PUR3_ARATH
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 03-AUG-2022, entry version 154.
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 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=(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; X74767; CAA52779.2; -; mRNA.
DR EMBL; AC004793; AAD21688.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31329.1; -; 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 STRING; 3702.AT1G31220.1; -.
DR PaxDb; P52422; -.
DR PRIDE; P52422; -.
DR ProteomicsDB; 226127; -.
DR EnsemblPlants; AT1G31220.1; AT1G31220.1; AT1G31220.
DR GeneID; 840010; -.
DR Gramene; AT1G31220.1; AT1G31220.1; AT1G31220.
DR KEGG; ath:AT1G31220; -.
DR Araport; AT1G31220; -.
DR TAIR; locus:2029554; AT1G31220.
DR eggNOG; KOG3076; Eukaryota.
DR HOGENOM; CLU_038395_4_0_1; -.
DR InParanoid; P52422; -.
DR OMA; CGGADYA; -.
DR OrthoDB; 1509844at2759; -.
DR PhylomeDB; P52422; -.
DR BioCyc; ARA:AT1G31220-MON; -.
DR UniPathway; UPA00074; UER00126.
DR PRO; PR:P52422; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P52422; baseline and differential.
DR Genevisible; P52422; AT.
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 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; 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="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
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
