ASE1_ARATH
ID ASE1_ARATH Reviewed; 566 AA.
AC Q9SI61; Q38999;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Amidophosphoribosyltransferase 1, chloroplastic;
DE Short=AtATase1;
DE Short=PRPP1;
DE EC=2.4.2.14;
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase 1;
DE Short=AtGPRAT1;
DE Flags: Precursor;
GN Name=ASE1; Synonyms=GPRAT1; OrderedLocusNames=At2g16570; ORFNames=F1P15;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta; TISSUE=Flower, and Root;
RX PubMed=7948903; DOI=10.1007/bf00039565;
RA Ito T., Shiraishi H., Okada K., Shimura Y.;
RT "Two amidophosphoribosyltransferase genes of Arabidopsis thaliana expressed
RT in different organs.";
RL Plant Mol. Biol. 26:529-533(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GENE FAMILY, AND
RP 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).
CC -!- FUNCTION: Catalyzes the first committed step of 'de novo' purine
CC biosynthesis from glutamine. Involved in plastid biogenesis and cell
CC division. {ECO:0000269|PubMed:15266056}.
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 -!- 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 -!- 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
CC {ECO:0000269|PubMed:15266056}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and roots. Also present in
CC leaves, and, to a lower extent, in cotyledons.
CC {ECO:0000269|PubMed:15266056, ECO:0000269|PubMed:7948903}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06023.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D28868; BAA06023.1; ALT_FRAME; mRNA.
DR EMBL; AC007195; AAD26498.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06510.1; -; Genomic_DNA.
DR PIR; E84541; E84541.
DR PIR; S52622; S52622.
DR RefSeq; NP_179247.1; NM_127208.2.
DR AlphaFoldDB; Q9SI61; -.
DR SMR; Q9SI61; -.
DR BioGRID; 1514; 2.
DR IntAct; Q9SI61; 2.
DR STRING; 3702.AT2G16570.1; -.
DR MEROPS; C44.A01; -.
DR SwissPalm; Q9SI61; -.
DR PaxDb; Q9SI61; -.
DR PRIDE; Q9SI61; -.
DR ProteomicsDB; 246498; -.
DR EnsemblPlants; AT2G16570.1; AT2G16570.1; AT2G16570.
DR GeneID; 816156; -.
DR Gramene; AT2G16570.1; AT2G16570.1; AT2G16570.
DR KEGG; ath:AT2G16570; -.
DR Araport; AT2G16570; -.
DR TAIR; locus:2045081; AT2G16570.
DR eggNOG; KOG0572; Eukaryota.
DR HOGENOM; CLU_022389_3_3_1; -.
DR InParanoid; Q9SI61; -.
DR OMA; ENAQPTF; -.
DR OrthoDB; 400911at2759; -.
DR PhylomeDB; Q9SI61; -.
DR BioCyc; ARA:AT2G16570-MON; -.
DR BRENDA; 2.4.2.14; 399.
DR UniPathway; UPA00074; UER00124.
DR PRO; PR:Q9SI61; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SI61; baseline and differential.
DR Genevisible; Q9SI61; AT.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009532; C:plastid stroma; IDA:UniProtKB.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; ISS:TAIR.
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; ISS:TAIR.
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 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 2: Evidence at transcript 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..58
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 59..566
FT /note="Amidophosphoribosyltransferase 1, chloroplastic"
FT /id="PRO_0000420281"
FT DOMAIN 91..311
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT BINDING 327
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 524
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 527
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT CONFLICT 74
FT /note="T -> A (in Ref. 1; BAA06023)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="C -> F (in Ref. 1; BAA06023)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="G -> A (in Ref. 1; BAA06023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 566 AA; 61842 MW; 887827A9FEB901E0 CRC64;
MAATTSFSSS LSLITKPNNS SYTNQPLPLF PKPFLKPPHL SLLPSPLSSP PPSLIHGVSS
YFSSPSPSED NSHTPFDYHN DEDDEKPREE CGVVGIYGDP EASRLCYLAL HALQHRGQEG
AGIVTVSPEK VLQTITGVGL VSEVFNESKL DQLPGEFAIG HVRYSTAGAS MLKNVQPFVA
GYRFGSIGVA HNGNLVNYKT LRAMLEENGS IFNTSSDTEV VLHLIAISKA RPFFMRIIDA
CEKLQGAYSM VFVTEDKLVA VRDPYGFRPL VMGRRSNGAV VFASETCALD LIEATYEREV
YPGEVLVVDK DGVKSQCLMP KFEPKQCIFE HIYFSLPNSI VFGRSVYESR HVFGEILATE
SPVECDVVIA VPDSGVVAAL GYAAKSGVPF QQGLIRSHYV GRTFIEPSQK IRDFGVKLKL
SPVRGVLEGK RVVVVDDSIV RGTTSSKIVR LLREAGAKEV HMRIASPPIV ASCYYGVDTP
SSEELISNRL SVEEINEFIG SDSLAFLSFD TLKKHLGKDS KSFCYACFTG DYPVKPTEVK
VKRGGGDFID DGLVGSFENI EAGWVR
