Reviewed, UniProtKB/Swiss-Prot P52422 (PUR3_ARATH)

Names and origin

Protein names

Recommended name:
    Phosphoribosylglycinamide formyltransferase, chloroplastic
    EC=2.1.2.2
Alternative name(s):
    5'-phosphoribosylglycinamide transformylase
    GAR transformylase
      Short name=GART

Gene names

Name:	PUR3
Ordered Locus Names:	At1g31220
ORF Names:	F28K20.18

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	292 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Subcellular location	Plastid › chloroplast.
Sequence similarities	Belongs to the GART family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast Inferred from direct assay. Source: TAIR
Molecular function	phosphoribosylglycinamide formyltransferase activity Ref.1 Inferred from genetic interaction. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 65	65	Chloroplast Potential
	Chain	66 – 292	227	Phosphoribosylglycinamide formyltransferase, chloroplastic		PRO_0000029876
Regions
	Region	88 – 90	3	5'-phosphoribosylglycinamide binding By similarity
	Region	167 – 170	4	10-formyltetrahydrofolate binding By similarity
Sites
	Active site	186	1	Proton donor By similarity
	Binding site	184	1	10-formyltetrahydrofolate By similarity
	Binding site	227	1	10-formyltetrahydrofolate; via amide nitrogen By similarity
	Binding site	256	1	5'-phosphoribosylglycinamide By similarity
	Site	227	1	Raises pKa of active site His By similarity

Sequences

	Sequence		Length	Mass (Da)
	P52422-1 [UniParc]. Last modified July 11, 2001. Version 2. Checksum: 880DBE443C7B493C	FASTA	292	32,170
	10 20 30 40 50 60 MESRVLFSSQ FNFPVNSPFK TRETSIAPLT PSRNVLSFSF RSPAERCAMR IVPLVKAASS 70 80 90 100 110 120 TPQIVAEVDG SSHEPRRKKL AVFVSGGGSN FRKIHEGCSD GSVNGDVVLL VTNKKDCGGA 130 140 150 160 170 180 EYARSNGIPV LVFPKAKREP SDGLSPSELV DVLRKYGVDF VLLAGYLKLI PVELVQAFPK 190 200 210 220 230 240 RILNIHPALL PAFGGKGLYG IKVHKAVLES GARYSGPTIH FVNEEYDTGR ILAQSAVRVI 250 260 270 280 290 ANDTPEELAK RVLHEEHKLY VEVVGAICEE RIKWREDGVP LIQNKQNPDE YY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of Arabidopsis thaliana cDNAs encoding three purine biosynthetic enzymes." Schnorr K.M., Nygaard P., Laloue M. Plant J. 6:113-121(1994) [PubMed: 7920700] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	Schnorr K.M. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X74767 mRNA. Translation: CAA52779.2. AC004793 Genomic DNA. Translation: AAD21688.1. BT003877 mRNA. Translation: AAO41926.1. BT006080 mRNA. Translation: AAP04065.1.
IPI	IPI00523064.
PIR	D86438. S37105.
RefSeq	NP_174407.1.
UniGene	At.48251
3D structure databases
HSSP	HSSP built from PDB template 1GRC based on UniProtKB P08179.
ModBase	Search...
Protein-protein interaction databases
STRING	P52422.
Proteomic databases
PRIDE	P52422.
Genome annotation databases
GeneID	840010.
GenomeReviews	Gene locus AT1G31220 in contig CT485782_GR.
KEGG	ath:AT1G31220.
NMPDR	fig|3702.1.peg.3464.
Organism-specific databases
TAIR	At1g31220.
Phylogenomic databases
OMA	RIHALEY.
Enzyme and pathway databases
BRENDA	2.1.2.2. 302.
Gene expression databases
ArrayExpress	P52422.
Genevestigator	P52422.
GermOnline	AT1G31220. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002376. Formyl_transf_N. IPR001555. GART_AS. IPR004607. PurN_trans. [Graphical view]
Gene3D	G3DSA:3.40.50.170. Formyl_transf_N. 1 hit.
Pfam	PF00551. Formyl_trans_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00639. PurN. 1 hit.
PROSITE	PS00373. GART. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUR3_ARATH

Accession

Primary (citable) accession number: P52422

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 11, 2001
Last modified:	November 3, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)