Gdh, partial [Streptococcus suis]
Protein Classification
dehydrogenase family protein( domain architecture ID 1001438)
dehydrogenase family protein such as glutamate dehydrogenase, which catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate using NAD+ and or NADP+ as cofactor
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| PRK09414 super family | cl32367 | NADP-specific glutamate dehydrogenase; |
1-230 | 1.77e-179 | ||||
NADP-specific glutamate dehydrogenase; The actual alignment was detected with superfamily member PRK09414: Pssm-ID: 181834 [Multi-domain] Cd Length: 445 Bit Score: 499.26 E-value: 1.77e-179
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| Name | Accession | Description | Interval | E-value | ||||
| PRK09414 | PRK09414 | NADP-specific glutamate dehydrogenase; |
1-230 | 1.77e-179 | ||||
NADP-specific glutamate dehydrogenase; Pssm-ID: 181834 [Multi-domain] Cd Length: 445 Bit Score: 499.26 E-value: 1.77e-179
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| GdhA | COG0334 | Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate ... |
1-229 | 5.46e-129 | ||||
Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate dehydrogenase/leucine dehydrogenase is part of the Pathway/BioSystem: Glutamine biosynthesis Pssm-ID: 440103 [Multi-domain] Cd Length: 411 Bit Score: 370.16 E-value: 5.46e-129
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| ELFV_dehydrog_N | pfam02812 | Glu/Leu/Phe/Val dehydrogenase, dimerization domain; |
1-120 | 2.18e-64 | ||||
Glu/Leu/Phe/Val dehydrogenase, dimerization domain; Pssm-ID: 460706 [Multi-domain] Cd Length: 129 Bit Score: 195.69 E-value: 2.18e-64
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| NAD_bind_2_Glu_DH | cd05313 | NAD(P) binding domain of glutamate dehydrogenase, subgroup 2; Amino acid dehydrogenase (DH) is ... |
130-230 | 1.64e-56 | ||||
NAD(P) binding domain of glutamate dehydrogenase, subgroup 2; 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+. Glutamate DH is a multidomain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia asimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. 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: 133455 [Multi-domain] Cd Length: 254 Bit Score: 180.12 E-value: 1.64e-56
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| Name | Accession | Description | Interval | E-value | ||||
| PRK09414 | PRK09414 | NADP-specific glutamate dehydrogenase; |
1-230 | 1.77e-179 | ||||
NADP-specific glutamate dehydrogenase; Pssm-ID: 181834 [Multi-domain] Cd Length: 445 Bit Score: 499.26 E-value: 1.77e-179
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| PTZ00079 | PTZ00079 | NADP-specific glutamate dehydrogenase; Provisional |
1-230 | 8.54e-141 | ||||
NADP-specific glutamate dehydrogenase; Provisional Pssm-ID: 185433 [Multi-domain] Cd Length: 454 Bit Score: 401.80 E-value: 8.54e-141
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| GdhA | COG0334 | Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate ... |
1-229 | 5.46e-129 | ||||
Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate dehydrogenase/leucine dehydrogenase is part of the Pathway/BioSystem: Glutamine biosynthesis Pssm-ID: 440103 [Multi-domain] Cd Length: 411 Bit Score: 370.16 E-value: 5.46e-129
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| PRK14030 | PRK14030 | glutamate dehydrogenase; Provisional |
1-230 | 2.15e-123 | ||||
glutamate dehydrogenase; Provisional Pssm-ID: 184463 [Multi-domain] Cd Length: 445 Bit Score: 357.22 E-value: 2.15e-123
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| PRK14031 | PRK14031 | NADP-specific glutamate dehydrogenase; |
2-229 | 1.80e-113 | ||||
NADP-specific glutamate dehydrogenase; Pssm-ID: 184464 [Multi-domain] Cd Length: 444 Bit Score: 331.90 E-value: 1.80e-113
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| ELFV_dehydrog_N | pfam02812 | Glu/Leu/Phe/Val dehydrogenase, dimerization domain; |
1-120 | 2.18e-64 | ||||
Glu/Leu/Phe/Val dehydrogenase, dimerization domain; Pssm-ID: 460706 [Multi-domain] Cd Length: 129 Bit Score: 195.69 E-value: 2.18e-64
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| NAD_bind_2_Glu_DH | cd05313 | NAD(P) binding domain of glutamate dehydrogenase, subgroup 2; Amino acid dehydrogenase (DH) is ... |
130-230 | 1.64e-56 | ||||
NAD(P) binding domain of glutamate dehydrogenase, subgroup 2; 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+. Glutamate DH is a multidomain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia asimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. 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: 133455 [Multi-domain] Cd Length: 254 Bit Score: 180.12 E-value: 1.64e-56
