MULTISPECIES: glutamyl-tRNA reductase [Salmonella]
glutamyl-tRNA reductase( domain architecture ID 11477807)
glutamyl-tRNA reductase catalyzes conversion of glutamyl-tRNA to glutamate-1-semialdehyde
List of domain hits
Name | Accession | Description | Interval | E-value | |||||||
hemA | PRK00045 | glutamyl-tRNA reductase; Reviewed |
1-418 | 0e+00 | |||||||
glutamyl-tRNA reductase; Reviewed : Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 602.56 E-value: 0e+00
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Name | Accession | Description | Interval | E-value | |||||||
hemA | PRK00045 | glutamyl-tRNA reductase; Reviewed |
1-418 | 0e+00 | |||||||
glutamyl-tRNA reductase; Reviewed Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 602.56 E-value: 0e+00
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HemA | COG0373 | Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ... |
1-418 | 0e+00 | |||||||
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis Pssm-ID: 440142 [Multi-domain] Cd Length: 425 Bit Score: 582.46 E-value: 0e+00
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hemA | TIGR01035 | glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ... |
3-418 | 0e+00 | |||||||
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase (TIGR00713), leads to the production of delta-amino-levulinic acid from Glu-tRNA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin] Pssm-ID: 273407 [Multi-domain] Cd Length: 417 Bit Score: 534.66 E-value: 0e+00
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NAD_bind_Glutamyl_tRNA_reduct | cd05213 | NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
3-318 | 1.02e-122 | |||||||
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts. Pssm-ID: 133452 [Multi-domain] Cd Length: 311 Bit Score: 358.12 E-value: 1.02e-122
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GlutR_N | pfam05201 | Glutamyl-tRNAGlu reductase, N-terminal domain; |
9-156 | 1.36e-66 | |||||||
Glutamyl-tRNAGlu reductase, N-terminal domain; Pssm-ID: 461585 Cd Length: 144 Bit Score: 208.51 E-value: 1.36e-66
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Name | Accession | Description | Interval | E-value | |||||||
hemA | PRK00045 | glutamyl-tRNA reductase; Reviewed |
1-418 | 0e+00 | |||||||
glutamyl-tRNA reductase; Reviewed Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 602.56 E-value: 0e+00
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HemA | COG0373 | Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ... |
1-418 | 0e+00 | |||||||
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis Pssm-ID: 440142 [Multi-domain] Cd Length: 425 Bit Score: 582.46 E-value: 0e+00
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hemA | TIGR01035 | glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ... |
3-418 | 0e+00 | |||||||
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase (TIGR00713), leads to the production of delta-amino-levulinic acid from Glu-tRNA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin] Pssm-ID: 273407 [Multi-domain] Cd Length: 417 Bit Score: 534.66 E-value: 0e+00
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NAD_bind_Glutamyl_tRNA_reduct | cd05213 | NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
3-318 | 1.02e-122 | |||||||
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts. Pssm-ID: 133452 [Multi-domain] Cd Length: 311 Bit Score: 358.12 E-value: 1.02e-122
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PLN00203 | PLN00203 | glutamyl-tRNA reductase |
2-407 | 4.37e-79 | |||||||
glutamyl-tRNA reductase Pssm-ID: 215101 [Multi-domain] Cd Length: 519 Bit Score: 253.52 E-value: 4.37e-79
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GlutR_N | pfam05201 | Glutamyl-tRNAGlu reductase, N-terminal domain; |
9-156 | 1.36e-66 | |||||||
Glutamyl-tRNAGlu reductase, N-terminal domain; Pssm-ID: 461585 Cd Length: 144 Bit Score: 208.51 E-value: 1.36e-66
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PRK13940 | PRK13940 | glutamyl-tRNA reductase; Provisional |
1-417 | 2.57e-66 | |||||||
glutamyl-tRNA reductase; Provisional Pssm-ID: 172450 [Multi-domain] Cd Length: 414 Bit Score: 217.19 E-value: 2.57e-66
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Shikimate_DH | pfam01488 | Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ... |
172-306 | 2.59e-61 | |||||||
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate. Pssm-ID: 460229 [Multi-domain] Cd Length: 136 Bit Score: 194.71 E-value: 2.59e-61
