PUR4_MOUSE
ID PUR4_MOUSE Reviewed; 1337 AA.
AC Q5SUR0; A4FUJ6; Q6A080;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase;
DE Short=FGAM synthase;
DE Short=FGAMS;
DE EC=6.3.5.3;
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase;
DE Short=FGAR amidotransferase;
DE Short=FGAR-AT;
DE AltName: Full=Formylglycinamide ribotide amidotransferase;
GN Name=Pfas; Synonyms=Kiaa0361;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 594-1337.
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the
CC purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of
CC formylglycinamide ribonucleotide (FGAR) and glutamine to yield
CC formylglycinamidine ribonucleotide (FGAM) and glutamate (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC ChEBI:CHEBI:456216; EC=6.3.5.3;
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000305}.
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DR EMBL; AL645902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC114997; AAI14998.1; -; mRNA.
DR EMBL; AK172938; BAD32216.1; -; mRNA.
DR CCDS; CCDS48823.1; -.
DR RefSeq; NP_001152991.1; NM_001159519.1.
DR AlphaFoldDB; Q5SUR0; -.
DR SMR; Q5SUR0; -.
DR BioGRID; 231910; 27.
DR STRING; 10090.ENSMUSP00000021282; -.
DR GlyConnect; 2586; 2 N-Linked glycans (1 site).
DR GlyGen; Q5SUR0; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q5SUR0; -.
DR PhosphoSitePlus; Q5SUR0; -.
DR SwissPalm; Q5SUR0; -.
DR EPD; Q5SUR0; -.
DR jPOST; Q5SUR0; -.
DR MaxQB; Q5SUR0; -.
DR PaxDb; Q5SUR0; -.
DR PeptideAtlas; Q5SUR0; -.
DR PRIDE; Q5SUR0; -.
DR ProteomicsDB; 301981; -.
DR Antibodypedia; 12486; 138 antibodies from 23 providers.
DR Ensembl; ENSMUST00000021282; ENSMUSP00000021282; ENSMUSG00000020899.
DR GeneID; 237823; -.
DR KEGG; mmu:237823; -.
DR UCSC; uc007jot.2; mouse.
DR CTD; 5198; -.
DR MGI; MGI:2684864; Pfas.
DR VEuPathDB; HostDB:ENSMUSG00000020899; -.
DR eggNOG; KOG1907; Eukaryota.
DR GeneTree; ENSGT00390000007600; -.
DR HOGENOM; CLU_001031_0_0_1; -.
DR InParanoid; Q5SUR0; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 38224at2759; -.
DR PhylomeDB; Q5SUR0; -.
DR TreeFam; TF106371; -.
DR Reactome; R-MMU-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00128.
DR BioGRID-ORCS; 237823; 28 hits in 72 CRISPR screens.
DR ChiTaRS; Pfas; mouse.
DR PRO; PR:Q5SUR0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SUR0; protein.
DR Bgee; ENSMUSG00000020899; Expressed in epiblast (generic) and 233 other tissues.
DR ExpressionAtlas; Q5SUR0; baseline and differential.
DR Genevisible; Q5SUR0; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; ISO:MGI.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; ISO:MGI.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; ISO:MGI.
DR GO; GO:0097294; P:'de novo' XMP biosynthetic process; ISO:MGI.
DR GO; GO:0097065; P:anterior head development; IMP:MGI.
DR GO; GO:0006541; P:glutamine metabolic process; ISO:MGI.
DR GO; GO:0006177; P:GMP biosynthetic process; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR Gene3D; 3.30.1330.10; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.650.10; -; 2.
DR HAMAP; MF_00419; PurL_1; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR010073; PurL_large.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR036604; PurS-like_sf.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR SUPFAM; SSF82697; SSF82697; 1.
