PUR1_MOUSE
ID PUR1_MOUSE Reviewed; 517 AA.
AC Q8CIH9; Q3TKC5; Q3TUW2; Q3UGU3;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Amidophosphoribosyltransferase;
DE Short=ATase;
DE EC=2.4.2.14 {ECO:0000250|UniProtKB:P35433};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase;
DE Short=GPAT;
DE Flags: Precursor;
GN Name=Ppat {ECO:0000312|MGI:MGI:2387203};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-477.
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC phosphoribosylpyrophosphate (PRPP) and glutamine.
CC {ECO:0000250|UniProtKB:P35433}.
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:0000250|UniProtKB:P35433};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14907;
CC Evidence={ECO:0000250|UniProtKB:P35433};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00497};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00497};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P00497};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P00497};
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:0000250|UniProtKB:P35433}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00497}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000305}.
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DR EMBL; AK147750; BAE28114.1; -; mRNA.
DR EMBL; AK160542; BAE35859.1; -; mRNA.
DR EMBL; AK164506; BAE37815.1; -; mRNA.
DR EMBL; AK167057; BAE39220.1; -; mRNA.
DR EMBL; BC023841; AAH23841.1; -; mRNA.
DR RefSeq; NP_742158.1; NM_172146.2.
DR AlphaFoldDB; Q8CIH9; -.
DR SMR; Q8CIH9; -.
DR STRING; 10090.ENSMUSP00000120632; -.
DR MEROPS; C44.001; -.
DR PhosphoSitePlus; Q8CIH9; -.
DR EPD; Q8CIH9; -.
DR MaxQB; Q8CIH9; -.
DR PaxDb; Q8CIH9; -.
DR PeptideAtlas; Q8CIH9; -.
DR PRIDE; Q8CIH9; -.
DR ProteomicsDB; 334682; -.
DR Antibodypedia; 24019; 367 antibodies from 28 providers.
DR DNASU; 231327; -.
DR Ensembl; ENSMUST00000140076; ENSMUSP00000120632; ENSMUSG00000029246.
DR GeneID; 231327; -.
DR KEGG; mmu:231327; -.
DR UCSC; uc008xvl.2; mouse.
DR CTD; 5471; -.
DR MGI; MGI:2387203; Ppat.
DR VEuPathDB; HostDB:ENSMUSG00000029246; -.
DR eggNOG; KOG0572; Eukaryota.
DR GeneTree; ENSGT00390000003428; -.
DR HOGENOM; CLU_022389_3_1_1; -.
DR InParanoid; Q8CIH9; -.
DR OMA; ENAQPTF; -.
DR OrthoDB; 400911at2759; -.
DR PhylomeDB; Q8CIH9; -.
DR TreeFam; TF106370; -.
DR Reactome; R-MMU-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00124.
DR BioGRID-ORCS; 231327; 24 hits in 77 CRISPR screens.
DR ChiTaRS; Ppat; mouse.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8CIH9; protein.
DR Bgee; ENSMUSG00000029246; Expressed in primitive streak and 244 other tissues.
DR ExpressionAtlas; Q8CIH9; baseline and differential.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IDA:MGI.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IDA:MGI.
DR GO; GO:0097294; P:'de novo' XMP biosynthetic process; IDA:MGI.
DR GO; GO:0006543; P:glutamine catabolic process; ISO:MGI.
DR GO; GO:0006177; P:GMP biosynthetic process; IDA:MGI.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; ISO:MGI.
DR GO; GO:0019693; P:ribose phosphate metabolic process; ISO:MGI.
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; Acetylation; Allosteric enzyme; Glutamine amidotransferase;
KW Glycosyltransferase; Iron; Iron-sulfur; Magnesium; Metal-binding;
KW Purine biosynthesis; Reference proteome; Transferase.
FT PROPEP 1..11
FT /evidence="ECO:0000250|UniProtKB:P35433"
FT /id="PRO_0000455153"
FT CHAIN 12..517
FT /note="Amidophosphoribosyltransferase"
FT /id="PRO_0000455154"
FT DOMAIN 12..261
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT BINDING 280
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT BINDING 389
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT BINDING 390
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT BINDING 426
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT BINDING 503
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT BINDING 506
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P00497"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q06203"
FT CONFLICT 359..362
FT /note="QPNM -> HPTL (in Ref. 1; BAE28114)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="L -> S (in Ref. 1; BAE28114)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="V -> M (in Ref. 1; BAE35859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 57403 MW; 730F84E0B31A72BA CRC64;
MELEELGIRE ECGVFGCIAS GDWPTQLDVP HVITLGLVGL QHRGQESAGI VTSDGSAVPK
FRVHKGMGLV NHVFTEDNLK KLYDSNLGIG HTRYATTGKC ELENCQPFVV ETLHGKIAVA
HNGELVNAAR LRKKLLRQGI GLSTSSDSEM ITQLLAYTPP QEKDDAPDWV ARIKNLMKEA
PAAYSLVIMH RDFIYAVRDP YGNRPLCIGR LMPVSDVNDK EKKSSETEGW VVSSESCSFL
SIGARYCHEV KPGEIVEISR HGIRTLDIIP RSNGDPVAFC IFEYVYFARP DSMFEDQMVY
TVRYRCGQQL AIEAPVEADL VSTVPESATP AALGYATKCG LPYVEVLCKN RYVGRTFIQP
NMRLRQLGVA KKFGVLSDNF KGKRIVLIDD SIVRGNTISP IIKLLKESGA KEVHIRVASP
PIKYPCFMGI NIPTKEELIA NKPEFDCLAE YLGANSVVYL SVEGLVSSVQ QEIKFKKQKV
KKHDIAIQEN GNGLEYFEKT GHCTACLTGQ YPVELEW
