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Links from Protein

Items: 1 to 20 of 32

1.

ACT domain-containing protein

Date:
2024-09-26

Family Accession:
NF046750.1
Method:
HMM

2.

ACT domain-containing protein

The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements [1]. In mammalian phenylalanine hydroxylase the domain forms no contacts but promotes an allosteric effect despite the apparent lack of ligand binding [2]. [1]. 16987805. The ACT domain: a small molecule binding domain and its role as. a common regulatory element.. Grant GA;. J Biol Chem. 2006;281:33825-33829.. [2]. 18368466. Searching distant homologs of the regulatory ACT domain in. phenylalanine hydroxylase.. Siltberg-Liberles J, Martinez A;. Amino Acids. 2009;36:235-249. (from Pfam)

Date:
2024-08-14

Family Accession:
NF025210.5
Method:
HMM

3.

Homoserine dehydrogenase, NAD binding domain

This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model. (from Pfam)

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Molecular Function:
NADP binding (GO:0050661)
Date:
2024-08-14

Family Accession:
NF015412.5
Method:
HMM

4.

Amino acid kinase family

This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4, Swiss:P00561. Acetylglutamate kinase EC:2.7.2.8, Swiss:Q07905. Glutamate 5-kinase EC:2.7.2.11, Swiss:P07005. Uridylate kinase EC:2.7.4.-, Swiss:P29464. Carbamate kinase EC:2.7.2.2, Swiss:O96432. [1]. 10860751. The 1.5 A resolution crystal structure of the carbamate. kinase-like carbamoyl phosphate synthetase from the. hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP,. confirms that this thermostable enzyme is a carbamate kinase,. and provides insight in. Ramon-Maiques S, Marina A, Uriarte M, Fita I, Rubio V;. J Mol Biol 2000;299:463-476. (from Pfam)

Date:
2024-08-14

Family Accession:
NF012899.5
Method:
HMM

5.

Homoserine dehydrogenase

GO Terms:
Biological Process:
amino acid metabolic process (GO:0006520)
Date:
2024-08-14

Family Accession:
NF012945.5
Method:
HMM

6.
new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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new record, indexing in progress
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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
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16.
new record, indexing in progress
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17.
new record, indexing in progress
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18.
new record, indexing in progress
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19.
new record, indexing in progress
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20.

bifunctional aspartate kinase/homoserine dehydrogenase I

bifunctional aspartate kinase/homoserine dehydrogenase I catalyzes the phosphorylation of L-aspartate to 4-phospho-L-aspartate and the conversion of L-homoserine to L-aspartate-4-semialdehyde, the first and third steps of the aspartate pathway

Date:
2023-03-01

Family Accession:
11484170
Method:
Sparcle

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