3-hydroxyisobutyrate dehydrogenase, mitochondrial isoform 1 precursor [Homo sapiens]
Protein Classification
3-hydroxyisobutyrate dehydrogenase( domain architecture ID 11493045)
3-hydroxyisobutyrate dehydrogenase (HIBADH) catalyzes the conversion from 3-hydroxy-2-methylpropanoate and NAD(+) to 2-methyl-3-oxopropanoate and NADH
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| HIBADH | TIGR01692 | 3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ... |
44-331 | 0e+00 | |||||
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that catalyzes the NAD+-dependent oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde of the valine catabolism pathway. In Pseudomonas aeruginosa, 3-hydroxyisobutyrate dehydrogenase (mmsB) is co-induced with methylmalonate-semialdehyde dehydrogenase (mmsA) when grown on medium containing valine as the sole carbon source. The positive transcriptional regulator of this operon (mmsR) is located upstream of these genes and has been identified as a member of the XylS/AraC family of transcriptional regulators. 3-hydroxyisobutyrate dehydrogenase shares high sequence homology to the characterized 3-hydroxyisobutyrate dehydrogenase from rat liver with conservation of proposed NAD+ binding residues at the N-terminus (G-8,10,13,24 and D-31). This enzyme belongs to the 3-hydroxyacid dehydrogenase family, sharing a common evolutionary origin and enzymatic mechanism with 6-phosphogluconate. HIBADH exhibits sequence similarity to the NAD binding domain of 6-phosphogluconate dehydrogenase above trusted (pfam03446). [Energy metabolism, Amino acids and amines] : Pssm-ID: 130753 [Multi-domain] Cd Length: 288 Bit Score: 512.42 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||
| HIBADH | TIGR01692 | 3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ... |
44-331 | 0e+00 | |||||
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that catalyzes the NAD+-dependent oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde of the valine catabolism pathway. In Pseudomonas aeruginosa, 3-hydroxyisobutyrate dehydrogenase (mmsB) is co-induced with methylmalonate-semialdehyde dehydrogenase (mmsA) when grown on medium containing valine as the sole carbon source. The positive transcriptional regulator of this operon (mmsR) is located upstream of these genes and has been identified as a member of the XylS/AraC family of transcriptional regulators. 3-hydroxyisobutyrate dehydrogenase shares high sequence homology to the characterized 3-hydroxyisobutyrate dehydrogenase from rat liver with conservation of proposed NAD+ binding residues at the N-terminus (G-8,10,13,24 and D-31). This enzyme belongs to the 3-hydroxyacid dehydrogenase family, sharing a common evolutionary origin and enzymatic mechanism with 6-phosphogluconate. HIBADH exhibits sequence similarity to the NAD binding domain of 6-phosphogluconate dehydrogenase above trusted (pfam03446). [Energy metabolism, Amino acids and amines] Pssm-ID: 130753 [Multi-domain] Cd Length: 288 Bit Score: 512.42 E-value: 0e+00
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| MmsB | COG2084 | 3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
39-330 | 1.79e-110 | |||||
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism]; Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 322.84 E-value: 1.79e-110
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| garR | PRK11559 | tartronate semialdehyde reductase; Provisional |
42-329 | 6.10e-70 | |||||
tartronate semialdehyde reductase; Provisional Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 219.92 E-value: 6.10e-70
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| NAD_binding_2 | pfam03446 | NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
42-200 | 2.33e-60 | |||||
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: 190.37 E-value: 2.33e-60
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| LDH_like | cd01619 | D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ... |
1-133 | 7.73e-05 | |||||
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. 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. Pssm-ID: 240620 [Multi-domain] Cd Length: 323 Bit Score: 43.83 E-value: 7.73e-05
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| Name | Accession | Description | Interval | E-value | |||||
| HIBADH | TIGR01692 | 3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ... |
44-331 | 0e+00 | |||||
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that catalyzes the NAD+-dependent oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde of the valine catabolism pathway. In Pseudomonas aeruginosa, 3-hydroxyisobutyrate dehydrogenase (mmsB) is co-induced with methylmalonate-semialdehyde dehydrogenase (mmsA) when grown on medium containing valine as the sole carbon source. The positive transcriptional regulator of this operon (mmsR) is located upstream of these genes and has been identified as a member of the XylS/AraC family of transcriptional regulators. 3-hydroxyisobutyrate dehydrogenase shares high sequence homology to the characterized 3-hydroxyisobutyrate dehydrogenase from rat liver with conservation of proposed NAD+ binding residues at the N-terminus (G-8,10,13,24 and D-31). This enzyme belongs to the 3-hydroxyacid dehydrogenase family, sharing a common evolutionary origin and enzymatic mechanism with 6-phosphogluconate. HIBADH exhibits sequence similarity to the NAD binding domain of 6-phosphogluconate dehydrogenase above trusted (pfam03446). [Energy metabolism, Amino acids and amines] Pssm-ID: 130753 [Multi-domain] Cd Length: 288 Bit Score: 512.42 E-value: 0e+00
