Rossmann-like and DUF2520 domain-containing protein [Barnesiella viscericola]
Rossmann-like and DUF2520 domain-containing protein( domain architecture ID 11475612)
Rossmann-like and DUF2520 domain-containing protein may function as an oxidoreductase
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
COG5495 | COG5495 | Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
1-253 | 2.47e-99 | |||||
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only]; : Pssm-ID: 444246 [Multi-domain] Cd Length: 286 Bit Score: 291.72 E-value: 2.47e-99
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Name | Accession | Description | Interval | E-value | |||||
COG5495 | COG5495 | Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
1-253 | 2.47e-99 | |||||
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only]; Pssm-ID: 444246 [Multi-domain] Cd Length: 286 Bit Score: 291.72 E-value: 2.47e-99
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DUF2520 | pfam10728 | Domain of unknown function (DUF2520); This presumed domain is found C-terminal to a ... |
125-248 | 7.95e-55 | |||||
Domain of unknown function (DUF2520); This presumed domain is found C-terminal to a Rossmann-like domain suggesting that these proteins are oxidoreductases. Pssm-ID: 463182 Cd Length: 126 Bit Score: 172.64 E-value: 7.95e-55
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PRK11880 | PRK11880 | pyrroline-5-carboxylate reductase; Reviewed |
1-87 | 1.43e-06 | |||||
pyrroline-5-carboxylate reductase; Reviewed Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 48.22 E-value: 1.43e-06
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NAD_bind_Glutamyl_tRNA_reduct | cd05213 | NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
2-45 | 2.85e-03 | |||||
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: 38.40 E-value: 2.85e-03
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Name | Accession | Description | Interval | E-value | |||||
COG5495 | COG5495 | Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
1-253 | 2.47e-99 | |||||
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only]; Pssm-ID: 444246 [Multi-domain] Cd Length: 286 Bit Score: 291.72 E-value: 2.47e-99
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DUF2520 | pfam10728 | Domain of unknown function (DUF2520); This presumed domain is found C-terminal to a ... |
125-248 | 7.95e-55 | |||||
Domain of unknown function (DUF2520); This presumed domain is found C-terminal to a Rossmann-like domain suggesting that these proteins are oxidoreductases. Pssm-ID: 463182 Cd Length: 126 Bit Score: 172.64 E-value: 7.95e-55
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ProC | COG0345 | Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-83 | 1.26e-08 | |||||
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 54.30 E-value: 1.26e-08
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PRK11880 | PRK11880 | pyrroline-5-carboxylate reductase; Reviewed |
1-87 | 1.43e-06 | |||||
pyrroline-5-carboxylate reductase; Reviewed Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 48.22 E-value: 1.43e-06
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AspD | COG1712 | L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism]; |
1-78 | 2.14e-05 | |||||
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism]; Pssm-ID: 441318 [Multi-domain] Cd Length: 263 Bit Score: 44.79 E-value: 2.14e-05
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F420_oxidored | pfam03807 | NADP oxidoreductase coenzyme F420-dependent; |
6-80 | 1.19e-04 | |||||
NADP oxidoreductase coenzyme F420-dependent; Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 39.91 E-value: 1.19e-04
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PLN02688 | PLN02688 | pyrroline-5-carboxylate reductase |
1-82 | 2.32e-04 | |||||
pyrroline-5-carboxylate reductase Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 41.48 E-value: 2.32e-04
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Rossmann-like | pfam10727 | Rossmann-like domain; This family of proteins contain a Rossmann-like domain. |
5-104 | 4.58e-04 | |||||
Rossmann-like domain; This family of proteins contain a Rossmann-like domain. Pssm-ID: 287672 [Multi-domain] Cd Length: 127 Bit Score: 39.07 E-value: 4.58e-04
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Shikimate_DH | pfam01488 | Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ... |
2-58 | 1.04e-03 | |||||
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: 38.32 E-value: 1.04e-03
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NAD_bind_Glutamyl_tRNA_reduct | cd05213 | NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
2-45 | 2.85e-03 | |||||
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: 38.40 E-value: 2.85e-03
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hemA | PRK00045 | glutamyl-tRNA reductase; Reviewed |
2-58 | 4.40e-03 | |||||
glutamyl-tRNA reductase; Reviewed Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 37.86 E-value: 4.40e-03
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Blast search parameters | ||||
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