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Links from Protein

Items: 12

1.

thiamine pyrophosphate-dependent enzyme

GO Terms:
Molecular Function:
catalytic activity (GO:0003824)
Molecular Function:
thiamine pyrophosphate binding (GO:0030976)
Date:
2024-08-14

Family Accession:
NF014794.5
Method:
HMM

2.

thiamine pyrophosphate-binding protein

GO Terms:
Molecular Function:
thiamine pyrophosphate binding (GO:0030976)
Date:
2024-08-14

Family Accession:
NF014795.5
Method:
HMM

3.

Thiamine pyrophosphate enzyme, central domain

The central domain of TPP enzymes contains a 2-fold Rossman fold. [1]. 8604141. Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution. Arjunan P, Umland T, Dyda F, Swaminathan S, Furey W, Sax M, Farrenkopf B, Gao Y, Zhang D, Jordan F;. J Mol Biol 1996;256:590-600. (from Pfam)

GO Terms:
Molecular Function:
magnesium ion binding (GO:0000287)
Molecular Function:
thiamine pyrophosphate binding (GO:0030976)
Date:
2024-10-16

Family Accession:
NF012431.5
Method:
HMM

4.
new record, indexing in progress
Family Accession:
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.

acetolactate synthase 3 large subunit

acetolactate synthase 3 large subunit is the catalytic subunit of the dimeric enzyme acetolactate synthase, which catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, the precursor of the branched chain amino acids, valine, isoleucine, and leucine

Date:
2019-07-30

Family Accession:
11482273
Method:
Sparcle

11.

acetolactate synthase 3 large subunit

GO Terms:
Molecular Function:
magnesium ion binding (GO:0000287)
Molecular Function:
acetolactate synthase activity (GO:0003984)
Biological Process:
branched-chain amino acid biosynthetic process (GO:0009082)
Molecular Function:
thiamine pyrophosphate binding (GO:0030976)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Date:
2021-09-20

Family Accession:
NF005058.0
Method:
HMM

12.

biosynthetic-type acetolactate synthase large subunit

Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed.

Gene:
ilvB
GO Terms:
Molecular Function:
magnesium ion binding (GO:0000287)
Molecular Function:
acetolactate synthase activity (GO:0003984)
Biological Process:
branched-chain amino acid biosynthetic process (GO:0009082)
Molecular Function:
thiamine pyrophosphate binding (GO:0030976)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Date:
2024-05-15

Family Accession:
TIGR00118.1
Method:
HMM

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