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Links from Protein

Items: 16

1.

NAD-binding protein

3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidised 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 [1]. [1]. 16126223. Crystal structure of novel NADP-dependent 3-hydroxyisobutyrate dehydrogenase from Thermus thermophilus HB8. Lokanath NK, Ohshima N, Takio K, Shiromizu I, Kuroishi C, Okazaki N, Kuramitsu S, Yokoyama S, Miyano M, Kunishima N;. J Mol Biol. 2005;352:905-917. (from Pfam)

GO Terms:
Molecular Function:
NAD binding (GO:0051287)
Date:
2024-10-16
Family Accession:
NF026183.5
Method:
HMM
2.

Acetohydroxy acid isomeroreductase, NADPH-binding domain

Acetohydroxy acid isomeroreductase catalyses 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, Pfam:PF01450. [1]. 9218783. The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution. Biou V, Dumas R, Cohen-Addad C, Douce R, Job D, Pebay-Peyroula E;. EMBO J 1997;16:3405-3415. [2]. 16322583. The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution. Tyagi R, Duquerroy S, Navaza J, Guddat LW, Duggleby RG;. Protein Sci. 2005;14:3089-3100. [3]. 19362563. Conformational changes in a plant ketol-acid reductoisomerase upon Mg(2+) and NADPH binding as revealed by two crystal structures. Leung EW, Guddat LW;. J Mol Biol. 2009;389:167-182. (from Pfam)

Date:
2024-10-16
Family Accession:
NF019603.5
Method:
HMM
3.

NAD(P)-binding domain-containing protein

Date:
2024-08-14
Family Accession:
NF015747.5
Method:
HMM
4.

NAD(P)-binding domain-containing protein

The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold. (from Pfam)

GO Terms:
Molecular Function:
NADP binding (GO:0050661)
Date:
2024-08-14
Family Accession:
NF015411.5
Method:
HMM
5.

NAD(P)-dependent oxidoreductase

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 Pfam:PF00389. [1]. 9126843. Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution. Dengler U, Niefind K, Kiess M, Schomburg D;. J Mol Biol 1997;267:640-660. (from Pfam)

GO Terms:
Molecular Function:
NAD binding (GO:0051287)
Date:
2024-10-16
Family Accession:
NF014841.5
Method:
HMM
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.
new record, indexing in progress
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12.
new record, indexing in progress
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13.
new record, indexing in progress
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14.
new record, indexing in progress
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15.
new record, indexing in progress
Family Accession:
16.

NAD(P)-dependent oxidoreductase

NAD(P)-dependent oxidoreductase similar to 3-hydroxyisobutyrate dehydrogenase, L-threonate dehydrogenase, 2-(hydroxymethyl)glutarate dehydrogenase, and glyoxylate/succinic semialdehyde reductase

Date:
2024-04-25
Family Accession:
11449905
Method:
Sparcle
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