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Protein

Amidophosphoribosyltransferase

Gene

PPAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity
  • [4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Amidophosphoribosyltransferase (PPAT), Amidophosphoribosyltransferase (PPAT)
  2. Trifunctional purine biosynthetic protein adenosine-3, Trifunctional purine biosynthetic protein adenosine-3 (GART), Trifunctional purine biosynthetic protein adenosine-3 (GART)
This subpathway is part of the pathway IMP biosynthesis via de novo 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 N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei12NucleophilePROSITE-ProRule annotation1
Metal bindingi280Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi327MagnesiumBy similarity1
Metal bindingi389MagnesiumBy similarity1
Metal bindingi390MagnesiumBy similarity1
Metal bindingi426Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi503Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi506Iron-sulfur (4Fe-4S)By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS05157-MONOMER.
ZFISH:HS05157-MONOMER.
ReactomeiR-HSA-73817. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00074; UER00124.

Protein family/group databases

MEROPSiC44.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Amidophosphoribosyltransferase (EC:2.4.2.14)
Short name:
ATase
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase
Short name:
GPAT
Gene namesi
Name:PPAT
Synonyms:GPAT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:9238. PPAT.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi5471.
OpenTargetsiENSG00000128059.
PharmGKBiPA33559.

Chemistry databases

ChEMBLiCHEMBL2362992.
DrugBankiDB00544. Fluorouracil.
DB00130. L-Glutamine.
DB01033. Mercaptopurine.

Polymorphism and mutation databases

BioMutaiPPAT.
DMDMi548638.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000292831 – 11CuratedAdd BLAST11
ChainiPRO_000002928412 – 517AmidophosphoribosyltransferaseAdd BLAST506

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ06203.
MaxQBiQ06203.
PaxDbiQ06203.
PeptideAtlasiQ06203.
PRIDEiQ06203.

PTM databases

iPTMnetiQ06203.
PhosphoSitePlusiQ06203.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiENSG00000128059.
CleanExiHS_PPAT.
ExpressionAtlasiQ06203. baseline and differential.
GenevisibleiQ06203. HS.

Organism-specific databases

HPAiHPA036091.
HPA036092.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi111467. 38 interactors.
IntActiQ06203. 3 interactors.
STRINGi9606.ENSP00000264220.

Structurei

3D structure databases

ProteinModelPortaliQ06203.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 261Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd BLAST250

Sequence similaritiesi

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.Curated
Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiKOG0572. Eukaryota.
COG0034. LUCA.
GeneTreeiENSGT00390000003428.
HOGENOMiHOG000033688.
HOVERGENiHBG002589.
InParanoidiQ06203.
KOiK00764.
OMAiIRHFGVK.
OrthoDBiEOG091G06F7.
PhylomeDBiQ06203.
TreeFamiTF106370.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF. 1 hit.
InterProiIPR017932. GATase_2_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005854. PurF.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFiPIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMiSSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01134. purF. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q06203-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELEELGIRE ECGVFGCIAS GEWPTQLDVP HVITLGLVGL QHRGQESAGI
60 70 80 90 100
VTSDGSSVPT FKSHKGMGLV NHVFTEDNLK KLYVSNLGIG HTRYATTGKC
110 120 130 140 150
ELENCQPFVV ETLHGKIAVA HNGELVNAAR LRKKLLRHGI GLSTSSDSEM
160 170 180 190 200
ITQLLAYTPP QEQDDTPDWV ARIKNLMKEA PTAYSLLIMH RDVIYAVRDP
210 220 230 240 250
YGNRPLCIGR LIPVSDINDK EKKTSETEGW VVSSESCSFL SIGARYYREV
260 270 280 290 300
LPGEIVEISR HNVQTLDIIS RSEGNPVAFC IFEYVYFARP DSMFEDQMVY
310 320 330 340 350
TVRYRCGQQL AIEAPVDADL VSTVPESATP AALAYAGKCG LPYVEVLCKN
360 370 380 390 400
RYVGRTFIQP NMRLRQLGVA KKFGVLSDNF KGKRIVLVDD SIVRGNTISP
410 420 430 440 450
IIKLLKESGA KEVHIRVASP PIKYPCFMGI NIPTKEELIA NKPEFDHLAE
460 470 480 490 500
YLGANSVVYL SVEGLVSSVQ EGIKFKKQKE KKHDIMIQEN GNGLECFEKS
510
GHCTACLTGK YPVELEW
Length:517
Mass (Da):57,399
Last modified:June 1, 1994 - v1
Checksum:iD3F2A354C36B29D9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti369V → I in AAC27345 (PubMed:8106516).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13757 mRNA. Translation: BAA02903.1.
U00238 mRNA. Translation: AAC27345.1.
U00239 Genomic DNA. No translation available.
BC004200 mRNA. Translation: AAH04200.1.
CCDSiCCDS3505.1.
PIRiA53342.
RefSeqiNP_002694.3. NM_002703.4.
UniGeneiHs.331420.

