ECMDB

Identification

Name:

GMP synthase [glutamine-hydrolyzing]

Synonyms:

GMP synthetase
GMPS
Glutamine amidotransferase

Gene Name:

guaA

Enzyme Class:

6.3.5.2

Biological Properties

General Function:

Involved in GMP synthase (glutamine-hydrolyzing) activity

Specific Function:

Catalyzes the synthesis of GMP from XMP

Cellular Location:

Not Available

SMPDB Pathways:

purine nucleotides de novo biosynthesis PW000910
purine nucleotides de novo biosynthesis 1435709748 PW000960
purine nucleotides de novo biosynthesis 2 PW002033

KEGG Pathways:

Drug metabolism - other enzymes ec00983
Metabolic pathways eco01100
Purine metabolism ec00230

KEGG Reactions:

1.0

→

1.0

2.0

1.0

1.0Adenosine triphosphate + 1.0L-Glutamine + 1.0Water + 1.0Xanthylic acid → 1.0Adenosine monophosphate + 1.0L-Glutamate + 1.0Guanosine monophosphate + 2.0Hydrogen ion + 1.0Pyrophosphate
ReactionCard

1.0

↔

1.0

1.0Adenosine triphosphate + 1.0Xanthylic acid + 1.0Ammonia ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0Guanosine monophosphate
ReactionCard

1.0

↔

1.0

1.0Adenosine triphosphate + 1.0Xanthylic acid + 1.0L-Glutamine + 1.0Water ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0Guanosine monophosphate + 1.0L-Glutamate
ReactionCard

1.06-Thioxanthine 5'-monophosphate

1.0

↔

1.06-Thioguanosine monophosphate

1.0

1.06-Thioxanthine 5'-monophosphate + 1.0Adenosine triphosphate + 1.0L-Glutamine + 1.0Water ↔ 1.06-Thioguanosine monophosphate + 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Glutamate
ReactionCard

1.0

→

1.0

1.0Water + 1.0L-Glutamine + 1.0Xanthylic acid + 1.0Adenosine triphosphate → 1.0Hydrogen ion + 1.0L-Glutamate + 1.0Guanosine monophosphate + 1.0Pyrophosphate + 1.0Adenosine monophosphate
ReactionCard

1.0

→

1.0

1.0Adenosine triphosphate + 1.0Xanthylic acid + 1.0Ammonia → 1.0Hydrogen ion + 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0Guanosine monophosphate
ReactionCard

1.0

↔

1.0

1.0Adenosine triphosphate + 1.0Xanthylic acid + 1.0L-Glutamine + 1.0Water + 1.0Ammonia ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0Guanosine monophosphate + 1.0L-Glutamate
ReactionCard

SMPDB Reactions:

1.0

→

1.0

1.0Pyrophosphate

1.0L-Glutamic acid

2.0

1.0

1.0Xanthylic acid + 1.0Adenosine triphosphate + 1.0L-Glutamine + 1.0Water → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Glutamic acid + 2.0Hydrogen ion + 1.0Guanosine monophosphate + 1.0L-Glutamate
ReactionCard

EcoCyc Reactions:

1.0

→

1.0

2.0

1.0

→

1.0

→

1.0

1.0Adenosine triphosphate + 1.0Xanthylic acid + 1.0Ammonia → 1.0Hydrogen ion + 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0Guanosine monophosphate
ReactionCard

Complex Reactions:

1.0

→

1.0

1.0Adenosine triphosphate + 1.0Xanthylic acid + 1.0L-Glutamine + 1.0Water → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0Guanosine monophosphate + 1.0L-Glutamate
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB00045	Adenosine monophosphate	MetaboCard
ECMDB00538	Adenosine triphosphate	MetaboCard
ECMDB00051	Ammonia	MetaboCard
ECMDB01397	Guanosine monophosphate	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB00148	L-Glutamate	MetaboCard
ECMDB00641	L-Glutamine	MetaboCard
ECMDB04142	Pyrophosphate	MetaboCard
ECMDB00494	Water	MetaboCard
ECMDB01554	Xanthylic acid	MetaboCard