DR TIGRFAMs; TIGR01735; FGAM_synt; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Glutamine amidotransferase; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..1337
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000370848"
FT DOMAIN 1063..1301
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 1157
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 1296
FT /evidence="ECO:0000250"
FT ACT_SITE 1298
FT /evidence="ECO:0000250"
FT BINDING 322..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 402..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 705
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 706
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 745
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 749
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 908
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 910
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15067"
FT MOD_RES 619
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15067"
FT MOD_RES 622
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15067"
FT CONFLICT 306
FT /note="F -> L (in Ref. 2; AAI14998)"
FT /evidence="ECO:0000305"
FT CONFLICT 594..597
FT /note="GDKR -> WGPQ (in Ref. 3; BAD32216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1337 AA; 144629 MW; DC0DD64F17F80030 CRC64;
MAPVLHFYVR PSGHEGAASG RVFRRLQEKL PTLQSVETEL CYNVHWAAET LPWAEEMKKL
MWLFGCPLVR DDVAQEPWLV PGSNDLLLEV GPRLNFSTPA STNIVSVCQA AGLRAVDRVE
TTRRYRLSFT DHPTAEMEAI SLAALHDRMT EQHYPDPIQS FSPQSIPAPL KGSIDILAEG
RPALEKANQE LGLALDSWDL DFYTKRFQEL QRNPSTVEVF DLAQSNSEHS RHWFFKGQLH
VDGKKLAHSL FESIMSTQAS SNPNNVLKFC DNSSAIQGKK VKFLRPEDST RPSCFQQQQG
LRHVVFTAET HNFPTGVAPF SGATTGTGGR IRDVQCTGRG AHVVAGTAGY CFGNLHIPDY
NLPWEDPSFQ YPGNFARPLE VAIEASNGAS DYGNKFGEPV LAGFARSLGL QLPDGQRREW
IKPIMFSGGI GSMEAKHVGK KPPEPGMEVV KVGGPVYRIG VGGGAASSVQ VQGDNTSDLD
FGAVQRGDPE MEQKMNRVIR ACVEAPGGNP ICSLHDQGAG GNGNVLKELS DPEGAIIYTS
RFQLGDPTLN ALEIWGAEYQ ESNALLLRPS DRDFLSRASA RERCPACFVG TITGDKRIVL
VDDRECLVGK TGQGDAPLTP PTPVDLDLDW VLGKMPQKEF FLQRKPPVLQ PLALPPELSV
RQALNRVLRL PAVASKRYLT NKVDRSVGGL VAQQQCVGPL QTPLADVAVV ALSHQECIGA
ATALGEQPVK SLLDPKAAAR LAVSEALTNL VFALVTDLRD VKCSGNWMWA AKLPGEGAAL
ADACEAMVAV MAALGVAVDG GKDSLSMAAR VGTETVQAPG SLVISAYAVC PDITATVTPD
LKHPGGKGHL LYVPLSPGQH RLGGTALAQC FSQLGEHPPD LDLPENLVRA FHITQGLLKE
CRLCSGHDVS DGGLVTCLLE MAFAGNCGIE VDVPAPGIHA LPVLFAEEPG LVLEVQEADV
AGVRQRYESA GLRCLELGHT GEAGPQAMAR ISVNKAVVVE EPVGELRALW EETSFQLDLL
QAEPRCVIEE KQGLKERTGP SYYLPPTFPV ASVPCKPGGP VPRVAILREE GSNGDREMAD
AFHLAGFEVW DVTMQDLCSG AIRLDTFRGV AFVGGFSYAD VLGSAKGWAA AVTFNPQARE
ELGRFRRRPD TFSLGVCNGC QLLALLGWVG SDPSEEQAEP GQDSQPTQPG LLLRHNLSGR
FESRWATVRV EPGPALMLRG MEGSVLPVWS AHGEGYMAFS SPELQAKIEA KGLVPLHWAD
DDGNPTEQYP LNPNGSPGGI AGICSQDGRH LALMPHPERA VRLWQWAWRP SPFDVLPTSP
WLQLFINARN WTQEDSC
