Protein Family Models for Protein (Select 446521137) - Protein Family Models

Select item 4304421.

Semialdehyde dehydrogenase, dimerisation domain

This entry represents the dimerisation domain found in N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) and related sequences not included in Pfam:PF02774 [1-3]. Paper describing PDB structure 2cvo. [1]. 16240442. Crystal structure of putative N-acetyl-gamma-glutamyl-phosphate reductase (AK071544) from rice (Oryza sativa). Nonaka T, Kita A, Miura-Ohnuma J, Katoh E, Inagaki N, Yamazaki T, Miki K;. Proteins. 2005;61:1137-1140. Paper describing PDB structure 2i3a. [2]. 17316682. Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase from Mycobacterium tuberculosis in complex with NADP(+). Cherney LT, Cherney MM, Garen CR, Niu C, Moradian F, James MN;. J Mol Biol. 2007;367:1357-1369. Paper describing PDB structure 5ein. [3]. 26966182. Crystal Structure of the LysY.LysW Complex from Thermus thermophilus. Shimizu T, Tomita T, Kuzuyama T, Nishiyama M;. J Biol Chem. 2016;291:9948-9959. (from Pfam)

Date:: 2024-10-16

Family Accession:: NF046896.1
Method:: HMM

Select item 4141642.

Asd/ArgC dimerization domain-containing protein

This Pfam domain model identifies C-terminal domains of N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), aspartate-semialdehyde dehydrogenase (Asd) and a few other, less common enzymes.

GO Terms:

Biological Process:: amino acid biosynthetic process (GO:0008652)

Molecular Function:: oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor (GO:0016620)

Molecular Function:: protein dimerization activity (GO:0046983)

Date:: 2024-10-16

Family Accession:: NF014793.5
Method:: HMM

Select item 4116793.

Semialdehyde dehydrogenase, NAD binding domain

This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase [1]. 10369777. Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis. Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R;. J Mol Biol 1999;289:991-1002. (from Pfam)

GO Terms:

Molecular Function:: oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor (GO:0016620)

Molecular Function:: NAD binding (GO:0051287)

Date:: 2024-10-16

Family Accession:: NF013298.5
Method:: HMM

Select item 3897804.

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Select item 3888085.

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Family Accession:

Select item 3482746.

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Family Accession:

Select item 3477927.

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Family Accession:

Select item 3394888.

N-acetyl-gamma-glutamyl-phosphate reductase

N-acetyl-gamma-glutamyl-phosphate reductase catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to N-acetyl-L-glutamate 5-semialdehyde, as part of the L-arginine biosynthesis

Date:: 2024-08-22

Family Accession:: 11414156
Method:: Sparcle

Select item 1421209.

N-acetyl-gamma-glutamyl-phosphate reductase

This HMM represents the more common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and the gap architecture in a multiple sequence alignment. Bacterial members of this family tend to be found within Arg biosynthesis operons.

Gene:: argC

GO Terms:

Molecular Function:: N-acetyl-gamma-glutamyl-phosphate reductase activity (GO:0003942)

Biological Process:: L-arginine biosynthetic process (GO:0006526)

Biological Process:: ornithine biosynthetic process (GO:0006592)

Molecular Function:: NADP+ binding (GO:0070401)

Date:: 2024-06-04

Family Accession:: TIGR01850.1
Method:: HMM

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