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Identification
HMDB Protein ID HMDBP00592
Secondary Accession Numbers
  • 5864
  • HMDBP03988
Name GMP synthase [glutamine-hydrolyzing]
Synonyms
  1. GMP synthetase
  2. Glutamine amidotransferase
Gene Name GMPS
Protein Type Unknown
Biological Properties
General Function Involved in catalytic activity
Specific Function Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division.
Pathways
  • 2-Hydroxyglutric Aciduria (D And L Form)
  • 4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase Deficiency
  • Adenine phosphoribosyltransferase deficiency (APRT)
  • Adenosine Deaminase Deficiency
  • Adenylosuccinate Lyase Deficiency
  • AICA-Ribosiduria
  • Azathioprine Action Pathway
  • Drug metabolism - other enzymes
  • Glutamate Metabolism
  • GMP biosynthesis
  • Gout or Kelley-Seegmiller Syndrome
  • Homocarnosinosis
  • Hyperinsulinism-Hyperammonemia Syndrome
  • Lesch-Nyhan Syndrome (LNS)
  • Mercaptopurine Action Pathway
  • Mercaptopurine Metabolism Pathway
  • Mitochondrial DNA depletion syndrome
  • Molybdenum Cofactor Deficiency
  • Myoadenylate deaminase deficiency
  • Purine Metabolism
  • Purine metabolism
  • Purine Nucleoside Phosphorylase Deficiency
  • Succinic semialdehyde dehydrogenase deficiency
  • Thioguanine Action Pathway
  • Xanthine Dehydrogenase Deficiency (Xanthinuria)
  • Xanthinuria type I
  • Xanthinuria type II
Reactions
Adenosine triphosphate + Xanthylic acid + L-Glutamine + Water → Adenosine monophosphate + Pyrophosphate + Guanosine monophosphate + L-Glutamic acid details
Adenosine triphosphate + Xanthylic acid + Ammonia → Adenosine monophosphate + Pyrophosphate + Guanosine monophosphate details
6-Thioxanthine 5'-monophosphate + Adenosine triphosphate + L-Glutamine + Water → 6-Thioguanosine monophosphate + Adenosine monophosphate + Pyrophosphate + L-Glutamic acid details
GO Classification
Biological Process
glutamine metabolic process
purine nucleobase biosynthetic process
Cellular Component
cytosol
Function
binding
catalytic activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
ligase activity
carbon-nitrogen ligase activity, with glutamine as amido-n-donor
gmp synthase (glutamine-hydrolyzing) activity
ligase activity, forming carbon-nitrogen bonds
Molecular Function
ATP binding
GMP synthase (glutamine-hydrolyzing) activity
GMP synthase activity
pyrophosphatase activity
Process
purine nucleotide metabolic process
purine nucleotide biosynthetic process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
purine nucleoside monophosphate biosynthetic process
purine ribonucleoside monophosphate biosynthetic process
gmp biosynthetic process
cellular metabolic process
glutamine metabolic process
glutamine family amino acid metabolic process
biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 3
Locus 3q24
SNPs GMPS
Gene Sequence
>2082 bp
ATGGCTCTGTGCAACGGAGACTCCAAGCTGGAGAATGCTGGAGGAGACCTTAAGGATGGC
CACCACCACTATGAAGGAGCTGTTGTCATTCTGGATGCTGGTGCTCAGTACGGGAAAGTC
