| Identification |
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| Name | GMP synthase [glutamine-hydrolyzing] |
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| Synonyms | - GMP synthetase
- Glutamine amidotransferase
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| Gene Name | GUA1 |
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| Enzyme Class | |
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| Biological Properties |
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| General Function | Involved in catalytic activity |
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| Specific Function | ATP + xanthosine 5'-phosphate + L-glutamine + H(2)O = AMP + diphosphate + GMP + L-glutamate |
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| Cellular Location | Cytoplasm |
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| SMPDB Pathways | Not Available |
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| KEGG Pathways | |
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| SMPDB Reactions | Not Available |
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| KEGG Reactions | |
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| Metabolites | | YMDB ID | Name | View |
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| YMDB00002 | L-Glutamine | Show | | YMDB00097 | Adenosine monophosphate | Show | | YMDB00109 | Adenosine triphosphate | Show | | YMDB00219 | Pyrophosphate | Show | | YMDB00261 | Guanosine monophosphate | Show | | YMDB00271 | L-Glutamic acid | Show | | YMDB00289 | Xanthylic acid | Show | | YMDB00862 | hydron | Show | | YMDB00890 | water | Show |
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| GO Classification | | Component |
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| Not Available | | Function |
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| nucleoside binding | | purine nucleoside binding | | adenyl nucleotide binding | | adenyl ribonucleotide binding | | ATP binding | | GMP synthase (glutamine-hydrolyzing) activity | | catalytic activity | | ligase activity | | ligase activity, forming carbon-nitrogen bonds | | carbon-nitrogen ligase activity, with glutamine as amido-N-donor | | binding | | Process |
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| nucleobase, nucleoside, nucleotide and nucleic acid metabolic process | | nucleobase, nucleoside and nucleotide metabolic process | | nucleoside phosphate metabolic process | | nucleotide metabolic process | | purine nucleotide metabolic process | | purine nucleotide biosynthetic process | | purine nucleoside monophosphate biosynthetic process | | GMP biosynthetic process | | purine ribonucleoside monophosphate biosynthetic process | | biosynthetic process | | cellular metabolic process | | metabolic process | | cellular amino acid and derivative metabolic process | | cellular amino acid metabolic process | | glutamine family amino acid metabolic process | | glutamine metabolic process | | nitrogen compound metabolic process | | cellular nitrogen compound metabolic process |
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| Gene Properties |
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| Chromosome Location | chromosome 13 |
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| Locus | YMR217W |
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| Gene Sequence | >1578 bp
ATGGCTGCCGGTGAACAAGTTTCTAACATGTTTGACACTATCTTAGTGTTAGACTTTGGT
TCTCAATACTCTCATTTGATTACCAGAAGATTAAGAGAGTTTAACATCTATGCTGAGATG
TTGCCATGCACTCAGAAGATCTCTGAGTTGGGCTGGACTCCAAAGGGTGTCATTCTTTCT
GGTGGTCCATATTCCGTATACGCTGAAGACGCTCCACACGTAGACCATGCTATCTTTGAT