GO Classification:

Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
carbon-nitrogen ligase activity, with glutamine as amido-N-donor
catalytic activity
GMP synthase (glutamine-hydrolyzing) activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
nucleoside binding
purine nucleoside binding
Process
biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
cellular nitrogen compound metabolic process
glutamine family amino acid metabolic process
glutamine metabolic process
GMP biosynthetic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
purine nucleoside monophosphate biosynthetic process
purine nucleotide biosynthetic process
purine nucleotide metabolic process
purine ribonucleoside monophosphate biosynthetic process

Gene Properties

Blattner:

b2507

Gene Orientation

Counterclockwise

Centisome Percentage:

56.66

Left Sequence End

2628980

Right Sequence End

2630557

Gene Sequence:

>1578 bp
ATGACGGAAAACATTCATAAGCATCGCATCCTCATTCTGGACTTCGGTTCTCAGTACACT
CAACTGGTTGCGCGCCGCGTGCGTGAGCTGGGTGTTTACTGCGAACTGTGGGCGTGGGAT
GTGACAGAAGCACAAATTCGTGACTTCAATCCAAGCGGCATTATTCTTTCCGGCGGCCCG
GAAAGTACTACTGAAGAAAACAGTCCGCGTGCGCCGCAGTATGTCTTTGAAGCAGGCGTA
CCGGTATTCGGCGTTTGCTATGGCATGCAGACCATGGCAATGCAGTTGGGCGGTCACGTT
GAAGCCTCTAACGAACGTGAATTTGGCTACGCGCAGGTTGAAGTCGTAAACGACAGCGCA
CTGGTTCGCGGTATCGAAGATGCGCTGACCGCAGACGGTAAACCGCTGCTCGATGTCTGG
ATGAGCCACGGCGATAAAGTTACCGCTATTCCGTCCGACTTCATCACCGTAGCCAGCACC
GAAAGCTGCCCGTTTGCCATTATGGCTAACGAAGAAAAACGCTTCTATGGCGTACAGTTC
CACCCGGAAGTGACTCATACCCGCCAGGGTATGCGCATGCTGGAGCGTTTTGTGCGTGAT
ATCTGCCAGTGTGAAGCCCTGTGGACGCCAGCGAAAATTATCGACGATGCTGTAGCTCGC
ATCCGCGAGCAGGTAGGCGACGATAAAGTCATCCTCGGCCTCTCTGGTGGTGTGGATTCC
TCCGTAACCGCAATGCTGCTGCACCGCGCTATCGGTAAAAACCTGACTTGCGTATTCGTC
GACAACGGCCTGCTGCGCCTCAACGAAGCAGAGCAGGTTCTGGATATGTTTGGCGATCAC
TTTGGTCTTAACATTGTTCACGTACCGGCAGAAGATCGCTTCCTGTCAGCGCTGGCTGGC
GAAAACGATCCGGAAGCAAAACGTAAAATCATCGGTCGCGTTTTCGTTGAAGTATTCGAT
GAAGAAGCGCTGAAACTGGAAGACGTGAAGTGGCTGGCGCAGGGCACCATCTACCCTGAC
GTTATCGAATCTGCGGCGTCTGCAACCGGTAAAGCACACGTCATCAAATCTCACCACAAC
GTGGGCGGCCTGCCGAAAGAGATGAAGATGGGCCTGGTTGAACCGCTGAAAGAGCTGTTC
AAAGACGAAGTGCGTAAGATTGGTCTGGAGCTGGGCCTGCCGTACGACATGCTGTACCGT
CACCCGTTCCCGGGACCAGGCCTTGGCGTTCGTGTTCTGGGTGAAGTGAAGAAAGAGTAC
TGTGACCTGCTGCGCCGTGCTGACGCCATCTTCATTGAAGAACTGCGTAAAGCGGACCTG
TACGACAAAGTCAGCCAGGCGTTCACTGTGTTCCTGCCGGTACGTTCCGTTGGCGTAATG
GGCGATGGTCGTAAGTATGACTGGGTTGTCTCTCTGCGTGCTGTCGAAACCATCGACTTT
ATGACCGCACACTGGGCGCATCTGCCGTACGATTTCCTCGGTCGCGTTTCCAACCGCATT
ATCAATGAAGTGAACGGTATTTCCCGCGTGGTGTATGACATCAGCGGCAAGCCGCCAGCT
ACCATTGAGTGGGAATGA

