PUR1_DROME
ID PUR1_DROME Reviewed; 546 AA.
AC Q27601; Q8T009; Q9VHY4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Amidophosphoribosyltransferase;
DE Short=ATase;
DE EC=2.4.2.14 {ECO:0000305|PubMed:8150282};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase;
DE Short=GPAT;
DE AltName: Full=Phosphoribosylamidotransferase {ECO:0000303|PubMed:8150282};
DE Short=PRAT {ECO:0000303|PubMed:8150282};
DE Flags: Precursor;
GN Name=Prat; ORFNames=CG2867;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=8150282; DOI=10.1093/genetics/136.2.547;
RA Clark D.V.;
RT "Molecular and genetic analyses of Drosophila Prat, which encodes the first
RT enzyme of de novo purine biosynthesis.";
RL Genetics 136:547-557(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; THR-114 AND SER-120, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Involved in the first step (and regulatory point) of the de
CC novo biosynthesis of purine nucleotides, where it catalyzes the
CC transfer of glutamine amide to 5-phospho-alpha-D-ribose 1-diphosphate.
CC {ECO:0000269|PubMed:8150282}.
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:0000305|PubMed:8150282};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14907;
CC Evidence={ECO:0000305|PubMed:8150282};
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. {ECO:0000305|PubMed:8150282}.
CC -!- DISRUPTION PHENOTYPE: Reduction in viability and frequent wing defects.
CC {ECO:0000269|PubMed:8150282}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39084.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF017096; AAC39084.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014297; AAF54163.2; -; Genomic_DNA.
DR EMBL; AY069652; AAL39797.1; -; mRNA.
DR PIR; S47860; S47860.
DR RefSeq; NP_001246972.1; NM_001260043.1.
DR RefSeq; NP_524271.2; NM_079547.3.
DR AlphaFoldDB; Q27601; -.
DR SMR; Q27601; -.
DR BioGRID; 66121; 1.
DR STRING; 7227.FBpp0081261; -.
DR MEROPS; C44.001; -.
DR iPTMnet; Q27601; -.
DR PaxDb; Q27601; -.
DR PRIDE; Q27601; -.
DR DNASU; 40935; -.
DR EnsemblMetazoa; FBtr0081764; FBpp0081261; FBgn0004901.
DR EnsemblMetazoa; FBtr0304705; FBpp0293248; FBgn0004901.
DR GeneID; 40935; -.
DR KEGG; dme:Dmel_CG2867; -.
DR CTD; 40935; -.
DR FlyBase; FBgn0004901; Prat.
DR VEuPathDB; VectorBase:FBgn0004901; -.
DR eggNOG; KOG0572; Eukaryota.
DR GeneTree; ENSGT00390000003428; -.
DR HOGENOM; CLU_022389_3_1_1; -.
DR InParanoid; Q27601; -.
DR OMA; CTHCFDG; -.
DR OrthoDB; 400911at2759; -.
DR PhylomeDB; Q27601; -.
DR Reactome; R-DME-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00124.
DR BioGRID-ORCS; 40935; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 40935; -.
DR PRO; PR:Q27601; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004901; Expressed in adult abdomen and 41 other tissues.
DR ExpressionAtlas; Q27601; baseline and differential.
DR Genevisible; Q27601; DM.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IMP:FlyBase.
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:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0040016; P:embryonic cleavage; IMP:FlyBase.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IMP:UniProtKB.
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 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 4Fe-4S; Glutamine amidotransferase; Glycosyltransferase; Iron; Iron-sulfur;
KW Magnesium; Metal-binding; Phosphoprotein; Purine biosynthesis;
KW Reference proteome; Transferase.
FT PROPEP 1..53
FT /evidence="ECO:0000305"
FT /id="PRO_0000029287"
FT CHAIN 54..546
FT /note="Amidophosphoribosyltransferase"
FT /id="PRO_0000029288"
FT DOMAIN 54..302
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 54
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT BINDING 321
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 528
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 531
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 114
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 150
FT /note="E -> V (in Ref. 1; AAC39084)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="T -> S (in Ref. 1; AAC39084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 59520 MW; 4CA4D981EF2C34CC CRC64;
MSAPQQQQQS QQKQQQHVRV VEQQQVEPAE AVTSSMESES ISASKELTGL THECGVFGAI
ACGDWPTQMD IAHVICLGLV ALQHRGQESA GIATSEGKCS KNFNVHKGMG MISTLFNDDS
MKKLRGNLGI GHTRYSTAGG SGVVNCQPFE VHTTHGALAL AHNGELVNNE SLRREVLARG
VGLSTHSDSE LIAQSLCCAP EDVSELDGPN WPARIRHFMM LAPLSYSLVI MLKDKIYAVR
DTYGNRPLCI GKIVPINAGH GNNLDTPADG WVVSSESCGF LSIGARYVRE VEPGEIVELS
RSGYRTVDIV ERPDFKRMAF CIFEYVYFAR GDSIFEGQMV YTVRLQCGRQ LWREAPVEAD
IVSSVPESGT AAAHGYARES GIEFAEVLCR NRYVGRTFIQ PSTRLRQLGV AKKFGALSEN
VAGKRLVLID DSIVRGNTIG PIIKLLRDAG AREVHIRIAS PPLQYPCYMG INIPTREELI
ANKLNPDQLA RHVGADSLAY LSVEGLVEAV QLKHRDAGDS KSKGTGHCTA CLTGEYPGGL
PDELSW
