Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hypoxanthine-guanine-xanthine phosphoribosyltransferase

Gene

LACZ

Organism
Plasmodium falciparum (isolate FCR-3 / Gambia)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Works with guanine, hypoxanthine and xanthine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway.

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein.

Pathwayi: GMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes GMP from guanine.
Proteins known to be involved in this subpathway in this organism are:
  1. Hypoxanthine-guanine-xanthine phosphoribosyltransferase (LACZ)
This subpathway is part of the pathway GMP 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 GMP from guanine, the pathway GMP biosynthesis via salvage pathway and in Purine metabolism.

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-xanthine phosphoribosyltransferase (LACZ)
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.

Pathwayi: XMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from xanthine.
Proteins known to be involved in this subpathway in this organism are:
  1. Hypoxanthine-guanine-xanthine phosphoribosyltransferase (LACZ)
This subpathway is part of the pathway XMP 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 XMP from xanthine, the pathway XMP biosynthesis via salvage pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei77GMP1
Active sitei148Proton acceptorBy similarity1
Binding sitei176GMP1
Metal bindingi204Magnesium1 Publication1
Binding sitei204GMP; via carbonyl oxygen1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi144 – 152GMP9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Keywords - Ligandi

Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.4.2.8. 4889.
UniPathwayiUPA00591; UER00648.
UPA00602; UER00658.
UPA00909; UER00887.

Names & Taxonomyi

Protein namesi
Recommended name:
Hypoxanthine-guanine-xanthine phosphoribosyltransferase (EC:2.4.2.22, EC:2.4.2.8)
Short name:
HGPRT
Short name:
HGXPRT
Short name:
HGXPRTase
Gene namesi
Name:LACZ
OrganismiPlasmodium falciparum (isolate FCR-3 / Gambia)
Taxonomic identifieri5838 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001395971 – 231Hypoxanthine-guanine-xanthine phosphoribosyltransferaseAdd BLAST231

Interactioni

Subunit structurei

Homotetramer.1 Publication

Chemistry databases

BindingDBiP20035.

Structurei

Secondary structure

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 29Combined sources3
Helixi34 – 39Combined sources6
Beta strandi40 – 45Combined sources6
Helixi47 – 65Combined sources19
Beta strandi70 – 76Combined sources7
Turni77 – 79Combined sources3
Helixi80 – 97Combined sources18
Beta strandi106 – 117Combined sources12
Beta strandi120 – 128Combined sources9
Helixi132 – 135Combined sources4
Beta strandi139 – 150Combined sources12
Helixi151 – 160Combined sources10
Helixi161 – 163Combined sources3
Beta strandi166 – 176Combined sources11
Beta strandi187 – 193Combined sources7
Beta strandi198 – 200Combined sources3
Beta strandi204 – 209Combined sources6
Beta strandi213 – 218Combined sources6
Helixi220 – 225Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CJBX-ray2.00A/B/C/D1-231[»]
2VFAX-ray2.80A/B1-56[»]
A/B171-231[»]
3OZFX-ray1.94A/B/C/D1-231[»]
3OZGX-ray1.99A/B/C/D1-231[»]
ProteinModelPortaliP20035.
SMRiP20035.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20035.

Family & Domainsi

Sequence similaritiesi

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.

P20035-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIPNNPGAG ENAFDPVFVN DDDGYDLDSF MIPAHYKKYL TKVLVPNGVI
60 70 80 90 100
KNRIEKLAYD IKKVYNNEEF HILCLLKGSR GFFTALLKHL SRIHNYSAVE
110 120 130 140 150
TSKPLFGEHY VRVKSYCNDQ STGTLEIVSE DLSCLKGKHV LIVEDIIDTG
160 170 180 190 200
KTLVKFCEYL KKFEIKTVAI ACLFIKRTPL WNGFKADFVG FSIPDHFVVG
210 220 230
YSLDYNEIFR DLDHCCLVND EGKKKYKATS L
Length:231
Mass (Da):26,348
Last modified:February 1, 1991 - v1
Checksum:i4E681B63FD3D8131
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16279 mRNA. Translation: CAA34355.1.
PIRiS06601.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16279 mRNA. Translation: CAA34355.1.
PIRiS06601.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CJBX-ray2.00A/B/C/D1-231[»]
2VFAX-ray2.80A/B1-56[»]
A/B171-231[»]
3OZFX-ray1.94A/B/C/D1-231[»]
3OZGX-ray1.99A/B/C/D1-231[»]
ProteinModelPortaliP20035.
SMRiP20035.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP20035.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00591; UER00648.
UPA00602; UER00658.
UPA00909; UER00887.
BRENDAi2.4.2.8. 4889.

Miscellaneous databases

EvolutionaryTraceiP20035.

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 nameiHGXR_PLAFG
AccessioniPrimary (citable) accession number: P20035
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 2, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.