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| PLN02477 | PLN02477 | glutamate dehydrogenase |
6-210 | 3.97e-49 | ||||
glutamate dehydrogenase Pssm-ID: 178095 [Multi-domain] Cd Length: 410 Bit Score: 165.70 E-value: 3.97e-49
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| ELFV_dehydrog | pfam00208 | Glutamate/Leucine/Phenylalanine/Valine dehydrogenase; |
137-229 | 1.86e-44 | ||||
Glutamate/Leucine/Phenylalanine/Valine dehydrogenase; Pssm-ID: 425526 [Multi-domain] Cd Length: 240 Bit Score: 148.82 E-value: 1.86e-44
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| NAD_bind_1_Glu_DH | cd01076 | NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is ... |
137-220 | 1.17e-21 | ||||
NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; 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+. Glutamate DH is a multidomain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia assimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. 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: 133445 [Multi-domain] Cd Length: 227 Bit Score: 89.13 E-value: 1.17e-21
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| NAD_bind_Glu_Leu_Phe_Val | cd05211 | NAD(P) binding domain of glutamate dehydrogenase, leucine dehydrogenase, phenylalanine ... |
145-221 | 1.25e-11 | ||||
NAD(P) binding domain of glutamate dehydrogenase, 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 NAD(P)+. This subfamily includes glutamate, leucine, phenylalanine, and valine DHs. Glutamate DH is a multi-domain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia assimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. As in other NAD+-dependent DHs, monomers in this family have 2 domains separated by a deep cleft. Here the c-terminal domain contains a modified NAD-binding Rossmann fold with 7 rather than the usual 6 beta strands and one strand anti-parrallel to the others. 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: 133450 [Multi-domain] Cd Length: 217 Bit Score: 61.80 E-value: 1.25e-11
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| Zn_ADH_like2 | cd08264 | Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ... |
156-229 | 3.82e-05 | ||||
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase family. However, this subgroup does not contain the characteristic catalytic zinc site. Also, it contains an atypical structural zinc-binding pattern: DxxCxxCxxxxxxxC. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. Pssm-ID: 176225 [Multi-domain] Cd Length: 325 Bit Score: 43.88 E-value: 3.82e-05
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| Qor | COG0604 | NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ... |
144-197 | 6.78e-04 | ||||
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only]; Pssm-ID: 440369 [Multi-domain] Cd Length: 322 Bit Score: 40.13 E-value: 6.78e-04
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| PRK06270 | PRK06270 | homoserine dehydrogenase; Provisional |
184-220 | 1.38e-03 | ||||
homoserine dehydrogenase; Provisional Pssm-ID: 235763 [Multi-domain] Cd Length: 341 Bit Score: 39.08 E-value: 1.38e-03
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| MDR_like_2 | cd05289 | alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ... |
166-210 | 2.86e-03 | ||||
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. Pssm-ID: 176191 [Multi-domain] Cd Length: 309 Bit Score: 37.93 E-value: 2.86e-03
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| NAD_bind_Leu_Phe_Val_DH | cd01075 | NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ... |
146-200 | 5.22e-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: 36.80 E-value: 5.22e-03
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| MDR6 | cd08272 | Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
168-211 | 7.86e-03 | ||||
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Pssm-ID: 176233 [Multi-domain] Cd Length: 326 Bit Score: 36.77 E-value: 7.86e-03
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| PRK13771 | PRK13771 | putative alcohol dehydrogenase; Provisional |
166-199 | 8.94e-03 | ||||
putative alcohol dehydrogenase; Provisional Pssm-ID: 184316 [Multi-domain] Cd Length: 334 Bit Score: 36.55 E-value: 8.94e-03
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| MDR | cd05188 | Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
145-199 | 9.89e-03 | ||||
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc. Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 36.15 E-value: 9.89e-03
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| Blast search parameters | ||||
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