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 13-FEB-2019, entry version 122. DE RecName: Full=GMP synthase [glutamine-hydrolyzing]; DE EC=6.3.5.2; DE AltName: Full=GMP synthetase; DE AltName: Full=Glutamine amidotransferase; GN Name=Gmps; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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 RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Involved in the de novo synthesis of guanine nucleotides CC which are not only essential for DNA and RNA synthesis, but also CC provide GTP, which is involved in a number of cellular processes CC important for cell division. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + CC 2 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 -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln CC route): step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SEQUENCE CAUTION: CC Sequence=BAE20667.1; Type=Frameshift; Positions=35; 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 UniGene; Mm.331051; -. DR UniGene; Mm.394565; -. DR UniGene; Mm.490620; -. DR ProteinModelPortal; Q3THK7; -. DR SMR; Q3THK7; -. DR BioGrid; 230837; 3. DR STRING; 10090.ENSMUSP00000029405; -. DR BindingDB; Q3THK7; -. DR ChEMBL; CHEMBL2765; -. DR MEROPS; C26.950; -. 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 PRIDE; Q3THK7; -. DR Ensembl; ENSMUST00000029405; ENSMUSP00000029405; ENSMUSG00000027823. DR GeneID; 229363; -. DR KEGG; mmu:229363; -. DR UCSC; uc008pke.1; mouse. DR CTD; 8833; -. DR MGI; MGI:2448526; Gmps. DR eggNOG; KOG1622; Eukaryota. DR eggNOG; COG0518; LUCA. DR eggNOG; COG0519; LUCA. DR GeneTree; ENSGT00390000006591; -. DR HOGENOM; HOG000223965; -. DR HOVERGEN; HBG005929; -. DR InParanoid; Q3THK7; -. DR KO; K01951; -. DR OMA; KRKIIGH; -. DR OrthoDB; 751525at2759; -. DR PhylomeDB; Q3THK7; -. DR TreeFam; TF106132; -. DR Reactome; R-MMU-73817; Purine ribonucleoside monophosphate biosynthesis. DR UniPathway; UPA00189; UER00296. DR PRO; PR:Q3THK7; -. DR Proteomes; UP000000589; Chromosome 3. DR Bgee; ENSMUSG00000027823; Expressed in 279 organ(s), highest expression level in ear vesicle. DR ExpressionAtlas; Q3THK7; baseline and differential. DR Genevisible; Q3THK7; MM. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0003921; F:GMP synthase activity; ISO:MGI. DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006177; P:GMP biosynthetic process; ISO:MGI. DR CDD; cd01742; GATase1_GMP_Synthase; 1. DR CDD; cd01997; GMP_synthase_C; 1. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.40.50.880; -; 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 Pfam; PF00117; GATase; 1. DR Pfam; PF00958; GMP_synt_C; 1. DR Pfam; PF02540; NAD_synthase; 1. DR SUPFAM; SSF52317; SSF52317; 1. 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; Complete proteome; Cytoplasm; KW Direct protein sequencing; Glutamine amidotransferase; KW GMP biosynthesis; Ligase; Nucleotide-binding; Phosphoprotein; KW Purine biosynthesis; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P49915}. FT CHAIN 2 693 GMP synthase [glutamine-hydrolyzing]. FT /FTId=PRO_0000284365. FT DOMAIN 27 216 Glutamine amidotransferase type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. FT DOMAIN 217 435 GMPS ATP-PPase. {ECO:0000255|PROSITE- FT ProRule:PRU00886}. FT NP_BIND 244 250 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00886}. FT ACT_SITE 104 104 For GATase activity. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. FT ACT_SITE 190 190 For GATase activity. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. FT ACT_SITE 192 192 For GATase activity. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. FT BINDING 337 337 Substrate. {ECO:0000250}. FT BINDING 522 522 Substrate. {ECO:0000250}. FT BINDING 610 610 Substrate. {ECO:0000250}. FT BINDING 685 685 Substrate. {ECO:0000250}. FT BINDING 691 691 Substrate. {ECO:0000250}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000250|UniProtKB:P49915}. FT MOD_RES 8 8 Phosphoserine. FT {ECO:0000250|UniProtKB:P49915}. FT MOD_RES 9 9 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P49915}. FT MOD_RES 318 318 Phosphothreonine. FT {ECO:0000250|UniProtKB:P49915}. FT MOD_RES 332 332 Phosphoserine. FT {ECO:0000250|UniProtKB:P49915}. FT CONFLICT 201 201 V -> I (in Ref. 1; BAE39875). FT {ECO:0000305}. FT CONFLICT 205 205 N -> Y (in Ref. 1; BAE39875). FT {ECO:0000305}. FT CONFLICT 265 265 V -> D (in Ref. 1; BAE39875). FT {ECO:0000305}. FT CONFLICT 356 356 S -> G (in Ref. 1; BAE40189). FT {ECO:0000305}. FT CONFLICT 359 359 P -> H (in Ref. 1; BAE40189). FT {ECO:0000305}. FT CONFLICT 359 359 P -> R (in Ref. 1; BAE39875). FT {ECO:0000305}. FT CONFLICT 363 363 Missing (in Ref. 1; BAE39875). FT {ECO:0000305}. FT CONFLICT 511 512 LL -> CC (in Ref. 1; BAE27334). FT {ECO:0000305}. FT CONFLICT 586 586 S -> G (in Ref. 1; BAE39875). FT {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 //