TTGAACGTTCCAATCCTGGGTATCTGTTACGGTATGCAAGAATTGGCTTGGATTAATGGT
AAACAAGTTGGTCGTGGTGACAAGAGAGAGTACGGTCCTGCCACTTTGAAGGTGATTGAC
GATTCCAACTCTCTATTCAAAGGTATGAACGACTCTACTGTCTGGATGTCTCACGGTGAT
AAATTGCACGGCTTGCCAACTGGTTACAAGACCATTGCCACCTCCGATAACTCCCCATAC
TGTGGTATTGTCCACGAAACTAAGCCAATCTATGGTATCCAATTCCACCCAGAAGTTACA
CATTCTACCCAAGGTAAGACTCTTTTGAAAAACTTCGCCGTTGATTTGTGTCACGCTAAG
CAAAACTGGACTATGGAAAACTTTATCGACACTGAAATAAACAGAATCAGAAAACTGGTC
GGTCCAACTGCTGAAGTCATTGGTGCTGTTTCCGGTGGTGTTGATTCTACTGTTGCATCC
AAATTGATGACAGAAGCCATCGGTGATAGATTCCATGCCATTTTGGTCGATAACGGTGTT
TTAAGATTAAATGAAGCTGCTAACGTTAAAAAGACTCTTGTCGAAGGTTTAGGTATCAAC
TTGATGGTTGTCGATGCTTCCGAAGAATTTTTAAGCAAATTGAAGGGTGTCACTGACCCA
GAAAAGAAGAGAAAGATTATTGGTAACACATTTATCCACGTCTTTGAAAGAGAAGCTGAA
AAAATTAAGCCAAGAGATGGTAAGGAGATTCAATTCCTGTTACAAGGTACTCTTTATCCA
GATGTCATCGAATCCATTTCTTTCAAAGGTCCTTCTCAAACCATTAAAACTCATCACAAC
GTCGGTGGTTTACTAGAGAACATGAAATTAAAGCTAATTGAACCATTGAGAGAACTGTTC
AAAGACGAAGTCAGGCATCTAGGTGAATTATTAGGAATCCCTCATGATCTAGTCTGGAGA
CACCCTTTCCCTGGTCCAGGTATTGCTATTCGTGTTCTAGGTGAAGTTACTAAGGAACAA
GTCGAAATAGCAAGAAAAGCTGACAACATTTACATTGAAGAAATCAAGAAGGCCGGCTTA
TACAACCAAATTTCCCAAGCCTTTGCCTGTTTGTTGCCCGTTAAATCCGTTGGTGTTATG
GGTGACCAAAGAACCTATGATCAAGTTATTGCTTTGAGGGCCATTGAAACTACTGATTTC
ATGACTGCTGACTGGTTCCCATTCGAACACAGTTTCTTGAAGAAAGTCGCCTCAAGAATT
GTCAATGAAGTCGATGGGGTTGCTAGGGTCACTTACGATATAACTTCCAAACCTCCTGCA
ACTGTTGAATGGGAATGA |
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| Protein Properties |
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| Pfam Domain Function | |
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| Protein Residues | 525 |
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| Protein Molecular Weight | 58481.80078 |
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| Protein Theoretical pI | 6.47 |
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| Signalling Regions | |
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| Transmembrane Regions | |
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| Protein Sequence | >GMP synthase [glutamine-hydrolyzing]
MAAGEQVSNMFDTILVLDFGSQYSHLITRRLREFNIYAEMLPCTQKISELGWTPKGVILS
GGPYSVYAEDAPHVDHAIFDLNVPILGICYGMQELAWINGKQVGRGDKREYGPATLKVID
DSNSLFKGMNDSTVWMSHGDKLHGLPTGYKTIATSDNSPYCGIVHETKPIYGIQFHPEVT
HSTQGKTLLKNFAVDLCHAKQNWTMENFIDTEINRIRKLVGPTAEVIGAVSGGVDSTVAS
KLMTEAIGDRFHAILVDNGVLRLNEAANVKKTLVEGLGINLMVVDASEEFLSKLKGVTDP
EKKRKIIGNTFIHVFEREAEKIKPKDGKEIQFLLQGTLYPDVIESISFKGPSQTIKTHHN
VGGLLENMKLKLIEPLRELFKDEVRHLGELLGIPHDLVWRHPFPGPGIAIRVLGEVTKEQ
VEIARKADNIYIEEIKKAGLYNQISQAFACLLPVKSVGVMGDQRTYDQVIALRAIETTDF
MTADWFPFEHSFLKKVASRIVNEVDGVARVTYDITSKPPATVEWE |
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| References |
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| External Links | |
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| General Reference | - Dujardin, G., Kermorgant, M., Slonimski, P. P., Boucherie, H. (1994). "Cloning and sequencing of the GMP synthetase-encoding gene of Saccharomyces cerevisiae." Gene 139:127-132.8112582
- Bowman, S., Churcher, C., Badcock, K., Brown, D., Chillingworth, T., Connor, R., Dedman, K., Devlin, K., Gentles, S., Hamlin, N., Hunt, S., Jagels, K., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Skelton, J., Walsh, S., Whitehead, S., Barrell, B. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Nature 387:90-93.9169872
- Boucherie, H., Dujardin, G., Kermorgant, M., Monribot, C., Slonimski, P., Perrot, M. (1995). "Two-dimensional protein map of Saccharomyces cerevisiae: construction of a gene-protein index." Yeast 11:601-613.7483834
- Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
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