ASE3_ARATH
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 03-AUG-2022, entry version 136.
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.AT4G38880.1; -.
DR MEROPS; C44.A02; -.
DR PaxDb; Q9T0J5; -.
DR PRIDE; Q9T0J5; -.
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; locus:2141811; AT4G38880.
DR eggNOG; KOG0572; Eukaryota.
DR HOGENOM; CLU_022389_3_1_1; -.
DR InParanoid; Q9T0J5; -.
DR OMA; PFIASCK; -.
DR OrthoDB; 400911at2759; -.
DR PhylomeDB; Q9T0J5; -.
DR BioCyc; ARA:AT4G38880-MON; -.
DR BRENDA; 2.4.2.14; 399.
DR UniPathway; UPA00074; UER00124.
DR PRO; PR:Q9T0J5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T0J5; baseline and differential.
DR Genevisible; Q9T0J5; AT.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IBA:GO_Central.
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 GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
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; -; 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 Pfam; PF13537; GATase_7; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01134; purF; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
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