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GlutR_dimer | pfam00745 | Glutamyl-tRNAGlu reductase, dimerization domain; |
320-413 | 4.65e-25 | |||||||
Glutamyl-tRNAGlu reductase, dimerization domain; Pssm-ID: 459922 [Multi-domain] Cd Length: 95 Bit Score: 98.03 E-value: 4.65e-25
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hemA | PRK00676 | glutamyl-tRNA reductase; Validated |
1-155 | 8.48e-21 | |||||||
glutamyl-tRNA reductase; Validated Pssm-ID: 234810 [Multi-domain] Cd Length: 338 Bit Score: 92.62 E-value: 8.48e-21
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AroE | COG0169 | Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
184-262 | 9.69e-13 | |||||||
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 439939 [Multi-domain] Cd Length: 270 Bit Score: 67.86 E-value: 9.69e-13
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NAD_bind_Shikimate_DH | cd01065 | NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
184-250 | 1.39e-10 | |||||||
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts. Pssm-ID: 133443 [Multi-domain] Cd Length: 155 Bit Score: 59.21 E-value: 1.39e-10
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COG5322 | COG5322 | Predicted amino acid dehydrogenase [General function prediction only]; |
173-291 | 2.37e-09 | |||||||
Predicted amino acid dehydrogenase [General function prediction only]; Pssm-ID: 444114 [Multi-domain] Cd Length: 362 Bit Score: 58.70 E-value: 2.37e-09
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aroE | PRK00258 | shikimate 5-dehydrogenase; Reviewed |
172-252 | 2.15e-08 | |||||||
shikimate 5-dehydrogenase; Reviewed Pssm-ID: 234703 [Multi-domain] Cd Length: 278 Bit Score: 55.19 E-value: 2.15e-08
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OCDMu | COG2423 | Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid ... |
184-262 | 9.49e-08 | |||||||
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid transport and metabolism]; Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family is part of the Pathway/BioSystem: Proline biosynthesis Pssm-ID: 441972 [Multi-domain] Cd Length: 322 Bit Score: 53.22 E-value: 9.49e-08
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F420_oxidored | pfam03807 | NADP oxidoreductase coenzyme F420-dependent; |
188-282 | 8.35e-06 | |||||||
NADP oxidoreductase coenzyme F420-dependent; Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 44.14 E-value: 8.35e-06
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PLN02520 | PLN02520 | bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase |
180-252 | 4.01e-05 | |||||||
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase Pssm-ID: 178135 [Multi-domain] Cd Length: 529 Bit Score: 45.91 E-value: 4.01e-05
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PRK08291 | PRK08291 | cyclodeaminase; |
172-257 | 5.39e-05 | |||||||
cyclodeaminase; Pssm-ID: 236221 [Multi-domain] Cd Length: 330 Bit Score: 44.95 E-value: 5.39e-05
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Sacchrp_dh_NADP | pfam03435 | Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ... |
185-284 | 1.05e-04 | |||||||
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase. Pssm-ID: 397480 [Multi-domain] Cd Length: 120 Bit Score: 41.42 E-value: 1.05e-04
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PRK08618 | PRK08618 | ornithine cyclodeaminase family protein; |
184-256 | 2.09e-03 | |||||||
ornithine cyclodeaminase family protein; Pssm-ID: 236313 [Multi-domain] Cd Length: 325 Bit Score: 40.04 E-value: 2.09e-03
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PRK07340 | PRK07340 | delta(1)-pyrroline-2-carboxylate reductase family protein; |
172-256 | 4.56e-03 | |||||||
delta(1)-pyrroline-2-carboxylate reductase family protein; Pssm-ID: 235996 Cd Length: 304 Bit Score: 38.79 E-value: 4.56e-03
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PRK14027 | PRK14027 | quinate/shikimate dehydrogenase (NAD+); |
184-255 | 4.57e-03 | |||||||
quinate/shikimate dehydrogenase (NAD+); Pssm-ID: 172521 [Multi-domain] Cd Length: 283 Bit Score: 38.87 E-value: 4.57e-03
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2-Hacid_dh_7 | cd12166 | Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ... |
173-280 | 8.70e-03 | |||||||
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Pssm-ID: 240643 [Multi-domain] Cd Length: 300 Bit Score: 37.95 E-value: 8.70e-03
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Blast search parameters | ||||
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