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Reviewed, UniProtKB/Swiss-Prot Q06203 (PUR1_HUMAN)

Last modified February 9, 2010. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete 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.

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 residue811N6-acetyllysine Ref.5

Experimental info

Sequence conflict3691V → I in AAC27345. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q06203-1 [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: 8380692] [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: 8106516] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle.
[4]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, MASS SPECTROMETRY.
+Additional computationally mapped references.

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.
IPIIPI00029534.
PIRA53342.
RefSeqNP_002694.3.
UniGeneHs.331420
Hs.708542

3D structure databases

SMRQ06203. Positions 12-515.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ06203.

Protein family/group databases

MEROPSC44.001.

Proteomic databases

PeptideAtlasQ06203.
PRIDEQ06203.

Genome annotation databases

EnsemblENST00000264220; ENSP00000264220; ENSG00000128059; Homo sapiens. [Genome view]
GeneID5471.
KEGGhsa:5471.
NMPDRfig|9606.3.peg.24134.
UCSCuc003hbr.1. human.

Organism-specific databases

CTD5471.
GeneCardsGC04M056954.
H-InvDBHIX0004233.
HGNCHGNC:9238. PPAT.
MIM172450. gene.
PharmGKBPA33559.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG15460.
HOGENOMHBG392416.
HOVERGENQ06203.
InParanoidQ06203.
OMASSETEGW.
OrthoDBEOG966Z6C.
PhylomeDBQ06203.

Enzyme and pathway databases

BRENDA2.4.2.14. 247.
ReactomeREACT_1698. Metabolism of nucleotides.

Gene expression databases

ArrayExpressQ06203.
BgeeQ06203.
CleanExHS_PPAT.
GenevestigatorQ06203.
GermOnlineENSG00000128059. Homo sapiens.

Family and domain databases

InterProIPR005854. Amd_phspho_trans.
IPR000583. GATase_2.
IPR017932. GATase_II.
IPR000836. PRibTrfase.
[Graphical view]
PANTHERPTHR11907. Amd_phspho_trans. 1 hit.
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 Resources

DrugBankDB00130. L-Glutamine.
DB00352. Thioguanine.
NextBio21182.
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: February 9, 2010
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 4

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

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents