ID GUAA_MOUSE Reviewed; 693 AA. AC Q3THK7; Q3TFR6; Q3TIH1; Q3UJ21; Q3V343; Q66JZ6; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 2. DT 28-JUN-2023, entry version 141. DE RecName: Full=GMP synthase [glutamine-hydrolyzing]; DE EC=6.3.5.2 {ECO:0000269|PubMed:240826}; DE AltName: Full=GMP synthetase; DE AltName: Full=Glutamine amidotransferase; GN Name=Gmps; 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]. RC STRAIN=BALB/cJ, C57BL/6J, DBA/2J, and NOD; RC TISSUE=Eye, Heart, Kidney, Spinal cord, and Thymus; 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 MRNA] OF 217-693. RC TISSUE=Limb; 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 PROTEIN SEQUENCE OF 536-548 AND 570-589, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [4] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY RP REGULATION. RX PubMed=240826; DOI=10.1016/s0021-9258(19)40954-x; RA Spector T.; RT "Studies with GMP synthetase from Ehrlich ascites cells. Purification, RT properties, and interactions with nucleotide analogs."; RL J. Biol. Chem. 250:7372-7376(1975). RN [5] 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: Catalyzes the conversion of xanthine monophosphate (XMP) to CC GMP in the presence of glutamine and ATP through an adenyl-XMP CC intermediate. {ECO:0000269|PubMed:240826}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 CC H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; CC Evidence={ECO:0000269|PubMed:240826}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11681; CC Evidence={ECO:0000305|PubMed:240826}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q4V7C6}; CC -!- ACTIVITY REGULATION: Stimulated by dithiothreitol and inhibited by 2- CC mercaptoethanol, p-chloromercuribenzoate and hydroxylamine. CC {ECO:0000269|PubMed:240826}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.0036 mM for XMP {ECO:0000269|PubMed:240826}; CC KM=0.28 mM for ATP {ECO:0000269|PubMed:240826}; CC KM=0.68 mM for glutamine {ECO:0000269|PubMed:240826}; CC Vmax=1.0 nmol/min/mg enzyme for XMP {ECO:0000269|PubMed:240826}; CC Vmax=1.1 nmol/min/mg enzyme for ATP {ECO:0000269|PubMed:240826}; CC Vmax=1.37 nmol/min/mg enzyme for glutamine CC {ECO:0000269|PubMed:240826}; CC pH dependence: CC Optimum pH is 7.6. {ECO:0000269|PubMed:240826}; CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln CC route): step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49915}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P49915}. CC -!- SEQUENCE CAUTION: CC Sequence=BAE20667.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK049755; BAE20667.1; ALT_FRAME; mRNA. DR EMBL; AK143197; BAE25299.1; -; mRNA. DR EMBL; AK146654; BAE27334.1; -; mRNA. DR EMBL; AK167857; BAE39875.1; -; mRNA. DR EMBL; AK168239; BAE40189.1; -; mRNA. DR EMBL; AK169043; BAE40832.1; -; mRNA. DR EMBL; AK169701; BAE41314.1; -; mRNA. DR EMBL; BC080685; AAH80685.1; -; mRNA. DR CCDS; CCDS17383.1; -. DR RefSeq; NP_001028472.2; NM_001033300.2. DR AlphaFoldDB; Q3THK7; -. DR SMR; Q3THK7; -. DR BioGRID; 230837; 21. DR STRING; 10090.ENSMUSP00000029405; -. DR BindingDB; Q3THK7; -. DR ChEMBL; CHEMBL2765; -. DR MEROPS; C26.950; -. DR GlyGen; Q3THK7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q3THK7; -. DR PhosphoSitePlus; Q3THK7; -. DR SwissPalm; Q3THK7; -. DR REPRODUCTION-2DPAGE; IPI00351252; -. DR EPD; Q3THK7; -. DR jPOST; Q3THK7; -. DR MaxQB; Q3THK7; -. DR PaxDb; Q3THK7; -. DR ProteomicsDB; 270905; -. DR Antibodypedia; 33632; 280 antibodies from 33 providers. DR Ensembl; ENSMUST00000029405; ENSMUSP00000029405; ENSMUSG00000027823. DR GeneID; 229363; -. DR KEGG; mmu:229363; -. DR UCSC; uc008pke.1; mouse. DR AGR; MGI:2448526; -. DR CTD; 8833; -. DR MGI; MGI:2448526; Gmps. DR VEuPathDB; HostDB:ENSMUSG00000027823; -. DR eggNOG; KOG1622; Eukaryota. DR GeneTree; ENSGT00390000006591; -. DR HOGENOM; CLU_014340_0_2_1; -. DR InParanoid; Q3THK7; -. DR OMA; DQLTCMF; -. DR OrthoDB; 6206at2759; -. DR PhylomeDB; Q3THK7; -. DR TreeFam; TF106132; -. DR Reactome; R-MMU-73817; Purine ribonucleoside monophosphate biosynthesis. DR Reactome; R-MMU-9748787; Azathioprine ADME. DR UniPathway; UPA00189; UER00296. DR BioGRID-ORCS; 229363; 23 hits in 80 CRISPR screens. DR ChiTaRS; Gmps; mouse. DR PRO; PR:Q3THK7; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; Q3THK7; protein. DR Bgee; ENSMUSG00000027823; Expressed in ear vesicle and 235 other tissues. DR ExpressionAtlas; Q3THK7; baseline and differential. DR Genevisible; Q3THK7; MM. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IDA:MGI. DR GO; GO:0003921; F:GMP synthase activity; ISO:MGI. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006177; P:GMP biosynthetic process; IDA:MGI. DR GO; GO:0032263; P:GMP salvage; ISO:MGI. DR CDD; cd01742; GATase1_GMP_Synthase; 1. DR CDD; cd01997; GMP_synthase_C; 1. DR Gene3D; 3.30.300.10; -; 2. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR001674; GMP_synth_C. DR InterPro; IPR004739; GMP_synth_GATase. DR InterPro; IPR025777; GMPS_ATP_PPase_dom. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1. DR PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1. DR Pfam; PF00117; GATase; 1. DR Pfam; PF00958; GMP_synt_C; 1. DR Pfam; PF02540; NAD_synthase; 1. DR PRINTS; PR00097; ANTSNTHASEII. DR PRINTS; PR00096; GATASE. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 2. DR TIGRFAMs; TIGR00888; guaA_Nterm; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. DR PROSITE; PS51553; GMPS_ATP_PPASE; 1. PE 1: Evidence at protein level; KW Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; KW Glutamine amidotransferase; GMP biosynthesis; Ligase; Nucleotide-binding; KW Phosphoprotein; Purine biosynthesis; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P49915" FT CHAIN 2..693 FT /note="GMP synthase [glutamine-hydrolyzing]" FT /id="PRO_0000284365" FT DOMAIN 27..216 FT /note="Glutamine amidotransferase type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT DOMAIN 217..435 FT /note="GMPS ATP-PPase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00886" FT ACT_SITE 104 FT /note="For GATase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT ACT_SITE 190 FT /note="For GATase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT ACT_SITE 192 FT /note="For GATase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT BINDING 244..250 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00886" FT BINDING 337 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /evidence="ECO:0000250|UniProtKB:P49915" FT BINDING 522 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /evidence="ECO:0000250|UniProtKB:P49915" FT BINDING 610 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /evidence="ECO:0000250|UniProtKB:P49915" FT BINDING 685 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /evidence="ECO:0000250|UniProtKB:P49915" FT BINDING 691 FT /ligand="XMP" FT /ligand_id="ChEBI:CHEBI:57464" FT /evidence="ECO:0000250|UniProtKB:P49915" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P49915" FT MOD_RES 8 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P49915" FT MOD_RES 9 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P49915" FT MOD_RES 318 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P49915" FT MOD_RES 332 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P49915" FT CONFLICT 201 FT /note="V -> I (in Ref. 1; BAE39875)" FT /evidence="ECO:0000305" FT CONFLICT 205 FT /note="N -> Y (in Ref. 1; BAE39875)" FT /evidence="ECO:0000305" FT CONFLICT 265 FT /note="V -> D (in Ref. 1; BAE39875)" FT /evidence="ECO:0000305" FT CONFLICT 356 FT /note="S -> G (in Ref. 1; BAE40189)" FT /evidence="ECO:0000305" FT CONFLICT 359 FT /note="P -> H (in Ref. 1; BAE40189)" FT /evidence="ECO:0000305" FT CONFLICT 359 FT /note="P -> R (in Ref. 1; BAE39875)" FT /evidence="ECO:0000305" FT CONFLICT 363 FT /note="Missing (in Ref. 1; BAE39875)" FT /evidence="ECO:0000305" FT CONFLICT 511..512 FT /note="LL -> CC (in Ref. 1; BAE27334)" FT /evidence="ECO:0000305" FT CONFLICT 586 FT /note="S -> G (in Ref. 1; BAE39875)" FT /evidence="ECO:0000305" SQ SEQUENCE 693 AA; 76723 MW; 854DBAD6A9C75A12 CRC64; MALCNGDSKP ENAGGDLKDG SHHYEGAVVI LDAGAQYGKV IDRRVRELFV QSEIFPLETP AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPI LGICYGMQMM NKVFGGTVHK KSVREDGVFN ISMDNTCSLF RGLQKEEIVL LTHGDSVDKV ADGFKVVARS GNIVAGIANE SKKLYGVQFH PEVGLTENGK VILKNFLYDI AGCSGNFTVQ NRELECIREI KEKVGTSKVL VLLSGGVDST VCTALLNRAL NQDQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE VIGEMSLKPE EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK LREEGKVIEP LKDFHKDEVR ILGRELDLPE ELVSRHPFPG PGLAIRVICA EEPYICKDFP ETNNILKIVA DFSASVKKPH TLLQRVKACT TEEDQEKLMQ ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW ESLIFLARLI PRMCHNINRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR ESGFAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGVP ATPGNEIPVE VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE //