PUR1_VIGAC
ID PUR1_VIGAC Reviewed; 485 AA.
AC P52419;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Amidophosphoribosyltransferase, chloroplastic;
DE Short=ATase;
DE EC=2.4.2.14;
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase;
DE Short=GPAT;
DE Flags: Precursor; Fragment;
GN Name=PUR1;
OS Vigna aconitifolia (Moth bean) (Phaseolus aconitifolius).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3918;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Root nodule;
RX PubMed=7894513; DOI=10.1046/j.1365-313x.1995.07010077.x;
RA Kim J.H., Delauney A.J., Verma D.P.S.;
RT "Control of de novo purine biosynthesis genes in ureide-producing legumes:
RT induction of glutamine phosphoribosylpyrophosphate amidotransferase gene
RT and characterization of its cDNA from soybean and Vigna.";
RL Plant J. 7:77-86(1995).
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=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
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 -!- 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.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000305}.
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DR EMBL; L23834; AAA73944.1; -; mRNA.
DR PIR; T10792; T10792.
DR AlphaFoldDB; P52419; -.
DR SMR; P52419; -.
DR MEROPS; C44.001; -.
DR UniPathway; UPA00074; UER00124.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
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; -; 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 2: Evidence at transcript level;
KW 4Fe-4S; Chloroplast; Glutamine amidotransferase; Glycosyltransferase; Iron;
KW Iron-sulfur; Magnesium; Metal-binding; Plastid; Purine biosynthesis;
KW Transferase; Transit peptide.
FT TRANSIT <1..18
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 19..485
FT /note="Amidophosphoribosyltransferase, chloroplastic"
FT /id="PRO_0000029290"
FT DOMAIN 19..237
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 19
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT BINDING 253
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 485 AA; 53205 MW; EE9CD20AE5BEDD82 CRC64;
KTTNTFASVN DDEKPREECG VVGIYGDPEA SRLCSLALHA LQHRGQEGAG IVAVHDNLFH
QVNGVGLVSD VFNEAKLSEL PGSCAIGHVR YSTAGHSKLV NVQPFVAGYR FGSVAVAHNG
NFVNYRSLRA KLEDNGSIFN TTSDTEVVLH LIATSKHRPF LLRVVDACEN LKGAYSLVFL
TEDKLVAVRD FGFRPLVMGR RKNGAVVFAS ETCALDLIDA TYEREVNPGE VVVVDHTGIQ
SLCLVTHQEP KQCIFEHIYF ALPNSVVFGR SVYESRRKFG EILATESPVE CDVVIAVPDS
GVVAALGYAA KAGVPFQQGL IRSHHVGRTF IEPSQKIRDF GVKLKLFPVR GVLEGKRVVV
VDDSIVRGTT SSKIVRLIKE AGAKEVHMRI ACPPIVASCY YGVDTPSKEE LISNRMDVEE
IRKFIGSDSL AFLPLDTLKS LLEDDAPNYC YACFSGKYPV QPENLNPTAS MSLTGTMFQW
QFETY
