PUR3_VIGUN
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 03-AUG-2022, entry version 98.
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=(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-
CC formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide;
CC Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC ChEBI:CHEBI:57454, ChEBI:CHEBI:143788, ChEBI:CHEBI:147286;
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}.
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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 AlphaFoldDB; P52423; -.
DR SMR; P52423; -.
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 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 Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
DR TIGRFAMs; TIGR00639; PurN; 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="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250"
FT BINDING 187..190
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
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