MULTISPECIES: ketol-acid reductoisomerase [Staphylococcus]
Protein Classification
NADP-dependent ketol-acid reductoisomerase( domain architecture ID 11481043)
NADP-dependent ketol-acid reductoisomerase catalyzes the conversion of 2-(S)-acetolactate (2SAL) into (R)-dihydroxyisovalerate (RDHIV), the second step in the biosynthesis of the branched-chain amino acids (BCAAs) valine, leucine and isoleucine
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| PRK05479 | PRK05479 | ketol-acid reductoisomerase; Provisional |
1-329 | 0e+00 | ||||||
ketol-acid reductoisomerase; Provisional : Pssm-ID: 235491 [Multi-domain] Cd Length: 330 Bit Score: 639.83 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| PRK05479 | PRK05479 | ketol-acid reductoisomerase; Provisional |
1-329 | 0e+00 | ||||||
ketol-acid reductoisomerase; Provisional Pssm-ID: 235491 [Multi-domain] Cd Length: 330 Bit Score: 639.83 E-value: 0e+00
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| IlvC | COG0059 | Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ... |
1-327 | 0e+00 | ||||||
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis Pssm-ID: 439829 [Multi-domain] Cd Length: 328 Bit Score: 619.77 E-value: 0e+00
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| ilvC | TIGR00465 | ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ... |
15-328 | 1.81e-152 | ||||||
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine biosynthetic pathway [Amino acid biosynthesis, Pyruvate family] Pssm-ID: 273093 [Multi-domain] Cd Length: 314 Bit Score: 430.65 E-value: 1.81e-152
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| IlvN | pfam07991 | Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ... |
14-177 | 1.59e-105 | ||||||
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, pfam01450. Pssm-ID: 285265 Cd Length: 165 Bit Score: 305.62 E-value: 1.59e-105
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| PGDH_1 | cd12155 | Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ... |
6-81 | 1.86e-05 | ||||||
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate Dehydrogenase (PGDH) catalyzes the NAD-dependent conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first step in serine biosynthesis. Over-expression of PGDH has been implicated as supporting proliferation of certain breast cancers, while PGDH deficiency is linked to defects in mammalian central nervous system development. PGDH is a member of the 2-hydroxyacid dehydrogenase family, enzymes that 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: 240632 [Multi-domain] Cd Length: 314 Bit Score: 45.65 E-value: 1.86e-05
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| AdoHcyase_NAD | smart00997 | S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
15-76 | 2.49e-04 | ||||||
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 40.90 E-value: 2.49e-04
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| Name | Accession | Description | Interval | E-value | ||||||
| PRK05479 | PRK05479 | ketol-acid reductoisomerase; Provisional |
1-329 | 0e+00 | ||||||
ketol-acid reductoisomerase; Provisional Pssm-ID: 235491 [Multi-domain] Cd Length: 330 Bit Score: 639.83 E-value: 0e+00
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| IlvC | COG0059 | Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ... |
1-327 | 0e+00 | ||||||
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis Pssm-ID: 439829 [Multi-domain] Cd Length: 328 Bit Score: 619.77 E-value: 0e+00
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| ilvC | TIGR00465 | ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine ... |
15-328 | 1.81e-152 | ||||||
ketol-acid reductoisomerase; This is the second enzyme in the parallel isoleucine-valine biosynthetic pathway [Amino acid biosynthesis, Pyruvate family] Pssm-ID: 273093 [Multi-domain] Cd Length: 314 Bit Score: 430.65 E-value: 1.81e-152
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| PRK13403 | PRK13403 | ketol-acid reductoisomerase; Provisional |
5-328 | 4.92e-145 | ||||||
ketol-acid reductoisomerase; Provisional Pssm-ID: 106361 [Multi-domain] Cd Length: 335 Bit Score: 412.60 E-value: 4.92e-145
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| IlvN | pfam07991 | Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ... |
14-177 | 1.59e-105 | ||||||
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, pfam01450. Pssm-ID: 285265 Cd Length: 165 Bit Score: 305.62 E-value: 1.59e-105
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| IlvC | pfam01450 | Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase ... |
190-321 | 5.54e-80 | ||||||
Acetohydroxy acid isomeroreductase, catalytic domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. Pssm-ID: 460215 [Multi-domain] Cd Length: 138 Bit Score: 239.68 E-value: 5.54e-80
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| PRK05225 | PRK05225 | ketol-acid reductoisomerase; Validated |
13-307 | 1.66e-42 | ||||||
ketol-acid reductoisomerase; Validated Pssm-ID: 235368 [Multi-domain] Cd Length: 487 Bit Score: 153.19 E-value: 1.66e-42
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| NAD_binding_2 | pfam03446 | NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
19-99 | 2.25e-06 | ||||||
