Identification |
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Name: | Glutamate-ammonia-ligase adenylyltransferase |
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Synonyms: | - Glutamine-synthetase adenylyltransferase
- ATase
- [Glutamate--ammonia-ligase] adenylyltransferase
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Gene Name: | glnE |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in [glutamate-ammonia-ligase] adenylyltransferase activity |
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Specific Function: | Adenylation and deadenylation of glutamate--ammonia ligase |
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Cellular Location: | Not Available |
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SMPDB Pathways: | Not Available |
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KEGG Pathways: | Not Available |
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KEGG Reactions: | |
1.0 | ↔ | 1.0 |
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Complex Reactions: | |
1.0 | + | 1.0[L-glutamate:ammonia ligase (ADP-forming)] | → | 1.0 | + | 1.0adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] |
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Metabolites: | |
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GO Classification: | Function |
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adenylyltransferase activity | catalytic activity | nucleotidyltransferase activity | transferase activity | transferase activity, transferring phosphorus-containing groups | [glutamate-ammonia-ligase] adenylyltransferase activity |
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Gene Properties |
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Blattner: | b3053 |
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Gene Orientation | Counterclockwise |
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Centisome Percentage: | 68.86 |
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Left Sequence End | 3194823 |
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Right Sequence End | 3197663 |
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Gene Sequence: | >2841 bp
ATGAAGCCGCTCTCTTCACCGTTACAGCAGTACTGGCAGACCGTTGTTGAGCGGCTGCCA
GAGCCTTTAGCCGAGGAATCACTTAGCGCACAGGCGAAGTCAGTACTTACTTTTAGTGAT
TTTGTGCAGGACAGCGTGATTGCGCATCCAGAGTGGCTGACGGAACTGGAAAGCCAACCG
CCGCAGGCCGACGAATGGCAGCATTACGCGGCATGGTTGCAGGAGGCGCTCTGTAATGTG
AGTGACGAAGCCGGGTTAATGCGCGAGCTGCGGCTATTCCGGCGGCGCATTATGGTGCGC
ATCGCCTGGGCGCAAACGCTGGCACTGGTTACTGAAGAGAGCATATTGCAGCAGCTCAGC
TATCTGGCGGAGACGCTGATTGTTGCGGCGCGTGACTGGCTGTATGACGCCTGCTGCCGC
GAGTGGGGAACGCCGTGCAATGCGCAGGGCGAAGCGCAACCGCTGCTGATTTTAGGCATG
GGTAAGCTGGGCGGTGGGGAGCTGAATTTCTCCTCTGATATCGATCTGATTTTTGCCTGG
CCGGAACATGGTTGTACGCAGGGTGGACGCCGGGAACTGGATAACGCGCAGTTTTTTACC
CGCATGGGGCAGCGGCTGATTAAAGTGCTGGATCAACCAACGCAGGATGGCTTCGTCTAT
CGCGTGGATATGCGGCTGCGTCCGTTTGGCGAAAGTGGCCCGCTGGTGCTGAGCTTTGCC
GCGTTGGAAGATTATTACCAGGAGCAGGGGCGCGACTGGGAGCGTTACGCGATGGTCAAG
GCGCGGATTATGGGCGATAGCGAAGGCGTCTATGCTAACGAGTTGCGTGCGATGCTGCGC
CCGTTTGTTTTCCGTCGTTACATCGATTTCAGCGTGATTCAGTCGCTGCGCAACATGAAA
GGGATGATTGCCCGTGAAGTGCGTCGACGTGGTTTGACCGACAATATCAAACTCGGCGCA
GGCGGCATTCGCGAAATTGAATTTATCGTTCAGGTGTTCCAGCTCATTCGCGGCGGACGC
GAACCGTCGCTGCAATCGCGCTCTTTACTGCCAACGCTCAGCGCCATTGCCGAGCTGCAT
CTGCTTTCTGAAAACGATGCTGAACAATTGCGAGTGGCGTATCTGTTCCTGCGGCGTCTG
GAAAACCTGCTGCAAAGCATTAACGACGAACAAACCCAGACGCTTCCTTCTGATGAGCTT
AATCGTGCGCGGCTGGCGTGGGCGATGGACTTTGCTGACTGGCCGCAACTGACCGGGGCG
CTGACCGCACATATGACCAATGTGCGCCGGGTGTTTAATGAATTGATTGGCGACGATGAA
AGTGAAACTCAGGAAGAGTCGCTGTCGGAACAGTGGCGTGAGCTGTGGCAGGATGCGTTG
