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Links from Protein

Items: 12

1.

AHAS-like ACT domain

This entry represents the ACT domain found at the N-terminal of acetohydroxyacid synthase isozyme III from Escherichia coli and similar sequences. Paper describing PDB structure 1psd. [1]. 7719856. The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Schuller DJ, Grant GA, Banaszak LJ;. Nat Struct Biol 1995;2:69-76. Paper describing PDB structure 1sc6. [2]. 15035616. Multiconformational states in phosphoglycerate dehydrogenase. Bell JK, Grant GA, Banaszak LJ;. Biochemistry. 2004;43:3450-3458. Paper describing PDB structure 1yba. [3]. 15823035. Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase. Thompson JR, Bell JK, Bratt J, Grant GA, Banaszak LJ;. Biochemistry. 2005;44:5763-5773. Paper describing PDB structure 2f1f. [4]. 16458324. Structure of the regulatory subunit of acetohydroxyacid synthase isozyme III from Escherichia coli. Kaplun A, Vyazmensky M, Zherdev Y, Belenky I, Slutzker A, Mendel S, Barak Z, Chipman DM, Shaanan B;. J Mol Biol. 2006;357:951-963. Paper describing PDB structure 2fgc. [5]. 17586771. Crystal structures of TM0549 and NE1324--two orthologs of E. coli AHAS isozyme III small regulatory subunit. Petkowski JJ, Chruszcz M, Zimmerman MD, Zheng H, Skarina T, Onopriyenko O, Cymborowski MT, Koclega KD, Savchenko A, Edwards A, Minor W;. Protein Sci. 2007;16:1360-1367. (from Pfam)

Date:
2024-10-16
Family Accession:
NF046878.1
Method:
HMM
2.

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
3.

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
4.

D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain

This family represents the largest portion of the catalytic domain of 2-hydroxyacid dehydrogenases as the NAD binding domain is inserted within the structural domain. [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:
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616)
Molecular Function:
NAD binding (GO:0051287)
Date:
2024-10-16
Family Accession:
NF012607.5
Method:
HMM
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.

phosphoglycerate dehydrogenase

Catalyzes the formation of 3-phosphonooxypyruvate from 3-phospho-D-glycerate in serine biosynthesis

Gene:
serA
GO Terms:
Molecular Function:
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (GO:0016616)
Molecular Function:
NAD binding (GO:0051287)
Date:
2021-07-30
Family Accession:
NF008759.0
Method:
HMM
12.

phosphoglycerate dehydrogenase

phosphoglycerate dehydrogenase catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, the first step in serine biosynthesis

Date:
2023-03-14
Family Accession:
11485509
Method:
Sparcle
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