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold. Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 46.69 E-value: 2.25e-06
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| COG2085 | COG2085 | Predicted dinucleotide-binding enzyme [General function prediction only]; |
20-81 | 4.04e-06 | ||||||
Predicted dinucleotide-binding enzyme [General function prediction only]; Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 46.70 E-value: 4.04e-06
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| PGDH_1 | cd12155 | Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ... |
6-81 | 1.86e-05 | ||||||
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate Dehydrogenase (PGDH) catalyzes the NAD-dependent conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first step in serine biosynthesis. Over-expression of PGDH has been implicated as supporting proliferation of certain breast cancers, while PGDH deficiency is linked to defects in mammalian central nervous system development. PGDH is a member of the 2-hydroxyacid dehydrogenase family, enzymes that 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: 240632 [Multi-domain] Cd Length: 314 Bit Score: 45.65 E-value: 1.86e-05
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| 2-Hacid_dh_6 | cd12165 | Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ... |
4-81 | 2.64e-05 | ||||||
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: 240642 [Multi-domain] Cd Length: 314 Bit Score: 45.31 E-value: 2.64e-05
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| MmsB | COG2084 | 3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
18-82 | 2.90e-05 | ||||||
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism]; Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 45.11 E-value: 2.90e-05
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| 2-Hacid_dh_C | pfam02826 | D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ... |
15-81 | 3.48e-05 | ||||||
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389. Pssm-ID: 427007 [Multi-domain] Cd Length: 178 Bit Score: 43.64 E-value: 3.48e-05
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| AdoHcyase_NAD | smart00997 | S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
15-76 | 2.49e-04 | ||||||
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 40.90 E-value: 2.49e-04
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| 2-Hacid_dh_7 | cd12166 | Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ... |
12-81 | 3.58e-04 | ||||||
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: 41.81 E-value: 3.58e-04
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| SAHH | cd00401 | S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ... |
17-75 | 6.12e-04 | ||||||
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+. Pssm-ID: 240619 [Multi-domain] Cd Length: 402 Bit Score: 41.29 E-value: 6.12e-04
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| 2-Hacid_dh_11 | cd12175 | Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ... |
14-81 | 1.33e-03 | ||||||
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 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: 240652 [Multi-domain] Cd Length: 311 Bit Score: 39.86 E-value: 1.33e-03
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| 2-Hacid_dh_1 | cd05300 | Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ... |
15-81 | 1.37e-03 | ||||||
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 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 subdomains 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. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Pssm-ID: 240625 [Multi-domain] Cd Length: 313 Bit Score: 39.81 E-value: 1.37e-03
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| NAD_bind_Leu_Phe_Val_DH | cd01075 | NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ... |
11-75 | 1.62e-03 | ||||||
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. 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 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: 133444 Cd Length: 200 Bit Score: 39.11 E-value: 1.62e-03
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| PRK05476 | PRK05476 | S-adenosyl-L-homocysteine hydrolase; Provisional |
17-76 | 1.82e-03 | ||||||
S-adenosyl-L-homocysteine hydrolase; Provisional Pssm-ID: 235488 [Multi-domain] Cd Length: 425 Bit Score: 39.72 E-value: 1.82e-03
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| formate_dh_like | cd05198 | Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ... |
15-81 | 3.86e-03 | ||||||
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that 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. 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. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. 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, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Pssm-ID: 240622 [Multi-domain] Cd Length: 302 Bit Score: 38.38 E-value: 3.86e-03
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| F420_oxidored | pfam03807 | NADP oxidoreductase coenzyme F420-dependent; |
21-81 | 5.07e-03 | ||||||
NADP oxidoreductase coenzyme F420-dependent; Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 35.67 E-value: 5.07e-03
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