CAGGAAGATGACACTACGCCAGTGCTGGCGCATCTTAGCGAGGATGATCGCAAACAGGTG
CTAACGCTGATTGCCGATTTCCGCAAAGAGCTGGATAAGCGCACCATCGGGCCGCGAGGA
CGTCAGGTGCTCGACCATCTGATGCCGCATCTGCTAAGTGATGTCTGTGCGCGTGAAGAC
GCTGCCGTTACGCTGTCGCGCATTACCGCCTTGCTGGTGGGGATTGTTACCCGCACCACC
TATTTAGAATTGCTCAGTGAATTCCCCGCGGCGCTTAAACATTTGATTTCTCTGTGTGCC
GCGTCGCCGATGATTGCCAGCCAGCTGGCGCGTTATCCATTATTGCTGGATGAATTGCTC
GATCCAAACACCCTTTACCAGCCGACGGCGACCGATGCCTACCGCGATGAGTTGCGCCAG
TATTTGCTGCGCGTGCCGGAAGATGACGAAGAGCAACAGCTTGAGGCGCTGCGTCAGTTC
AAACAGGCGCAGCTGTTACGCATCGCCGCAGCGGATATCGCCGGTACGCTACCGGTGATG
AAAGTGAGCGATCACTTAACCTGGCTGGCGGAAGCCATGATAGATGCCGTCGTTCAGCAG
GCGTGGGTTCAAATGGTTGCCCGCTACGGTAAGCCGAATCACCTGAACGAACGCGAAGGG
CGTGGTTTTGCGGTGGTCGGCTACGGCAAGCTGGGCGGCTGGGAGTTAGGCTACAGTTCC
GATCTTGACCTTATCTTCCTCCATGATTGCCCAATGGATGCGATGACTGACGGTGAGCGG
GAAATCGACGGGCGGCAGTTTTATCTGCGTCTGGCGCAACGCATTATGCATCTGTTCAGT
ACGCGTACCTCTTCCGGCATTTTGTATGAAGTGGATGCTCGACTGCGTCCGTCCGGGGCG
GCGGGAATGCTGGTGACATCCGCAGAAGCATTTGCCGATTATCAGAAAAACGAGGCCTGG
ACGTGGGAACATCAGGCGCTGGTGCGTGCGCGTGTAGTGTACGGCGATCCGCAGCTCACC
GCGCACTTTGACGCAGTGCGTCGCGAGATTATGACGCTGCCGCGTGAAGGTAAAACTCTG
CAAACGGAAGTGCGGGAAATGCGCGAGAAAATGCGCGCTCATCTCGGCAATAAACATCGC
GATCGCTTTGATATCAAAGCTGATGAAGGGGGAATTACCGATATCGAATTTATTACCCAA
TATCTGGTGTTGCGCTACGCTCATGAAAAACCGAAGTTAACGCGCTGGTCAGACAACGTG
CGTATTCTGGAACTACTGGCGCAAAACGACATTATGGAAGAGCAGGAAGCGATGGCGCTG
ACCCGTGCTTACACTACGCTTCGCGATGAACTTCATCATCTGGCATTACAGGAATTGCCG
GGCCATGTGTCGGAGGATTGCTTCACCGCAGAGCGTGAACTGGTGCGGGCAAGCTGGCAG
AAGTGGCTGGTGGAAGAATGA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 946 |
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Protein Molecular Weight: | 108417 |
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Protein Theoretical pI: | 5 |
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PDB File: | 1V4A |
Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >Glutamate-ammonia-ligase adenylyltransferase
MKPLSSPLQQYWQTVVERLPEPLAEESLSAQAKSVLTFSDFVQDSVIAHPEWLTELESQP
PQADEWQHYAAWLQEALCNVSDEAGLMRELRLFRRRIMVRIAWAQTLALVTEESILQQLS
YLAETLIVAARDWLYDACCREWGTPCNAQGEAQPLLILGMGKLGGGELNFSSDIDLIFAW
PEHGCTQGGRRELDNAQFFTRMGQRLIKVLDQPTQDGFVYRVDMRLRPFGESGPLVLSFA
ALEDYYQEQGRDWERYAMVKARIMGDSEGVYANELRAMLRPFVFRRYIDFSVIQSLRNMK
GMIAREVRRRGLTDNIKLGAGGIREIEFIVQVFQLIRGGREPSLQSRSLLPTLSAIAELH
LLSENDAEQLRVAYLFLRRLENLLQSINDEQTQTLPSDELNRARLAWAMDFADWPQLTGA
LTAHMTNVRRVFNELIGDDESETQEESLSEQWRELWQDALQEDDTTPVLAHLSEDDRKQV
LTLIADFRKELDKRTIGPRGRQVLDHLMPHLLSDVCAREDAAVTLSRITALLVGIVTRTT
YLELLSEFPAALKHLISLCAASPMIASQLARYPLLLDELLDPNTLYQPTATDAYRDELRQ
YLLRVPEDDEEQQLEALRQFKQAQLLRIAAADIAGTLPVMKVSDHLTWLAEAMIDAVVQQ
AWVQMVARYGKPNHLNEREGRGFAVVGYGKLGGWELGYSSDLDLIFLHDCPMDAMTDGER
EIDGRQFYLRLAQRIMHLFSTRTSSGILYEVDARLRPSGAAGMLVTSAEAFADYQKNEAW
TWEHQALVRARVVYGDPQLTAHFDAVRREIMTLPREGKTLQTEVREMREKMRAHLGNKHR
DRFDIKADEGGITDIEFITQYLVLRYAHEKPKLTRWSDNVRILELLAQNDIMEEQEAMAL
TRAYTTLRDELHHLALQELPGHVSEDCFTAERELVRASWQKWLVEE |
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References |
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External Links: | |
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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
- 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
- van Heeswijk, W. C., Rabenberg, M., Westerhoff, H. V., Kahn, D. (1993). "The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli." Mol Microbiol 9:443-457. Pubmed: 8412694
- Xu, Y., Zhang, R., Joachimiak, A., Carr, P. D., Huber, T., Vasudevan, S. G., Ollis, D. L. (2004). "Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase." Structure 12:861-869. Pubmed: 15130478
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