PUR3_SOYBN
ID PUR3_SOYBN Reviewed; 295 AA.
AC Q42805;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 AltName: Full=GMpurN;
DE Flags: Precursor;
GN Name=PUR3; Synonyms=PURN;
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Root nodule;
RX PubMed=8980527; DOI=10.1007/bf00020216;
RA Schnorr K.M., Laloue M., Hirel B.;
RT "Isolation of cDNAs encoding two purine biosynthetic enzymes of soybean and
RT expression of the corresponding transcripts in roots and root nodules.";
RL Plant Mol. Biol. 32:751-757(1996).
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 -!- TISSUE SPECIFICITY: Highly expressed in young and mature nodules but
CC weakly expressed in roots and leaves.
CC -!- SIMILARITY: Belongs to the GART family. {ECO:0000305}.
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DR EMBL; X96865; CAA65608.1; -; mRNA.
DR PIR; T07781; T07781.
DR AlphaFoldDB; Q42805; -.
DR SMR; Q42805; -.
DR PRIDE; Q42805; -.
DR InParanoid; Q42805; -.
DR UniPathway; UPA00074; UER00126.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR001555; GART_AS.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
DR PROSITE; PS00373; GART; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Plastid; Purine biosynthesis; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..295
FT /note="Phosphoribosylglycinamide formyltransferase,
FT chloroplastic"
FT /id="PRO_0000029877"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 96..98
FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT /ligand_id="ChEBI:CHEBI:143788"
FT /evidence="ECO:0000250"
FT BINDING 171..174
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT /ligand_id="ChEBI:CHEBI:143788"
FT /evidence="ECO:0000250"
FT SITE 230
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000250"
SQ SEQUENCE 295 AA; 32823 MW; 44908F208E95A752 CRC64;
MSVPSIPIVK QQFSPKFPRL PSSSLYPSSQ SQNLNVPSGA FHPISIVHKE VCSSSCKRIW
CSSSSSSTAE PKEGHEVRAQ VTVRRKKLGV FVSGGGTNFR AIHEATKRGS LHGDVLVLVT
NKSDCGGAEY ARNNGIPVIL YHISKDESNG SDLVDTLRKF EVDFILLAGY LNLYQWNDPS
LQKIYIQHSS ITSSSFWRQG IHGMKVHKAV IASGARFSGP TIHFVDEHYD TGRILAQRVV
PVQANDTVEE LAARVLKEEH QLYVEVVEAL CEERVVWRQD GVPLIQSKEN PNEFR
