Glutamyl-tRNA reductase (P0A6X1)

Identification
Name:Glutamyl-tRNA reductase
Synonyms:
  • GluTR
Gene Name:hemA
Enzyme Class:
Biological Properties
General Function:Involved in glutamyl-tRNA reductase activity
Specific Function:Catalyzes the NADPH-dependent reduction of glutamyl- tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0L-Glutamyl-tRNA(Glu)+1.0Thumb+1.0Thumb+1.0tRNA(Glu) ↔ 1.0Thumb+1.0tRNA(Glu)+1.0Thumb+1.0Thumb
1.0L-Glutamyl-tRNA(Glu) + 1.0NADPH + 1.0Hydrogen ion + 1.0tRNA(Glu) ↔ 1.0(S)-4-Amino-5-oxopentanoate + 1.0tRNA(Glu) + 1.0NADP + 1.0L-Glutamyl-tRNA(Glu)
ReactionCard
SMPDB Reactions:
8.0L-glutamyl-tRNA(Glu)+8.0NADPH+8.0Thumb → 8.0tRNA(Glu)+8.0Thumb+8.0Thumb
8.0L-glutamyl-tRNA(Glu) + 8.0NADPH + 8.0NADPH → 8.0tRNA(Glu) + 8.0NADP + 8.0(S)-4-Amino-5-oxopentanoate
ReactionCard
Complex Reactions:
1.0L-Glutamyl-tRNA(Glu)+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0tRNA (Glu)
1.0L-Glutamyl-tRNA(Glu) + 1.0Hydrogen ion + 1.0NADPH → 1.0(S)-4-Amino-5-oxopentanoate + 1.0NADP + 1.0tRNA (Glu)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(Glu) → 1.0L-glutamyl-tRNA(Glu)+1.0Thumb
1.0(S)-4-Amino-5-oxopentanoate + 1.0NADP + 1.0tRNA(Glu) → 1.0L-glutamyl-tRNA(Glu) + 1.0NADPH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB20017(S)-4-Amino-5-oxopentanoateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB23782L-Glutamyl-tRNA(Glu)MetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
binding
catalytic activity
glutamyl-tRNA reductase activity
NADP or NADPH binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
shikimate 5-dehydrogenase activity
Process
biosynthetic process
cellular biosynthetic process
heterocycle biosynthetic process
metabolic process
oxidation reduction
tetrapyrrole biosynthetic process
Gene Properties
Blattner:b1210
Gene OrientationClockwise
Centisome Percentage:27.22
Left Sequence End1262937
Right Sequence End1264193
Gene Sequence:
>1257 bp
ATGGGTAGTAATATACATGGAATTAGTTGCACTGCAAATAATTATTTGAAACAGGCCTGG
AACGATATAAAAAATGAGTACGAAAAAAATCAAACATATTCAATCACGCTTTTTGAAAAC
ACACTGGTGTGTTTTATGCGGTTATACAATGAACTCAGACGTAAAGTAAATGAAGAGGAT
ACTCCATGTCTGGAATGTGAATCACTAGAAAAAGAATTTGAGGAAATGCAGAATGATAAT
GATCTATCATTATTTATGAGAATATTGCGTACTAATGATACACAAATTTATTCAGGGGTT
TCAGGAGGTATTACATATACTATACAATATGTTCGAGATATTGATATTGTTAGAGTGTCC
TTGCCGGGCAGAGCTTCAGAGTCTATCACAGATTTTAAAGGTTATTATTGGTATAACTTT
ATGGAGTATATTGAAAACATTAATGCGTGTGATGATGTTTTTTCTGAGTATTGTTTTGAT
GATGAAAATATAAGTGTCCAGCCAGAGCGGATAAATACGCCGGGAATATCTGATTTGGAT
TCTGACATTGATTTGTCTGGTATATCTTTTATTCAGCGTGAAACTAACCAGGCATTAGGA
TTAAAATATGCTCCTGTAGATGGCGATGGATATTGTCTGTTAAGAGCTATACTGGTTTTA
AAACAACATGATTATTCATGGGCGCTGGTCAGTTATAAGATGCAAAAGGAAGTTTACAAC
GAATTCATTAAAATGGTTGATAAAAAAACGATCGAGGCTCTTGTTGATACGGCATTCTAT
AATCTCAGGGAAGATGTAAAGACGTTATTTGGCGTTGATCTACAATCTGACAACCAAATT
CAGGGGCAGAGTAGTCTTATGTCATGGAGCTTTCTGTTTTTTAAAAAACAATTCATTGAT
AGTTGCTTGAATAACGAAAAATGTATCCTGCATTTACCCGAGTTTATATTTAATGATAAC
AAGAACTTGCTTGCTTTAGATACCGACACGTCGGATAGGATTAAAGCGGTGAAGAATTTT
CTTGTTGTTCTTTCAGATAGCATTTGCTCATTATTTATTGTTAATAGTAATGTGGCATCA
ATCTCCTTGGGGAATGAATCCTTTTCAACAGATGAAGATCTTGAGTATGGTTATTTAATG
AACACTGGCAATCATTATGACGTTTACCTCCCTCCTGAACTTTTTGCTCAGGCTTACAAG
TTAAACAATAAGGAAATGAATGCGCAACTCGACTATTTAAATCGTTATGCAATTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:418
Protein Molecular Weight:46306
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glutamyl-tRNA reductase
MTLLALGINHKTAPVSLRERVSFSPDKLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVE
EQDNLQEALIRWLCDYHNLNEEDLRKSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQ
VKKAFADSQKGHMKASELERMFQKSFSVAKRVRTETDIGASAVSVAFAACTLARQIFESL
STVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQILADEVGAEVIALSDIDERL
READIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSV
DDLQSIISHNLAQRKAAAVEAETIVAQETSEFMAWLRAQSASETIREYRSQAEQVRDELT
AKALAALEQGGDAQAIMQDLAWKLTNRLIHAPTKSLQQAARDGDNERLNILRDSLGLE
References
External Links:
ResourceLink
Uniprot ID:P0A6X1
Uniprot Name:HEM1_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062556
Ecogene ID:EG10427
Ecocyc:EG10427
ColiBase:b1210
Kegg Gene:b1210
EchoBASE ID:EB0422
CCDB:HEM1_ECOLI
BacMap:16129173
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
  • Drolet, M., Peloquin, L., Echelard, Y., Cousineau, L., Sasarman, A. (1989). "Isolation and nucleotide sequence of the hemA gene of Escherichia coli K12." Mol Gen Genet 216:347-352. Pubmed: 2664455
  • 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
  • Ikemi, M., Murakami, K., Hashimoto, M., Murooka, Y. (1992). "Cloning and characterization of genes involved in the biosynthesis of delta-aminolevulinic acid in Escherichia coli." Gene 121:127-132. Pubmed: 1427085
  • Li, J. M., Russell, C. S., Cosloy, S. D. (1989). "Cloning and structure of the hem A gene of Escherichia coli K-12." Gene 82:209-217. Pubmed: 2684779
  • Luer, C., Schauer, S., Mobius, K., Schulze, J., Schubert, W. D., Heinz, D. W., Jahn, D., Moser, J. (2005). "Complex formation between glutamyl-tRNA reductase and glutamate-1-semialdehyde 2,1-aminomutase in Escherichia coli during the initial reactions of porphyrin biosynthesis." J Biol Chem 280:18568-18572. Pubmed: 15757895
  • Luer, C., Schauer, S., Virus, S., Schubert, W. D., Heinz, D. W., Moser, J., Jahn, D. (2007). "Glutamate recognition and hydride transfer by Escherichia coli glutamyl-tRNA reductase." FEBS J 274:4609-4614. Pubmed: 17697121
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Schauer, S., Chaturvedi, S., Randau, L., Moser, J., Kitabatake, M., Lorenz, S., Verkamp, E., Schubert, W. D., Nakayashiki, T., Murai, M., Wall, K., Thomann, H. U., Heinz, D. W., Inokuchi, H., Soll, D., Jahn, D. (2002). "Escherichia coli glutamyl-tRNA reductase. Trapping the thioester intermediate." J Biol Chem 277:48657-48663. Pubmed: 12370189
  • Strohmaier, H., Remler, P., Renner, W., Hogenauer, G. (1995). "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12." J Bacteriol 177:4488-4500. Pubmed: 7543480
  • Verkamp, E., Chelm, B. K. (1989). "Isolation, nucleotide sequence, and preliminary characterization of the Escherichia coli K-12 hemA gene." J Bacteriol 171:4728-4735. Pubmed: 2548996
  • Verkamp, E., Jahn, M., Jahn, D., Kumar, A. M., Soll, D. (1992). "Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression." J Biol Chem 267:8275-8280. Pubmed: 1569081