle31049_0137.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0634.
HOGENOMHOG000236520.
KOK00760.
OrthoDBEOG693GNP.

Enzyme and pathway databases

UniPathwayUPA00591; UER00648.

Family and domain databases

Gene3D3.40.50.2020. 1 hit.
InterProIPR005904. Hxn_phspho_trans.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMSSF53271. SSF53271. 1 hit.
TIGRFAMsTIGR01203. HGPRTase. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHPRT_SHIFL
AccessionPrimary (citable) accession number: P0A9M4
Secondary accession number(s): P36766
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: June 11, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways