Reviewed, UniProtKB/Swiss-Prot P52419 (PUR1_VIGAC)

Names and origin

Protein names

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

Gene names

Name:

PUR1

Organism

Vigna aconitifolia (Mothbean)

Taxonomic identifier

3918 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Vigna

Protein attributes

Sequence length	485 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Subcellular location	Plastid › chloroplast.
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
Cellular component	Chloroplast Plastid
Domain	Glutamine amidotransferase Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
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 Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW amidophosphoribosyltransferase activity Inferred from electronic annotation. Source: EC 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
	Transit peptide	‹1 – 18	›18	Chloroplast Potential
	Chain	19 – 485	467	Amidophosphoribosyltransferase, chloroplastic		PRO_0000029290
Regions
	Domain	19 – 237	219	Glutamine amidotransferase type-2
Sites
	Active site	19	1	For GATase activity By similarity
	Metal binding	253	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	300	1	Magnesium By similarity
	Metal binding	362	1	Magnesium By similarity
	Metal binding	363	1	Magnesium By similarity
	Metal binding	399	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	450	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	453	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P52419-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: EE9CD20AE5BEDD82	FASTA	485	53,205
	10 20 30 40 50 60 KTTNTFASVN DDEKPREECG VVGIYGDPEA SRLCSLALHA LQHRGQEGAG IVAVHDNLFH 70 80 90 100 110 120 QVNGVGLVSD VFNEAKLSEL PGSCAIGHVR YSTAGHSKLV NVQPFVAGYR FGSVAVAHNG 130 140 150 160 170 180 NFVNYRSLRA KLEDNGSIFN TTSDTEVVLH LIATSKHRPF LLRVVDACEN LKGAYSLVFL 190 200 210 220 230 240 TEDKLVAVRD FGFRPLVMGR RKNGAVVFAS ETCALDLIDA TYEREVNPGE VVVVDHTGIQ 250 260 270 280 290 300 SLCLVTHQEP KQCIFEHIYF ALPNSVVFGR SVYESRRKFG EILATESPVE CDVVIAVPDS 310 320 330 340 350 360 GVVAALGYAA KAGVPFQQGL IRSHHVGRTF IEPSQKIRDF GVKLKLFPVR GVLEGKRVVV 370 380 390 400 410 420 VDDSIVRGTT SSKIVRLIKE AGAKEVHMRI ACPPIVASCY YGVDTPSKEE LISNRMDVEE 430 440 450 460 470 480 IRKFIGSDSL AFLPLDTLKS LLEDDAPNYC YACFSGKYPV QPENLNPTAS MSLTGTMFQW QFETY

References

[1]

"Control of de novo purine biosynthesis genes in ureide-producing legumes: induction of glutamine phosphoribosylpyrophosphate amidotransferase gene and characterization of its cDNA from soybean and Vigna." Kim J.H., Delauney A.J., Verma D.P.S. Plant J. 7:77-86(1995) [PubMed: 7894513] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Root nodule.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L23834 mRNA. Translation: AAA73944.1.
PIR	T10792.
3D structure databases
HSSP	HSSP built from PDB template 1AO0 based on UniProtKB P00497.
ModBase	Search...
Protein family/group databases
MEROPS	C44.001.
Enzyme and pathway databases
BRENDA	2.4.2.14. 18771.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR000583. GATase_2. IPR017932. GATase_II. 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_VIGAC

Accession

Primary (citable) accession number: P52419

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)