Genome annotation databases

EnsembliENST00000264220; ENSP00000264220; ENSG00000128059.
GeneIDi5471.
KEGGihsa:5471.
UCSCiuc003hbr.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13757 mRNA. Translation: BAA02903.1.
U00238 mRNA. Translation: AAC27345.1.
U00239 Genomic DNA. No translation available.
BC004200 mRNA. Translation: AAH04200.1.
CCDSiCCDS3505.1.
PIRiA53342.
RefSeqiNP_002694.3. NM_002703.4.
UniGeneiHs.331420.

3D structure databases

ProteinModelPortaliQ06203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111467. 38 interactors.
IntActiQ06203. 3 interactors.
STRINGi9606.ENSP00000264220.

Chemistry databases

ChEMBLiCHEMBL2362992.
DrugBankiDB00544. Fluorouracil.
DB00130. L-Glutamine.
DB01033. Mercaptopurine.

Protein family/group databases

MEROPSiC44.001.

PTM databases

iPTMnetiQ06203.
PhosphoSitePlusiQ06203.

Polymorphism and mutation databases

BioMutaiPPAT.
DMDMi548638.

Proteomic databases

EPDiQ06203.
MaxQBiQ06203.
PaxDbiQ06203.
PeptideAtlasiQ06203.
PRIDEiQ06203.

Protocols and materials databases

DNASUi5471.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264220; ENSP00000264220; ENSG00000128059.
GeneIDi5471.
KEGGihsa:5471.
UCSCiuc003hbr.4. human.

Organism-specific databases

CTDi5471.
DisGeNETi5471.
GeneCardsiPPAT.
HGNCiHGNC:9238. PPAT.
HPAiHPA036091.
HPA036092.
MIMi172450. gene.
neXtProtiNX_Q06203.
OpenTargetsiENSG00000128059.
PharmGKBiPA33559.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0572. Eukaryota.
COG0034. LUCA.
GeneTreeiENSGT00390000003428.
HOGENOMiHOG000033688.
HOVERGENiHBG002589.
InParanoidiQ06203.
KOiK00764.
OMAiIRHFGVK.
OrthoDBiEOG091G06F7.
PhylomeDBiQ06203.
TreeFamiTF106370.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00124.
BioCyciMetaCyc:HS05157-MONOMER.
ZFISH:HS05157-MONOMER.
ReactomeiR-HSA-73817. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

GeneWikiiAmidophosphoribosyltransferase.
GenomeRNAii5471.
PROiQ06203.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000128059.
CleanExiHS_PPAT.
ExpressionAtlasiQ06203. baseline and differential.
GenevisibleiQ06203. HS.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF. 1 hit.
InterProiIPR017932. GATase_2_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005854. PurF.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFiPIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMiSSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01134. purF. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPUR1_HUMAN
AccessioniPrimary (citable) accession number: Q06203
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.