ID   PUR3_ARATH              Reviewed;         292 AA.
AC   P52422;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   02-SEP-2026, entry version 170.
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; OrderedLocusNames=At1g31220; ORFNames=F28K20.18;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=7920700; DOI=10.1046/j.1365-313x.1994.6010113.x;
RA   Schnorr K.M., Nygaard P., Laloue M.;
RT   "Molecular characterization of Arabidopsis thaliana cDNAs encoding three
RT   purine biosynthetic enzymes.";
RL   Plant J. 6:113-121(1994).
RN   [2]
RP   SEQUENCE REVISION.
RA   Schnorr K.M.;
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
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; X74767; CAA52779.2; -; mRNA.
DR   EMBL; AC004793; AAD21688.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31329.1; -; Genomic_DNA.
DR   EMBL; OZ408683; CAO7029285.1; -; Genomic_DNA.
DR   EMBL; BT003877; AAO41926.1; -; mRNA.
DR   EMBL; BT006080; AAP04065.1; -; mRNA.
DR   PIR; D86438; D86438.
DR   PIR; S37105; S37105.
DR   RefSeq; NP_174407.1; NM_102860.3.
DR   AlphaFoldDB; P52422; -.
DR   SMR; P52422; -.
DR   BioGRID; 25245; 1.
DR   FunCoup; P52422; 478.
DR   STRING; 3702.P52422; -.
DR   PaxDb; 3702-P52422; -.
DR   ProteomicsDB; 226127; -.
DR   GeneID; 840010; -.
DR   KEGG; ath:AT1G31220; -.
DR   Araport; AT1G31220; -.
DR   TAIR; AT1G31220; -.
DR   eggNOG; KOG3076; Eukaryota.
DR   HOGENOM; CLU_038395_4_0_1; -.
DR   InParanoid; P52422; -.
DR   OMA; CGGADYA; -.
DR   PhylomeDB; P52422; -.
DR   BioCyc; ARA:AT1G31220-MONOMER; -.
DR   UniPathway; UPA00074; UER00126.
DR   PRO; PR:P52422; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
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   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   SUPFAM; SSF53328; Formyltransferase; 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..65
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           66..292
FT                   /note="Phosphoribosylglycinamide formyltransferase,
FT                   chloroplastic"
FT                   /id="PRO_0000029876"
FT   ACT_SITE        186
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         88..90
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..170
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000250"
FT   SITE            227
FT                   /note="Raises pKa of active site His"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   292 AA;  32170 MW;  880DBE443C7B493C CRC64;
     MESRVLFSSQ FNFPVNSPFK TRETSIAPLT PSRNVLSFSF RSPAERCAMR IVPLVKAASS
     TPQIVAEVDG SSHEPRRKKL AVFVSGGGSN FRKIHEGCSD GSVNGDVVLL VTNKKDCGGA
     EYARSNGIPV LVFPKAKREP SDGLSPSELV DVLRKYGVDF VLLAGYLKLI PVELVQAFPK
     RILNIHPALL PAFGGKGLYG IKVHKAVLES GARYSGPTIH FVNEEYDTGR ILAQSAVRVI
     ANDTPEELAK RVLHEEHKLY VEVVGAICEE RIKWREDGVP LIQNKQNPDE YY
//