ID PUR3_VIGUN Reviewed; 312 AA. AC P52423; Q9XGS3; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 08-DEC-2000, sequence version 2. DT 09-APR-2025, entry version 107. DE RecName: Full=Phosphoribosylglycinamide formyltransferase, chloroplastic; DE EC=2.1.2.2; DE AltName: Full=5'-phosphoribosylglycinamide transformylase; DE AltName: Full=GAR transformylase; DE Short=GART; DE Flags: Precursor; GN Name=PUR3; OS Vigna unguiculata (Cowpea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna. OX NCBI_TaxID=3917; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Vita 3; TISSUE=Root nodule; RA Hall D.J., Bussell J.D., Mann A.J., Goggin D.E., Atkins C.A., Smith P.M.C.; RT "Vupur3 mRNA from cowpea nodules encoding glycinamide ribonucleotide RT transformylase."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(1)-(5-phospho-beta-D-ribosyl)glycinamide + (6R)-10- CC formyltetrahydrofolate = N(2)-formyl-N(1)-(5-phospho-beta-D- CC ribosyl)glycinamide + (6S)-5,6,7,8-tetrahydrofolate + H(+); CC Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, CC ChEBI:CHEBI:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:195366; CC EC=2.1.2.2; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)- CC formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D- CC ribosyl)glycinamide (10-formyl THF route): step 1/1. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. CC -!- SIMILARITY: Belongs to the GART family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U30875; AAA75367.2; -; mRNA. DR EMBL; AF160196; AAD45353.2; -; Genomic_DNA. DR EMBL; AY189137; AAO25114.1; -; mRNA. DR EMBL; AY189138; AAO25115.1; -; mRNA. DR PIR; T11574; T11574. DR RefSeq; NP_001363005.1; NM_001376076.1. DR AlphaFoldDB; P52423; -. DR SMR; P52423; -. DR EnsemblPlants; Vigun01g091700.1.v1.2; Vigun01g091700.1.v1.2; Vigun01g091700.v1.2. DR EnsemblPlants; Vigun01g091700.10.v1.2; Vigun01g091700.10.v1.2; Vigun01g091700.v1.2. DR EnsemblPlants; Vigun01g091700.2.v1.2; Vigun01g091700.2.v1.2; Vigun01g091700.v1.2. DR EnsemblPlants; Vigun01g091700.3.v1.2; Vigun01g091700.3.v1.2; Vigun01g091700.v1.2. DR EnsemblPlants; Vigun01g091700.4.v1.2; Vigun01g091700.4.v1.2; Vigun01g091700.v1.2. DR EnsemblPlants; Vigun01g091700.5.v1.2; Vigun01g091700.5.v1.2; Vigun01g091700.v1.2. DR EnsemblPlants; Vigun01g091700.6.v1.2; Vigun01g091700.6.v1.2; Vigun01g091700.v1.2. DR EnsemblPlants; Vigun01g091700.7.v1.2; Vigun01g091700.7.v1.2; Vigun01g091700.v1.2. DR EnsemblPlants; Vigun01g091700.8.v1.2; Vigun01g091700.8.v1.2; Vigun01g091700.v1.2. DR EnsemblPlants; Vigun01g091700.9.v1.2; Vigun01g091700.9.v1.2; Vigun01g091700.v1.2. DR GeneID; 114188452; -. DR Gramene; Vigun01g091700.1.v1.2; Vigun01g091700.1.v1.2; Vigun01g091700.v1.2. DR Gramene; Vigun01g091700.10.v1.2; Vigun01g091700.10.v1.2; Vigun01g091700.v1.2. DR Gramene; Vigun01g091700.2.v1.2; Vigun01g091700.2.v1.2; Vigun01g091700.v1.2. DR Gramene; Vigun01g091700.3.v1.2; Vigun01g091700.3.v1.2; Vigun01g091700.v1.2. DR Gramene; Vigun01g091700.4.v1.2; Vigun01g091700.4.v1.2; Vigun01g091700.v1.2. DR Gramene; Vigun01g091700.5.v1.2; Vigun01g091700.5.v1.2; Vigun01g091700.v1.2. DR Gramene; Vigun01g091700.6.v1.2; Vigun01g091700.6.v1.2; Vigun01g091700.v1.2. DR Gramene; Vigun01g091700.7.v1.2; Vigun01g091700.7.v1.2; Vigun01g091700.v1.2. DR Gramene; Vigun01g091700.8.v1.2; Vigun01g091700.8.v1.2; Vigun01g091700.v1.2. DR Gramene; Vigun01g091700.9.v1.2; Vigun01g091700.9.v1.2; Vigun01g091700.v1.2. DR OrthoDB; 2018833at2759; -. DR UniPathway; UPA00074; UER00126. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd08645; FMT_core_GART; 1. DR FunFam; 3.40.50.170:FF:000011; phosphoribosylglycinamide formyltransferase, chloroplastic; 1. DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1. DR HAMAP; MF_01930; PurN; 1. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR036477; Formyl_transf_N_sf. DR InterPro; IPR004607; GART. DR InterPro; IPR001555; GART_AS. DR NCBIfam; TIGR00639; PurN; 1. DR PANTHER; PTHR43369; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1. DR PANTHER; PTHR43369:SF2; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1. DR Pfam; PF00551; Formyl_trans_N; 1. DR PIRSF; PIRSF036480; FormyFH4_hydr; 1. DR SUPFAM; SSF53328; Formyltransferase; 1. DR PROSITE; PS00373; GART; 1. PE 2: Evidence at transcript level; KW Chloroplast; Plastid; Purine biosynthesis; Transferase; Transit peptide. FT TRANSIT 1..73 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 74..312 FT /note="Phosphoribosylglycinamide formyltransferase, FT chloroplastic" FT /id="PRO_0000029878" FT ACT_SITE 206 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 109..111 FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide" FT /ligand_id="ChEBI:CHEBI:143788" FT /evidence="ECO:0000250" FT BINDING 162 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000250" FT BINDING 187..190 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000250" FT BINDING 204 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000250" FT BINDING 247 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000250" FT BINDING 276 FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide" FT /ligand_id="ChEBI:CHEBI:143788" FT /evidence="ECO:0000250" FT SITE 247 FT /note="Raises pKa of active site His" FT /evidence="ECO:0000250" SQ SEQUENCE 312 AA; 34583 MW; 51196B04E3D1385D CRC64; MEAQQIISRF CPKSSLAPSI PMVKQPFSLN FPPLHSLSSY PFLQSQNLGF PTGALHAISF VHKEVCSSSW RIWCSKSSSS TAEPEEDHEV RAQVTVRRKK LAVFVSGGGS NFRSIHEASK KGSLHGDVTV LVTNKSECGG AQYARNNGIP VILFPKAKDE PKGLSPCDLV DTLRKFEVDF VLLAGYLKLI PVELIRAFER SIFNIHPSLL PAFGGKGYYG MKVHKAVIAS GARFSGPTIH FVDEHYDTGR ILAQRVVPVL ANDTAEELAA RVLNEEHQLY VEVVEALCEE RIVWRKDGVP LIQSRENPNE FL //