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Q06203 (PUR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amidophosphoribosyltransferase

Short name=ATase
EC=2.4.2.14
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase
Short name=GPAT
Gene names
Name:PPAT
Synonyms:GPAT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Binds 1 4Fe-4S cluster per subunit By similarity.

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.

Subunit structure

Homotetramer.

Tissue specificity

Ubiquitously expressed.

Sequence similarities

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.

Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
   Biological processPurine biosynthesis
   DomainGlutamine amidotransferase
   Ligand4Fe-4S
Iron
Iron-sulfur
Magnesium
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

cellular response to drug

Inferred from electronic annotation. Source: Ensembl

cellular response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

glutamine catabolic process

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from electronic annotation. Source: Ensembl

lactation

Inferred from electronic annotation. Source: Ensembl

maternal process involved in female pregnancy

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

nucleoside metabolic process

Inferred from electronic annotation. Source: InterPro

organ regeneration

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

purine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

purine nucleobase metabolic process

Traceable author statement. Source: Reactome

purine nucleotide biosynthetic process

Traceable author statement Ref.2. Source: ProtInc

purine ribonucleoside monophosphate biosynthetic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

amidophosphoribosyltransferase activity

Traceable author statement Ref.2. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1111 Probable
PRO_0000029283
Chain12 – 517506Amidophosphoribosyltransferase
PRO_0000029284

Regions

Domain12 – 261250Glutamine amidotransferase type-2

Sites

Active site121For GATase activity By similarity
Metal binding2801Iron-sulfur (4Fe-4S) By similarity
Metal binding3271Magnesium By similarity
Metal binding3891Magnesium By similarity
Metal binding3901Magnesium By similarity
Metal binding4261Iron-sulfur (4Fe-4S) By similarity
Metal binding5031Iron-sulfur (4Fe-4S) By similarity
Metal binding5061Iron-sulfur (4Fe-4S) By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5

Experimental info

Sequence conflict3691V → I in AAC27345. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q06203 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: D3F2A354C36B29D9

FASTA51757,399
        10         20         30         40         50         60 
MELEELGIRE ECGVFGCIAS GEWPTQLDVP HVITLGLVGL QHRGQESAGI VTSDGSSVPT 

        70         80         90        100        110        120 
FKSHKGMGLV NHVFTEDNLK KLYVSNLGIG HTRYATTGKC ELENCQPFVV ETLHGKIAVA 

       130        140        150        160        170        180 
HNGELVNAAR LRKKLLRHGI GLSTSSDSEM ITQLLAYTPP QEQDDTPDWV ARIKNLMKEA 

       190        200        210        220        230        240 
PTAYSLLIMH RDVIYAVRDP YGNRPLCIGR LIPVSDINDK EKKTSETEGW VVSSESCSFL 

       250        260        270        280        290        300 
SIGARYYREV LPGEIVEISR HNVQTLDIIS RSEGNPVAFC IFEYVYFARP DSMFEDQMVY 

       310        320        330        340        350        360 
TVRYRCGQQL AIEAPVDADL VSTVPESATP AALAYAGKCG LPYVEVLCKN RYVGRTFIQP 

       370        380        390        400        410        420 
NMRLRQLGVA KKFGVLSDNF KGKRIVLVDD SIVRGNTISP IIKLLKESGA KEVHIRVASP 

       430        440        450        460        470        480 
PIKYPCFMGI NIPTKEELIA NKPEFDHLAE YLGANSVVYL SVEGLVSSVQ EGIKFKKQKE 

       490        500        510 
KKHDIMIQEN GNGLECFEKS GHCTACLTGK YPVELEW 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of human amidophosphoribosyltransferase."
Iwahana H., Oka J., Mizusawa N., Kudo E., Ii S., Yoshimoto K., Holmes E.W., Itakura M.
Biochem. Biophys. Res. Commun. 190:192-200(1993) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13757 mRNA. Translation: BAA02903.1.
U00238 mRNA. Translation: AAC27345.1.
U00239 Genomic DNA. No translation available.
BC004200 mRNA. Translation: AAH04200.1.
PIRA53342.
RefSeqNP_002694.3. NM_002703.4.
UniGeneHs.331420.

3D structure databases

ProteinModelPortalQ06203.
SMRQ06203. Positions 12-515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111467. 19 interactions.
IntActQ06203. 2 interactions.
STRING9606.ENSP00000264220.

Chemistry

ChEMBLCHEMBL2362992.
DrugBankDB00130. L-Glutamine.
DB00352. Thioguanine.

Protein family/group databases

MEROPSC44.001.

PTM databases

PhosphoSiteQ06203.

Polymorphism databases

DMDM548638.

Proteomic databases

PaxDbQ06203.
PeptideAtlasQ06203.
PRIDEQ06203.

Protocols and materials databases

DNASU5471.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264220; ENSP00000264220; ENSG00000128059.
GeneID5471.
KEGGhsa:5471.
UCSCuc003hbr.3. human.

Organism-specific databases

CTD5471.
GeneCardsGC04M057259.
HGNCHGNC:9238. PPAT.
HPAHPA036091.
HPA036092.
MIM172450. gene.
neXtProtNX_Q06203.
PharmGKBPA33559.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0034.
HOGENOMHOG000033688.
HOVERGENHBG002589.
InParanoidQ06203.
KOK00764.
OMADSMFEDQ.
OrthoDBEOG789C9W.
PhylomeDBQ06203.
TreeFamTF106370.

Enzyme and pathway databases

BioCycMetaCyc:HS05157-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00074; UER00124.

Gene expression databases

ArrayExpressQ06203.
BgeeQ06203.
CleanExHS_PPAT.
GenevestigatorQ06203.

Family and domain databases

InterProIPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR000836. PRibTrfase_dom.
[Graphical view]
PfamPF00310. GATase_2. 2 hits.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFPIRSF000485. Amd_phspho_trans. 1 hit.
TIGRFAMsTIGR01134. purF. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAmidophosphoribosyltransferase.
GenomeRNAi5471.
NextBio21182.
PROQ06203.
SOURCESearch...

Entry information

Entry namePUR1_HUMAN
AccessionPrimary (citable) accession number: Q06203
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM