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Protein

Amidophosphoribosyltransferase

Gene

PPAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionAllosteric enzyme, Glycosyltransferase, Transferase
Biological processPurine biosynthesis
Ligand4Fe-4S, Iron, Iron-sulfur, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc: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

EuPathDBiHostDB:ENSG00000128059.8
HGNCiHGNC:9238 PPAT
MIMi172450 gene
neXtProtiNX_Q06203

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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, 5 interactors
STRINGi9606.ENSP00000264220

Structurei

3D structure databases

ProteinModelPortaliQ06203
SMRiQ06203
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

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

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

Family and domain databases

CDDicd00715 GPATase_N, 1 hit
cd06223 PRTases_typeI, 1 hit
HAMAPiMF_01931 PurF, 1 hit
InterProiView protein in InterPro
IPR017932 GATase_2_dom
IPR029055 Ntn_hydrolases_N
IPR000836 PRibTrfase_dom
IPR029057 PRTase-like
IPR005854 PurF
IPR035584 PurF_N
PfamiView protein in Pfam
PF00156 Pribosyltran, 1 hit
PIRSFiPIRSF000485 Amd_phspho_trans, 1 hit
SUPFAMiSSF53271 SSF53271, 1 hit
SSF56235 SSF56235, 1 hit
TIGRFAMsiTIGR01134 purF, 1 hit
PROSITEiView protein in PROSITE
PS51278 GATASE_TYPE_2, 1 hit
PS00103 PUR_PYR_PR_TRANSFER, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiPUR1_HUMAN
AccessioniPrimary (citable) accession number: Q06203
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: March 28, 2018
This is version 171 of the entry and version 1 of the sequence. See 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

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health