Reviewed, UniProtKB/Swiss-Prot P41390 (PUR1_SCHPO)

Names and origin

Protein names

Recommended name:
    Amidophosphoribosyltransferase
      Short name=ATase
    EC=2.4.2.14
Alternative name(s):
    Glutamine phosphoribosylpyrophosphate amidotransferase

Gene names

Name:	ade4
ORF Names:	SPAC4D7.08c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	533 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 + H(2)O.
Cofactor	Binds 1 magnesium ion per subunit.
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.
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	Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	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 purine nucleotide biosynthetic process Ref.1 Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	amidophosphoribosyltransferase activity Ref.1 Inferred from electronic annotation. Source: InterPro 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
	Chain	1 – 533	533	Amidophosphoribosyltransferase		PRO_0000139646
Regions
	Domain	2 – 238	237	Glutamine amidotransferase type-2
Sites
	Active site	2	1	For GATase activity By similarity
	Metal binding	383	1	Magnesium By similarity
	Metal binding	384	1	Magnesium By similarity
Amino acid modifications
	Modified residue	506	1	Phosphoserine

Sequences

	Sequence		Length	Mass (Da)
	P41390-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 53C7C99F30A68B57	FASTA	533	59,832
	10 20 30 40 50 60 MCGILALMLA DPHQQACPEI YEGLYSLQHR GQDAAGIVTA GNKGRLYQCK GSGMVADVFS 70 80 90 100 110 120 QHQLRQLVGS MGIGHLRYPT AGSCAHSEAQ PFYVNSPYGL VLGHNGNLIN GPELRRFLDT 130 140 150 160 170 180 EAHRHVNTGS DSELLLNIFA YELQRLDKFR INENDIFEAL RNVYDRVNGG YACVAMIAGL 190 200 210 220 230 240 GVLGFRDPNG IRPLVIGERD TPEGKDYMLA SESVVLTQFG YRTFRDIRPG ECVFIRRSNR 250 260 270 280 290 300 EDILAGFRGP RLFSRQILPC LRFTPDIFEY VYFARPDSVI DGLSVYQSRL NMGEKLAHTI 310 320 330 340 350 360 MKRFGPDYME KIDAVIPVPD SARTSALALA QTAQLPYVEA FIKNRYIGRT FIMPGQQIRR 370 380 390 400 410 420 KSVRRKLNVQ PQEFFDKNVL IVDDSIVRGT TSREIVQMAR ESGAKNVYLA SCAPMITHPH 430 440 450 460 470 480 VYGIDLADCK DLIAYGKTED EVAEAISADG VIYQTLEDLL DSCRTAELTE FEVGLFTGEY 490 500 510 520 530 TTGASKEYLV HLEQMRIANN RARKHSFAED EEREAPEDIS LHNTHSDVTF DFV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The ade4 gene of Schizosaccharomyces pombe: cloning, sequence and regulation." Ludin K.M., Hilti N., Schweingruber M.E. Curr. Genet. 25:465-468(1994) [PubMed: 8082193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X72293 Genomic DNA. Translation: CAA51034.1. CU329670 Genomic DNA. Translation: CAB11280.1.
PIR	S43526.
RefSeq	NP_594961.1.
3D structure databases
HSSP	HSSP built from PDB template 1ECB based on UniProtKB P00496.
ModBase	Search...
Protein family/group databases
MEROPS	C44.971.
Genome annotation databases
GeneID	2543626.
KEGG	spo:SPAC4D7.08c.
NMPDR	fig|4896.1.peg.4931.
Organism-specific databases
GeneDB_Spombe	SPAC4D7.08c.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003021-MON.
Gene expression databases
ArrayExpress	P41390.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR000583. GATase_2. IPR002375. Pr/py_Pribosyl_transf_CS. IPR000836. PRibTrfase. [Graphical view]
PANTHER	PTHR11907. Amd_phspho_trans. 1 hit.
Pfam	PF00310. GATase_2. 1 hit. 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...

Entry information

Entry name

PUR1_SCHPO

Accession

Primary (citable) accession number: P41390

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 25, 2008
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)