Arginine N-succinyltransferase beta subunit; Arginine N-succinyltransferase EC:2.3.1.109 catalyzes the transfer of succinyl-CoA to arginine to produce succinyl-arginine. This is the first step in arginine catabolism by the arginine succinyltransferase pathway.
The actual alignment was detected with superfamily member TIGR03245:
Pssm-ID: 448257 Cd Length: 336 Bit Score: 550.18 E-value: 0e+00
arginine/ornithine succinyltransferase, alpha subunit; In some bacteria, including Pseudomonas ...
3-339
0e+00
arginine/ornithine succinyltransferase, alpha subunit; In some bacteria, including Pseudomonas aeruginosa, the astB gene (arginine N-succinyltransferase) is replaced by tandem paralogs that form a heterodimer. This heterodimer from P. aeruginosa is characterized as arginine and ornithine N-2 succinyltransferase (AOST). Members of this protein family represent the less widespread paralog, designated AruI, or arginine/ornithine succinyltransferase, alpha subunit.
Pssm-ID: 274489 Cd Length: 336 Bit Score: 550.18 E-value: 0e+00
Arginine N-succinyltransferase beta subunit; Arginine N-succinyltransferase EC:2.3.1.109 catalyzes the transfer of succinyl-CoA to arginine to produce succinyl-arginine. This is the first step in arginine catabolism by the arginine succinyltransferase pathway.
Pssm-ID: 428220 Cd Length: 336 Bit Score: 466.22 E-value: 3.40e-166
arginine/ornithine succinyltransferase, alpha subunit; In some bacteria, including Pseudomonas ...
3-339
0e+00
arginine/ornithine succinyltransferase, alpha subunit; In some bacteria, including Pseudomonas aeruginosa, the astB gene (arginine N-succinyltransferase) is replaced by tandem paralogs that form a heterodimer. This heterodimer from P. aeruginosa is characterized as arginine and ornithine N-2 succinyltransferase (AOST). Members of this protein family represent the less widespread paralog, designated AruI, or arginine/ornithine succinyltransferase, alpha subunit.
Pssm-ID: 274489 Cd Length: 336 Bit Score: 550.18 E-value: 0e+00
arginine and ornithine succinyltransferase subunits; In many bacteria, the sole member of this ...
3-339
5.64e-172
arginine and ornithine succinyltransferase subunits; In many bacteria, the sole member of this protein family is arginine N-succinyltransferase (EC 2.3.1.109), the AstA protein of the arginine succinyltransferase (ast) pathway. However, in Pseudomonas aeruginosa and several other species, a tandem gene pair encodes alpha and beta subunits of a heterodimer that is designated arginine and ornithine succinyltransferase (AOST).
Pssm-ID: 274487 Cd Length: 335 Bit Score: 480.99 E-value: 5.64e-172
Arginine N-succinyltransferase beta subunit; Arginine N-succinyltransferase EC:2.3.1.109 catalyzes the transfer of succinyl-CoA to arginine to produce succinyl-arginine. This is the first step in arginine catabolism by the arginine succinyltransferase pathway.
Pssm-ID: 428220 Cd Length: 336 Bit Score: 466.22 E-value: 3.40e-166
arginine N-succinyltransferase; In many bacteria, the arginine succinyltransferase (ast) ...
3-338
1.89e-116
arginine N-succinyltransferase; In many bacteria, the arginine succinyltransferase (ast) pathway operon consists of five genes, including this protein, arginine N-succinyltransferase (EC 2.3.1.109). In a few species, such as Pseudomonas aeruginosa, the member of this family is encoded adjacent to a paralog, and the two polypeptides form a heterodimeric enzyme, active on both arginine and ornithine. In such species, this polypeptide may be treated as the beta subunit of an enzyme that may be named either arginine N-succinyltransferase (AST) or arginine and orthithine N-succinyltransferase (AOST). [Energy metabolism, Amino acids and amines]
Pssm-ID: 274488 Cd Length: 336 Bit Score: 340.08 E-value: 1.89e-116
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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