Protein Properties

Pfam Domain Function:

GATase (PF00117 )
GMP_synt_C (PF00958 )
NAD_synthase (PF02540 )

Protein Residues:

525

Protein Molecular Weight:

58679

Protein Theoretical pI:

PDB File:

1GPM

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>GMP synthase [glutamine-hydrolyzing]
MTENIHKHRILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGP
ESTTEENSPRAPQYVFEAGVPVFGVCYGMQTMAMQLGGHVEASNEREFGYAQVEVVNDSA
LVRGIEDALTADGKPLLDVWMSHGDKVTAIPSDFITVASTESCPFAIMANEEKRFYGVQF
HPEVTHTRQGMRMLERFVRDICQCEALWTPAKIIDDAVARIREQVGDDKVILGLSGGVDS
SVTAMLLHRAIGKNLTCVFVDNGLLRLNEAEQVLDMFGDHFGLNIVHVPAEDRFLSALAG
ENDPEAKRKIIGRVFVEVFDEEALKLEDVKWLAQGTIYPDVIESAASATGKAHVIKSHHN
VGGLPKEMKMGLVEPLKELFKDEVRKIGLELGLPYDMLYRHPFPGPGLGVRVLGEVKKEY
CDLLRRADAIFIEELRKADLYDKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDF
MTAHWAHLPYDFLGRVSNRIINEVNGISRVVYDISGKPPATIEWE

References

External Links:

Resource	Link
Uniprot ID:	P04079
Uniprot Name:	GUAA_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	1805567
PDB ID:	1GPM
Ecogene ID:	EG10420
Ecocyc:	EG10420
ColiBase:	b2507
Kegg Gene:	b2507
EchoBASE ID:	EB0415
CCDB:	GUAA_ECOLI
BacMap:	16130432

General Reference:

Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
Deras, M. L., Chittur, S. V., Davisson, V. J. (1999). "N2-hydroxyguanosine 5'-monophosphate is a time-dependent inhibitor of Escherichia coli guanosine monophosphate synthetase." Biochemistry 38:303-310. Pubmed: 9890911
Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
Hutchings, M. I., Drabble, W. T. (2000). "Regulation of the divergent guaBA and xseA promoters of Escherichia coli by the cyclic AMP receptor protein." FEMS Microbiol Lett 187:115-122. Pubmed: 10856643
Tesfa-Selase, F., Drabble, W. T. (1992). "Regulation of the gua operon of Escherichia coli by the DnaA protein." Mol Gen Genet 231:256-264. Pubmed: 1736096
Tesmer, J. J., Klem, T. J., Deras, M. L., Davisson, V. J., Smith, J. L. (1996). "The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families." Nat Struct Biol 3:74-86. Pubmed: 8548458
Tiedeman, A. A., Smith, J. M., Zalkin, H. (1985). "Nucleotide sequence of the guaA gene encoding GMP synthetase of Escherichia coli K12." J Biol Chem 260:8676-8679. Pubmed: 3894345
Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837
Zalkin, H., Argos, P., Narayana, S. V., Tiedeman, A. A., Smith, J. M. (1985). "Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase." J Biol Chem 260:3350-3354. Pubmed: 2982857

GMP synthase [glutamine-hydrolyzing] (P04079)