Reviewed, UniProtKB/Swiss-Prot Q06203 (PUR1_HUMAN)

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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
PTM	Acetylation
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from Experiment. Source: Reactome glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW nucleoside metabolic process Inferred from electronic annotation. Source: InterPro purine base biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW amidophosphoribosyltransferase activity Ref.2 Traceable author statement. Source: ProtInc iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium 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
Amino acid modifications
	Modified residue	81	1	N6-acetyllysine Ref.5
Experimental info
	Sequence conflict	369	1	V → I in AAC27345. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q06203-1 [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: 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.
IPI	IPI00029534.
PIR	A53342.
RefSeq	NP_002694.3.
UniGene	Hs.331420 Hs.708542
3D structure databases
SMR	Q06203. Positions 12-515.
ModBase	Search...
Protein-protein interaction databases
STRING	Q06203.
Protein family/group databases
MEROPS	C44.001.
Proteomic databases
PeptideAtlas	Q06203.
PRIDE	Q06203.
Genome annotation databases
Ensembl	ENST00000264220; ENSP00000264220; ENSG00000128059; Homo sapiens. [Genome view]
GeneID	5471.
KEGG	hsa:5471.
NMPDR	fig|9606.3.peg.24134.
UCSC	uc003hbr.1. human.
Organism-specific databases
CTD	5471.
GeneCards	GC04M056954.
H-InvDB	HIX0004233.
HGNC	HGNC:9238. PPAT.
MIM	172450. gene.
PharmGKB	PA33559.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15460.
HOGENOM	HBG392416.
HOVERGEN	Q06203.
InParanoid	Q06203.
OMA	SSETEGW.
OrthoDB	EOG966Z6C.
PhylomeDB	Q06203.
Enzyme and pathway databases
BRENDA	2.4.2.14. 247.
Reactome	REACT_1698. Metabolism of nucleotides.
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. IPR000583. GATase_2. IPR017932. GATase_II. IPR000836. PRibTrfase. [Graphical view]
PANTHER	PTHR11907. Amd_phspho_trans. 1 hit.
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 Resources
DrugBank	DB00130. L-Glutamine. DB00352. Thioguanine.
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:	February 9, 2010
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.