ID   PUR2_ARATH              Reviewed;         532 AA.
AC   P52420; O04505;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=Phosphoribosylamine--glycine ligase, chloroplastic;
DE            EC=6.3.4.13;
DE   AltName: Full=Glycinamide ribonucleotide synthetase;
DE            Short=GARS;
DE   AltName: Full=Phosphoribosylglycinamide synthetase;
DE   Flags: Precursor;
GN   Name=PUR2; OrderedLocusNames=At1g09830; ORFNames=F21M12.22;
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   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   [3]
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   [4]
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=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681,
CC         ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC       (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC       diphosphate: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA52778.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X74766; CAA52778.2; ALT_INIT; mRNA.
DR   EMBL; AC000132; AAB60737.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28500.1; -; Genomic_DNA.
DR   EMBL; AY050820; AAK92755.1; -; mRNA.
DR   EMBL; AY091422; AAM14361.1; -; mRNA.
DR   PIR; E86232; E86232.
DR   PIR; S37104; S37104.
DR   RefSeq; NP_172454.1; NM_100857.4.
DR   AlphaFoldDB; P52420; -.
DR   SMR; P52420; -.
DR   BioGRID; 22756; 6.
DR   STRING; 3702.P52420; -.
DR   PaxDb; 3702-AT1G09830-1; -.
DR   ProteomicsDB; 224868; -.
DR   EnsemblPlants; AT1G09830.1; AT1G09830.1; AT1G09830.
DR   GeneID; 837515; -.
DR   Gramene; AT1G09830.1; AT1G09830.1; AT1G09830.
DR   KEGG; ath:AT1G09830; -.
DR   Araport; AT1G09830; -.
DR   TAIR; AT1G09830; PUR2.
DR   eggNOG; KOG0237; Eukaryota.
DR   HOGENOM; CLU_027420_3_1_1; -.
DR   InParanoid; P52420; -.
DR   OMA; KATVCKY; -.
DR   OrthoDB; 729at2759; -.
DR   PhylomeDB; P52420; -.
DR   BioCyc; ARA:AT1G09830-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   PRO; PR:P52420; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P52420; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 1.
DR   HAMAP; MF_00138; GARS; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   InterPro; IPR000115; PRibGlycinamide_synth.
DR   InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR   InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR   InterPro; IPR020559; PRibGlycinamide_synth_CS.
DR   InterPro; IPR020562; PRibGlycinamide_synth_N.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   NCBIfam; TIGR00877; purD; 1.
DR   PANTHER; PTHR43472; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE; 1.
DR   PANTHER; PTHR43472:SF1; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01071; GARS_A; 1.
DR   Pfam; PF02843; GARS_C; 1.
DR   Pfam; PF02844; GARS_N; 1.
DR   SMART; SM01209; GARS_A; 1.
DR   SMART; SM01210; GARS_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00184; GARS; 1.
DR   Genevisible; P52420; AT.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; Ligase; Nucleotide-binding; Plastid;
KW   Purine biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..75
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000305"
FT   CHAIN           76..532
FT                   /note="Phosphoribosylamine--glycine ligase, chloroplastic"
FT                   /id="PRO_0000029875"
FT   DOMAIN          204..412
FT                   /note="ATP-grasp"
FT   CONFLICT        1..91
FT                   /note="MSSLCASNCYPSSSSINLFSNNNNPTKPFLLSLRFASSNSLPFVAPLKFSTT
FT                   NHVLSNSRFSSNRIQRRLFLLRCVSEESQPSLSIGNGGS -> LNPCLRWSESRVLYFD
FT                   SLPPCRRCVHLIAILHLLLSISSPTTTTQLNPFFSPSDSPPPILFHLLLLSNSLLPITS
FT                   LVTLVSLRTESKDAFFCSDAFQKNLSRLFLIG (in Ref. 1; CAA52778)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        377..380
FT                   /note="LPKL -> FLSF (in Ref. 1; CAA52778)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        511..532
FT                   /note="GFFRHDIGWRALRQKQVATKEE -> RFL (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   532 AA;  56473 MW;  30C81EAB7497152B CRC64;
     MSSLCASNCY PSSSSINLFS NNNNPTKPFL LSLRFASSNS LPFVAPLKFS TTNHVLSNSR
     FSSNRIQRRL FLLRCVSEES QPSLSIGNGG SEERVNVLVI GGGGREHALC HALKRSPSCD
     SVLCAPGNAG ISSSGDATCV PDLDISDSLA VISFCQKWNV GLVVVGPEVP LVAGLANDLV
     KAGILTFGPS SQAAALEGSK NFMKNLCHKY NIPTAKYKTF SDASAAKEYI QEQGAPIVIK
     ADGLAAGKGV TVAMELEEAF EAVDSMLVKG VFGSAGCQVV VEEFLEGEEA SFFALVDGEN
     AIPLESAQDH KRVGDGDTGP NTGGMGAYSP APVLTKELQD FVMESIIHPT VKGMAEEGCK
     FVGVLFAGLM IEKKSGLPKL IEFNVRFGDP ECQVLMMRLE SDLAKVLLAA CKGELSGVSL
     DWSKDSAMVV VMASNGYPGS YEKGSIIKNL EEAERVAPGV KVFHAGTGLD SEGNVVATGG
     RVLGVTAKGK DLEEARERAY SAVQQINWPG GFFRHDIGWR ALRQKQVATK EE
//