Q06203 (PUR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	517 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Purine biosynthesis
Domain	Glutamine amidotransferase
Ligand	4Fe-4S Iron Iron-sulfur Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
Technical term	Allosteric 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: Compara cellular response to drug Inferred from electronic annotation. Source: Compara cellular response to insulin stimulus Inferred from electronic annotation. Source: Compara glutamine catabolic process Inferred from electronic annotation. Source: Compara kidney development Inferred from electronic annotation. Source: Compara lactation Inferred from electronic annotation. Source: Compara maternal process involved in female pregnancy Inferred from electronic annotation. Source: Compara nucleoside metabolic process Inferred from electronic annotation. Source: InterPro organ regeneration Inferred from electronic annotation. Source: Compara protein homotetramerization Inferred from electronic annotation. Source: Compara 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
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	4 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 11	11	Probable		PRO_0000029283
	Chain	12 – 517	506	Amidophosphoribosyltransferase		PRO_0000029284
Regions
	Domain	12 – 261	250	Glutamine amidotransferase type-2
Sites
	Active site	12	1	For GATase activity By similarity
	Metal binding	280	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	327	1	Magnesium By similarity
	Metal binding	389	1	Magnesium By similarity
	Metal binding	390	1	Magnesium By similarity
	Metal binding	426	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	503	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	506	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Sequence conflict	369	1	V → I in AAC27345. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q06203 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: D3F2A354C36B29D9	FASTA	517	57,399
	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

References

	« Hide 'large scale' referencesShow '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].

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.
IPI	IPI00029534.
PIR	A53342.
RefSeq	NP_002694.3. NM_002703.4.
UniGene	Hs.331420.
3D structure databases
ProteinModelPortal	Q06203.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q06203. 2 interactions.
STRING	9606.ENSP00000264220.
Protein family/group databases
MEROPS	C44.001.
PTM databases
PhosphoSite	Q06203.
Polymorphism databases
DMDM	548638.
Proteomic databases
PaxDb	Q06203.
PeptideAtlas	Q06203.
PRIDE	Q06203.
Protocols and materials databases
DNASU	5471.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264220; ENSP00000264220; ENSG00000128059.
GeneID	5471.
KEGG	hsa:5471.
UCSC	uc003hbr.3. human.
Organism-specific databases
CTD	5471.
GeneCards	GC04M057259.
HGNC	HGNC:9238. PPAT.
HPA	HPA036092.
MIM	172450. gene.
neXtProt	NX_Q06203.
PharmGKB	PA33559.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0034.
HOGENOM	HOG000033688.
HOVERGEN	HBG002589.
InParanoid	Q06203.
KO	K00764.
OMA	GIPFELG.
OrthoDB	EOG47M1XN.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00074; UER00124.
Gene expression databases
ArrayExpress	Q06203.
Bgee	Q06203.
CleanEx	HS_PPAT.
Genevestigator	Q06203.
GermOnline	ENSG00000128059. Homo sapiens.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR000836. PRibTrfase_dom. [Graphical view]
Pfam	PF00310. GATase_2. 2 hits. PF00156. Pribosyltran. 1 hit. [Graphical view]
PIRSF	PIRSF000485. Amd_phspho_trans. 1 hit.
TIGRFAMs	TIGR01134. purF. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. PS00103. PUR_PYR_PR_TRANSFER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00130. L-Glutamine. DB00352. Thioguanine.
GenomeRNAi	5471.
NextBio	21182.
SOURCE	Search...

Entry information

Entry name

PUR1_HUMAN

Accession

Primary (citable) accession number: Q06203

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.