gene name: guaA
| locus tag k12 | ECK2503 | information on phylogenetic profile |
|---|---|---|
| locus tag mg1655 | b2507 | |
| locus tag w3110 | JW2491 | |
| gene name k12 | guaA | |
| locus name | guaA | |
| synonyms of locus name |
| scop id | 52317; 52402 |
|---|---|
| superfamily | Class I glutamine amidotransferase-like; Adenine nucleotide alpha hydrolases |
| pfam id | PF00117; PF00958 |
| pfam domain | Glutamine amidotransferase class-I; GMP synthase C terminal domain |
| tigrfam id | TIGR00888; TIGR00884 |
| name | guaA_Nterm; guaA_Cterm |
| function | GMP synthase, N-terminal domai; GMP synthase, C-terminal domai |
| swissprot name | GUAA_ECOLI |
|---|---|
| description | GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (Glutamine|amidotransferase) (GMP synthetase) (GMPS). |
| seq length | 525 |
| fastaseq |
| go id | GO:0005737; GO:0015949; GO:0006164; GO:0006164; GO:0015949; GO:0006164 |
|---|---|
| go term | cytoplasm; nucleobase, nucleoside and nucleotide interconversion; purine nucleotide biosynthesis; purine nucleotide biosynthesis; nucleobase, nucleoside and nucleotide interconversion; purine nucleotide biosynth |
| gene product description | GMP synthetase (glutamine aminotransferase) |
|---|---|
| comment gene product description | |
| evidence | E |
| context | |
| gene product desc | Enzyme |
| cell location | Cytoplasmic |
| features | CDS |
| functional category code | F |
|---|---|
| functional category | Nucleotide transport and metabolism |
| reference #1 | Nucleotide sequence of the guaA gene encoding GMP synthetase of Escherichia coli K12. Tiedeman A., Smith J., Zalkin H. (J Biol Chem. 1985 Jul 25; 260(15):8676-9) |
|---|---|
| reference #2 | Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase. Zalkin H., Argos P., Narayana S., Tiedeman A., Smith J. (J Biol Chem. 1985 Mar 25; 260(6):3350-4) |
| reference #3 | Nucleotide sequence of the guaA gene encoding GMP synthetase of Escherichia coli K12. Tiedeman A., Smith J., Zalkin H. (J Biol Chem. 1985 Jul 25; 260(15):8676-9) |
| reference #4 | The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Tesmer J., Klem T., Deras M., Davisson V., Smith J. (Nat Struct Biol. 1996 Jan; 3(1):74-86) |
| phylogenetic profile |
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