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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

Pathway:iIMP 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 (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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei12 – 121NucleophilePROSITE-ProRule annotation
Metal bindingi280 – 2801Iron-sulfur (4Fe-4S)By similarity
Metal bindingi327 – 3271MagnesiumBy similarity
Metal bindingi389 – 3891MagnesiumBy similarity
Metal bindingi390 – 3901MagnesiumBy similarity
Metal bindingi426 – 4261Iron-sulfur (4Fe-4S)By similarity
Metal bindingi503 – 5031Iron-sulfur (4Fe-4S)By similarity
Metal bindingi506 – 5061Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • amidophosphoribosyltransferase activity Source: ProtInc
  • metal ion binding Source: UniProtKB-KW

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.
ReactomeiREACT_1776. 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
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:9238. PPAT.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33559.

Chemistry

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

Polymorphism and mutation databases

BioMutaiPPAT.
DMDMi548638.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1111CuratedPRO_0000029283Add
BLAST
Chaini12 – 517506AmidophosphoribosyltransferasePRO_0000029284Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ06203.
PaxDbiQ06203.
PeptideAtlasiQ06203.
PRIDEiQ06203.

PTM databases

PhosphoSiteiQ06203.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiQ06203.
CleanExiHS_PPAT.
ExpressionAtlasiQ06203. baseline and differential.
GenevisibleiQ06203. HS.

Organism-specific databases

HPAiHPA036091.
HPA036092.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi111467. 19 interactions.
IntActiQ06203. 2 interactions.
STRINGi9606.ENSP00000264220.

Structurei

3D structure databases

ProteinModelPortaliQ06203.
SMRiQ06203. Positions 12-515.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 261250Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG0034.
GeneTreeiENSGT00390000003428.
HOGENOMiHOG000033688.
HOVERGENiHBG002589.
InParanoidiQ06203.
KOiK00764.
OMAiIRHFGVK.
OrthoDBiEOG789C9W.
PhylomeDBiQ06203.
TreeFamiTF106370.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005854. PurF.
[Graphical view]
PfamiPF00310. GATase_2. 2 hits.
PF00156. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti369 – 3691V → I in AAC27345 (PubMed:8106516).Curated

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.3. 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.
SMRiQ06203. Positions 12-515.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111467. 19 interactions.
IntActiQ06203. 2 interactions.
STRINGi9606.ENSP00000264220.

Chemistry

ChEMBLiCHEMBL2362992.
DrugBankiDB00544. Fluorouracil.
DB00130. L-Glutamine.
DB01033. Mercaptopurine.
GuidetoPHARMACOLOGYi2761.

Protein family/group databases

MEROPSiC44.001.

PTM databases

PhosphoSiteiQ06203.

Polymorphism and mutation databases

BioMutaiPPAT.
DMDMi548638.

Proteomic databases

MaxQBiQ06203.
PaxDbiQ06203.
PeptideAtlasiQ06203.
PRIDEiQ06203.

Protocols and materials databases

DNASUi5471.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264220; ENSP00000264220; ENSG00000128059.
GeneIDi5471.
KEGGihsa:5471.
UCSCiuc003hbr.3. human.

Organism-specific databases

CTDi5471.
GeneCardsiGC04M057259.
HGNCiHGNC:9238. PPAT.
HPAiHPA036091.
HPA036092.
MIMi172450. gene.
neXtProtiNX_Q06203.
PharmGKBiPA33559.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0034.
GeneTreeiENSGT00390000003428.
HOGENOMiHOG000033688.
HOVERGENiHBG002589.
InParanoidiQ06203.
KOiK00764.
OMAiIRHFGVK.
OrthoDBiEOG789C9W.
PhylomeDBiQ06203.
TreeFamiTF106370.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00124.
BioCyciMetaCyc:HS05157-MONOMER.
ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

GeneWikiiAmidophosphoribosyltransferase.
GenomeRNAii5471.
NextBioi21182.
PROiQ06203.
SOURCEiSearch...

Gene expression databases

BgeeiQ06203.
CleanExiHS_PPAT.
ExpressionAtlasiQ06203. baseline and differential.
GenevisibleiQ06203. HS.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005854. PurF.
[Graphical view]
PfamiPF00310. GATase_2. 2 hits.
PF00156. 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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Hepatoma.
  2. "Two genes for de novo purine nucleotide synthesis on human chromosome 4 are closely linked and divergently transcribed."
    Brayton K.A., Chen Z., Zhou G., Nagy P.L., Gavalas A., Trent J.M., Deaven L.L., Dixon J.E., Zalkin H.
    J. Biol. Chem. 269:5313-5321(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: July 22, 2015
This is version 153 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

External Data

Dasty 3

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 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.