ATAGACCGAAGAGTGAGGGAACTGTTCGTGCAGTCTGAAATTTTCCCCTTGGAAACACCA
GCATTTGCTATAAAGGAACAAGGATTCCGTGCTATTATCATCTCTGGAGGACCTAATTCT
GTGTATGCTGAAGATGCTCCCTGGTTTGATCCAGCAATATTCACTATTGGCAAGCCTGTT
CTTGGAATTTGCTATGGTATGCAGATGATGAATAAGGTATTTGGAGGTACTGTGCACAAA
AAAAGTGTCAGAGAAGATGGAGTTTTCAACATTAGTGTGGATAATACATGTTCATTATTC
AGGGGCCTTCAGAAGGAAGAAGTTGTTTTGCTTACACATGGAGATAGTGTAGACAAAGTA
GCTGATGGATTCAAGGTTGTGGCACGTTCTGGAAACATAGTAGCAGGCATAGCAAATGAA
TCTAAAAAGTTATATGGAGCACAGTTCCACCCTGAAGTTGGCCTTACAGAAAATGGAAAA
GTAATACTGAAGAATTTCCTTTATGATATAGCTGGATGCAGTGGAACCTTCACCGTGCAG
AACAGAGAACTTGAGTGTATTCGAGAGATCAAAGAGAGAGTAGGCACGTCAAAAGTTTTG
GTTTTACTCAGTGGTGGAGTAGACTCAACAGTTTGTACAGCTTTGCTAAATCGTGCTTTG
AACCAAGAACAAGTCATTGCTGTGCACATTGATAATGGCTTTATGAGAAAACGAGAAAGC
CAGTCTGTTGAAGAGGCCCTCAAAAAGCTTGGAATTCAGGTCAAAGTGATAAATGCTGCT
CATTCTTTCTACAATGGAACAACAACCCTACCAATATCAGATGAAGATAGAACCCCACGG
AAAAGAATTAGCAAAACGTTAAATATGACCACAAGTCCTGAAGAGAAAAGAAAAATCATT
GGGGATACTTTTGTTAAGATTGCCAATGAAGTAATTGGAGAAATGAACTTGAAACCAGAG
GAGGTTTTCCTTGCCCAAGGTACTTTACGGCCTGATCTAATTGAAAGTGCATCCCTTGTT
GCAAGTGGCAAAGCTGAACTCATCAAAACCCATCACAATGACACAGAGCTCATCAGAAAG
TTGAGAGAGGAGGGAAAAGTAATAGAACCTCTGAAAGATTTTCATAAAGATGAAGTGAGA
ATTTTGGGCAGAGAACTTGGACTTCCAGAAGAGTTAGTTTCCAGGCATCCATTTCCAGGT
CCTGGCCTGGCAATCAGAGTAATATGTGCTGAAGAACCTTATATTTGTAAGGACTTTCCT
GAAACCAACAATATTTTGAAAATAGTAGCTGATTTTTCTGCAAGTGTTAAAAAGCCACAT
ACCCTATTACAGAGAGTCAAAGCCTGCACAACAGAAGAGGATCAGGAGAAGCTGATGCAA
ATTACCAGTCTGCATTCACTGAATGCCTTCTTGCTGCCAATTAAAACTGTAGGTGTGCAG
GGTGACTGTCGTTCCTACAGTTACGTGTGTGGAATCTCCAGTAAAGATGAACCTGACTGG
GAATCACTTATTTTTCTGGCTAGGCTTATACCTCGCATGTGTCACAACGTTAACAGAGTT
GTTTATATATTTGGCCCACCAGTTAAAGAACCTCCTACAGATGTTACTCCCACTTTCTTG
ACAACAGGGGTGCTCAGTACTTTACGCCAAGCTGATTTTGAGGCCCATAACATTCTCAGG
GAGTCTGGGTATGCTGGGAAAATCAGCCAGATGCCGGTGATTTTGACACCATTACATTTT
GATCGGGACCCACTTCAAAAGCAGCCTTCATGCCAGAGATCTGTGGTTATTCGAACCTTT
ATTACTAGTGACTTCATGACTGGTATACCTGCAACACCTGGCAATGAGATCCCTGTAGAG
GTGGTATTAAAGATGGTCACTGAGATTAAGAAGATTCCTGGTATTTCTCGAATTATGTAT
GACTTAACATCAAAGCCCCCAGGAACTACTGAGTGGGAGTAA
Protein Properties
Number of Residues 693
Molecular Weight 76714.79
Theoretical pI 6.867
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>GMP synthase [glutamine-hydrolyzing]
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P49915
UniProtKB/Swiss-Prot Entry Name GUAA_HUMAN
PDB IDs
GenBank Gene ID U10860
GeneCard ID GMPS
GenAtlas ID GMPS
HGNC ID HGNC:4378
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  4. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed:18187866 ]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  6. Hirst M, Haliday E, Nakamura J, Lou L: Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA. J Biol Chem. 1994 Sep 23;269(38):23830-7. [PubMed:8089153 ]
  7. Pegram LD, Megonigal MD, Lange BJ, Nowell PC, Rowley JD, Rappaport EF, Felix CA: t(3;11) translocation in treatment-related acute myeloid leukemia fuses MLL with the GMPS (GUANOSINE 5' MONOPHOSPHATE SYNTHETASE) gene. Blood. 2000 Dec 15;96(13):4360-2. [PubMed:11110714 ]