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Protein

Hypoxanthine-guanine phosphoribosyltransferase

Gene

hpt

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

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-guanine 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 sitei126Proton acceptorBy similarity1
Binding sitei154IMPBy similarity1
Binding sitei176IMP; via carbonyl oxygenBy similarity1
Metal bindingi182MagnesiumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi122 – 131IMPBy similarity10
Nucleotide bindingi181 – 182IMPBy similarity2

GO - Molecular functioni

  • guanine phosphoribosyltransferase activity Source: MTBBASE
  • hypoxanthine phosphoribosyltransferase activity Source: MTBBASE
  • metal ion binding Source: UniProtKB-KW
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  • GMP biosynthetic process Source: MTBBASE
  • IMP biosynthetic process Source: MTBBASE
  • IMP salvage Source: UniProtKB-UniPathway
  • purine-containing compound salvage Source: MTBBASE
  • purine ribonucleoside salvage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Keywords - Ligandi

Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-7903-MONOMER.
UniPathwayiUPA00591; UER00648.

Names & Taxonomyi

Protein namesi
Recommended name:
Hypoxanthine-guanine phosphoribosyltransferase (EC:2.4.2.8)
Short name:
HGPRT
Short name:
HGPRTase
Gene namesi
Name:hpt
Synonyms:hprT
Ordered Locus Names:Rv3624c
ORF Names:MTCY15C10.28
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3624c.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001396091 – 202Hypoxanthine-guanine phosphoribosyltransferaseAdd BLAST202

Proteomic databases

PaxDbiP9WHQ9.

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv3624c.

Structurei

Secondary structure

1202
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni20 – 22Combined sources3
Beta strandi23 – 28Combined sources6
Helixi30 – 47Combined sources18
Turni48 – 50Combined sources3
Helixi51 – 55Combined sources5
Beta strandi59 – 64Combined sources6
Turni65 – 68Combined sources4
Helixi69 – 78Combined sources10
Beta strandi79 – 81Combined sources3
Beta strandi83 – 90Combined sources8
Beta strandi105 – 107Combined sources3
Beta strandi117 – 128Combined sources12
Helixi129 – 139Combined sources11
Beta strandi144 – 153Combined sources10
Helixi155 – 159Combined sources5
Beta strandi165 – 170Combined sources6
Beta strandi176 – 178Combined sources3
Beta strandi191 – 196Combined sources6
Turni198 – 200Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RHTX-ray2.76A/B/C/D2-202[»]
4RHUX-ray2.57A/B/C/D/E/F2-202[»]
4RHXX-ray2.03A/B/C/D2-202[»]
4RHYX-ray2.32A/B/C/D2-202[»]
ProteinModelPortaliP9WHQ9.
SMRiP9WHQ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108UGV. Bacteria.
COG0634. LUCA.
KOiK00760.
OMAiDIAYVGF.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
InterProiIPR005904. Hxn_phspho_trans.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01203. HGPRTase. 1 hit.
PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P9WHQ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHVTQSSSAI TPGQTAELYP GDIKSVLLTA EQIQARIAEL GEQIGNDYRE
60 70 80 90 100
LSATTGQDLL LITVLKGAVL FVTDLARAIP VPTQFEFMAV SSYGSSTSSS
110 120 130 140 150
GVVRILKDLD RDIHGRDVLI VEDVVDSGLT LSWLSRNLTS RNPRSLRVCT
160 170 180 190 200
LLRKPDAVHA NVEIAYVGFD IPNDFVVGYG LDYDERYRDL SYIGTLDPRV

YQ
Length:202
Mass (Da):22,251
Last modified:April 16, 2014 - v1
Checksum:i17AD6817A2F8ED90
GO

Sequence cautioni

The sequence CCP46447 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti173 – 174ND → KT in AAB48624 (Ref. 1) Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88876 Genomic DNA. Translation: AAB48624.1.
AL123456 Genomic DNA. Translation: CCP46447.1. Different initiation.
PIRiA70561.
RefSeqiNP_218141.1. NC_000962.3.
WP_003419558.1. NC_000962.3.
WP_003912454.1. NZ_KK339374.1.

Genome annotation databases

EnsemblBacteriaiCCP46447; CCP46447; Rv3624c.
GeneIDi885398.
KEGGimtu:Rv3624c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88876 Genomic DNA. Translation: AAB48624.1.
AL123456 Genomic DNA. Translation: CCP46447.1. Different initiation.
PIRiA70561.
RefSeqiNP_218141.1. NC_000962.3.
WP_003419558.1. NC_000962.3.
WP_003912454.1. NZ_KK339374.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RHTX-ray2.76A/B/C/D2-202[»]
4RHUX-ray2.57A/B/C/D/E/F2-202[»]
4RHXX-ray2.03A/B/C/D2-202[»]
4RHYX-ray2.32A/B/C/D2-202[»]
ProteinModelPortaliP9WHQ9.
SMRiP9WHQ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3624c.

Proteomic databases

PaxDbiP9WHQ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46447; CCP46447; Rv3624c.
GeneIDi885398.
KEGGimtu:Rv3624c.

Organism-specific databases

TubercuListiRv3624c.

Phylogenomic databases

eggNOGiENOG4108UGV. Bacteria.
COG0634. LUCA.
KOiK00760.
OMAiDIAYVGF.

Enzyme and pathway databases

UniPathwayiUPA00591; UER00648.
BioCyciMTBH37RV:G185E-7903-MONOMER.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
InterProiIPR005904. Hxn_phspho_trans.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01203. HGPRTase. 1 hit.
PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHPRT_MYCTU
AccessioniPrimary (citable) accession number: P9WHQ9
Secondary accession number(s): L0TER1
, O06383, P0A5T0, P96906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 30, 2016
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.