ID   ASE3_ARATH              Reviewed;         532 AA.
AC   Q9T0J5;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Amidophosphoribosyltransferase 3, chloroplastic;
DE            Short=AtATase3;
DE            Short=PRPP3;
DE            EC=2.4.2.14;
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase 3;
DE            Short=AtGPRAT3;
DE   Flags: Precursor;
GN   Name=ASE3; Synonyms=GPRAT3; OrderedLocusNames=At4g38880;
GN   ORFNames=F19H22.3, T9A14;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
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   [3]
RP   TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15266056; DOI=10.1104/pp.104.040956;
RA   Hung W.-F., Chen L.-J., Boldt R., Sun C.-W., Li H.-M.;
RT   "Characterization of Arabidopsis glutamine phosphoribosyl pyrophosphate
RT   amidotransferase-deficient mutants.";
RL   Plant Physiol. 135:1314-1323(2004).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=17616508; DOI=10.1104/pp.107.099705;
RA   Walsh T.A., Bauer T., Neal R., Merlo A.O., Schmitzer P.R., Hicks G.R.,
RA   Honma M., Matsumura W., Wolff K., Davies J.P.;
RT   "Chemical genetic identification of glutamine phosphoribosylpyrophosphate
RT   amidotransferase as the target for a novel bleaching herbicide in
RT   Arabidopsis.";
RL   Plant Physiol. 144:1292-1304(2007).
CC   -!- FUNCTION: Catalyzes the first committed step of 'de novo' purine
CC       biosynthesis from glutamine. {ECO:0000269|PubMed:17616508}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC         Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:58681; EC=2.4.2.14;
CC         Evidence={ECO:0000269|PubMed:17616508};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by the phenyltriazole acetic acid
CC       compound [5-(4-chlorophenyl)-1-isopropyl-1H-[1,2,4]triazol-3-yl]-acetic
CC       acid (DAS734), a bleaching herbicide. Repressed by AMP, ADP, ATP and
CC       GTP, and slightly by GMP. {ECO:0000269|PubMed:17616508}.
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 1/2.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed at low levels in leaves, and, to a
CC       lower extent, in cotyledons. {ECO:0000269|PubMed:15266056}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000305}.
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DR   EMBL; AL035656; CAB38622.1; -; Genomic_DNA.
DR   EMBL; AL161594; CAB80551.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86986.1; -; Genomic_DNA.
DR   PIR; T06087; T06087.
DR   RefSeq; NP_195599.1; NM_120048.1.
DR   AlphaFoldDB; Q9T0J5; -.
DR   SMR; Q9T0J5; -.
DR   STRING; 3702.Q9T0J5; -.
DR   MEROPS; C44.A02; -.
DR   PaxDb; 3702-AT4G38880-1; -.
DR   ProteomicsDB; 246676; -.
DR   EnsemblPlants; AT4G38880.1; AT4G38880.1; AT4G38880.
DR   GeneID; 830043; -.
DR   Gramene; AT4G38880.1; AT4G38880.1; AT4G38880.
DR   KEGG; ath:AT4G38880; -.
DR   Araport; AT4G38880; -.
DR   TAIR; AT4G38880; ASE3.
DR   eggNOG; KOG0572; Eukaryota.
DR   HOGENOM; CLU_022389_3_1_1; -.
DR   InParanoid; Q9T0J5; -.
DR   OMA; PFIASCK; -.
DR   OrthoDB; 4975at2759; -.
DR   PhylomeDB; Q9T0J5; -.
DR   BioCyc; ARA:AT4G38880-MONOMER; -.
DR   BRENDA; 2.4.2.14; 399.
DR   SABIO-RK; Q9T0J5; -.
DR   UniPathway; UPA00074; UER00124.
DR   PRO; PR:Q9T0J5; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9T0J5; baseline and differential.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   CDD; cd00715; GPATase_N; 1.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   HAMAP; MF_01931; PurF; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR005854; PurF.
DR   InterPro; IPR035584; PurF_N.
DR   NCBIfam; TIGR01134; purF; 1.
DR   PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11907:SF24; AMIDOPHOSPHORIBOSYLTRANSFERASE 3, CHLOROPLASTIC; 1.
DR   Pfam; PF13537; GATase_7; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
DR   Genevisible; Q9T0J5; AT.
PE   1: Evidence at protein level;
KW   Chloroplast; Glutamine amidotransferase; Glycosyltransferase; Iron;
KW   Iron-sulfur; Magnesium; Metal-binding; Plastid; Purine biosynthesis;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..59
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           60..532
FT                   /note="Amidophosphoribosyltransferase 3, chloroplastic"
FT                   /id="PRO_0000420283"
FT   DOMAIN          77..296
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   ACT_SITE        77
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   BINDING         313
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         459
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         511
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         514
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   532 AA;  58041 MW;  C1B67B430D36A775 CRC64;
     MAFSVEEISS ILPNSLSANP RNVSQNTISP SFFKPSLKPY ASKTLISLSC RRSLSPVFSA
     GTYVTNVDED DKLHEECGVV GIHGDPEASR LSYLALHALQ HRGQEGAGIV AANQNGLESI
     TGVGLVSDVF TESKLNNLPG DIAIGHVRYS TSGASMLKNV QPFIASCKLG SLAVAHNGNF
     VNYKQLKTKL EEMGSIFITS SDTELVLHLI AKSKAKTFLL RVIDACEKLR GAYSMVFVFE
     DKLIAVRDPF GFRPLVMGRR SNGAVVFASE TCALDLIDAT YEREVCPGEI VVVDRNHGDS
     SMFMISHPEQ KQCVFEHGYF SQPNSIVFGR SVYETRRMYG EILATVAPVD CDVVIAVPDS
     GTVAALGYAA KAGVPFQIGL LRSHYAKRTF IEPTQEIRDF AVKVKLSPVR AVLEGKRVVV
     VDDSIVRGTT SLKIVRMLRD AGAKEVHMRI ALPPMIASCY YGVDTPRSQE LISSKMSVEA
     IQKHINCDSL AFLPLDSLKG VYGPVESHRY CYACFTGKYP VTKTESEEAD AS
//