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| MmsB | COG2084 | 3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
39-330 | 1.79e-110 | |||||
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism]; Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 322.84 E-value: 1.79e-110
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| garR | PRK11559 | tartronate semialdehyde reductase; Provisional |
42-329 | 6.10e-70 | |||||
tartronate semialdehyde reductase; Provisional Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 219.92 E-value: 6.10e-70
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| NAD_binding_2 | pfam03446 | NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
42-200 | 2.33e-60 | |||||
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: 190.37 E-value: 2.33e-60
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| tartro_sem_red | TIGR01505 | 2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ... |
42-330 | 4.08e-58 | |||||
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism. Pssm-ID: 130569 [Multi-domain] Cd Length: 291 Bit Score: 189.33 E-value: 4.08e-58
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| PRK15461 | PRK15461 | sulfolactaldehyde 3-reductase; |
42-331 | 6.05e-50 | |||||
sulfolactaldehyde 3-reductase; Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 168.50 E-value: 6.05e-50
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| PRK15059 | PRK15059 | 2-hydroxy-3-oxopropionate reductase; |
42-330 | 4.71e-43 | |||||
2-hydroxy-3-oxopropionate reductase; Pssm-ID: 185019 [Multi-domain] Cd Length: 292 Bit Score: 150.17 E-value: 4.71e-43
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| PLN02858 | PLN02858 | fructose-bisphosphate aldolase |
42-326 | 3.14e-42 | |||||
fructose-bisphosphate aldolase Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 156.55 E-value: 3.14e-42
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| PLN02858 | PLN02858 | fructose-bisphosphate aldolase |
37-308 | 7.39e-36 | |||||
fructose-bisphosphate aldolase Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 138.06 E-value: 7.39e-36
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| NAD_binding_11 | pfam14833 | NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ... |
203-330 | 9.29e-33 | |||||
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidized to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure. Pssm-ID: 434252 [Multi-domain] Cd Length: 122 Bit Score: 118.01 E-value: 9.29e-33
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| YqeC | COG1023 | 6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]; |
42-229 | 1.44e-21 | |||||
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]; Pssm-ID: 440646 [Multi-domain] Cd Length: 300 Bit Score: 92.85 E-value: 1.44e-21
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| PRK09599 | PRK09599 | NADP-dependent phosphogluconate dehydrogenase; |
42-209 | 5.71e-19 | |||||
NADP-dependent phosphogluconate dehydrogenase; Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 85.57 E-value: 5.71e-19
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| ProC | COG0345 | Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
42-100 | 4.97e-07 | |||||
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: 50.45 E-value: 4.97e-07
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| PRK11880 | PRK11880 | pyrroline-5-carboxylate reductase; Reviewed |
38-100 | 1.91e-05 | |||||
pyrroline-5-carboxylate reductase; Reviewed Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 45.52 E-value: 1.91e-05
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| LDH_like | cd01619 | D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ... |
1-133 | 7.73e-05 | |||||
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. 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. Pssm-ID: 240620 [Multi-domain] Cd Length: 323 Bit Score: 43.83 E-value: 7.73e-05
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| PTDH | cd12157 | Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ... |
7-130 | 2.53e-04 | |||||
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. 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. Pssm-ID: 240634 [Multi-domain] Cd Length: 318 Bit Score: 42.27 E-value: 2.53e-04
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| PGDH_like_2 | cd12172 | Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ... |
7-130 | 2.86e-04 | |||||
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as 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. Many, not all, members of this family are dimeric. Pssm-ID: 240649 [Multi-domain] Cd Length: 306 Bit Score: 42.09 E-value: 2.86e-04
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| PTZ00142 | PTZ00142 | 6-phosphogluconate dehydrogenase; Provisional |
42-213 | 5.44e-04 | |||||
6-phosphogluconate dehydrogenase; Provisional Pssm-ID: 240287 [Multi-domain] Cd Length: 470 Bit Score: 41.70 E-value: 5.44e-04
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| E1_enzyme_family | cd01483 | Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ... |
42-175 | 1.46e-03 | |||||
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. Pssm-ID: 238760 [Multi-domain] Cd Length: 143 Bit Score: 38.40 E-value: 1.46e-03
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| 2-Hacid_dh_14 | cd12179 | Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ... |
38-97 | 5.83e-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: 240656 [Multi-domain] Cd Length: 306 Bit Score: 38.04 E-value: 5.83e-03
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