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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:
2024-08-14

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 AlsS

Gene:
alsS
GO Terms:
Molecular Function:
magnesium ion binding (GO:0000287)
Molecular Function:
acetolactate synthase activity (GO:0003984)
Molecular Function:
thiamine pyrophosphate binding (GO:0030976)
Biological Process:
butanediol metabolic process (GO:0034077)
Date:
2021-08-30

Family Accession:
NF006378.0
Method:
HMM

11.

acetolactate synthase

acetolactate synthase (ALS) catalyzes the first step in the synthesis of the branched-chain amino acids (valine, leucine, and isoleucine)

Date:
2019-05-08

Family Accession:
11483380
Method:
Sparcle

12.

acetolactate synthase AlsS

Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (PF00205, PF02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family.

Gene:
alsS
GO Terms:
Molecular Function:
magnesium ion binding (GO:0000287)
Molecular Function:
acetolactate synthase activity (GO:0003984)
Molecular Function:
thiamine pyrophosphate binding (GO:0030976)
Biological Process:
butanediol metabolic process (GO:0034077)
Date:
2024-05-15

Family Accession:
TIGR02418.1
Method:
HMM

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