4-phosphopantetheinyl transferase family protein containing an ACPS (holo-[ACP] synthase) domain; ACPS transfers the 4'-phosphopantetheine moiety from coenzyme A to a serine of an acyl-carrier-protein (ACP)
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
104-203
7.25e-09
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pfam00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. This superfamily consists of two subtypes: The ACPS type and the Sfp type. The structure of the Sfp type is known, which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.
Pssm-ID: 426364 [Multi-domain] Cd Length: 111 Bit Score: 51.84 E-value: 7.25e-09
holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, ...
42-94
1.23e-03
holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, phosphopantethiene, to the acyl carrier protein (ACP) apo-enzyme to generate the holo-enzyme. Related phosphopantethiene--protein transferases also exist. There is an orthologous domain in eukaryotic proteins. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273114 [Multi-domain] Cd Length: 121 Bit Score: 37.36 E-value: 1.23e-03
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ...
104-203
7.25e-09
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pfam00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. This superfamily consists of two subtypes: The ACPS type and the Sfp type. The structure of the Sfp type is known, which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.
Pssm-ID: 426364 [Multi-domain] Cd Length: 111 Bit Score: 51.84 E-value: 7.25e-09
4'-phosphopantetheinyl transferase N-terminal domain; This entry represents the N-terminal ...
39-97
5.35e-05
4'-phosphopantetheinyl transferase N-terminal domain; This entry represents the N-terminal domain from 4'- phosphopantetheinyl transferase enzymes. This domain is structurally related to the pfam01648 domain with which it forms a pseudodimeric arrangement.
Pssm-ID: 465526 [Multi-domain] Cd Length: 68 Bit Score: 39.92 E-value: 5.35e-05
holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, ...
42-94
1.23e-03
holo-[acyl-carrier-protein] synthase; Formerly dpj. This enzyme adds the prosthetic group, phosphopantethiene, to the acyl carrier protein (ACP) apo-enzyme to generate the holo-enzyme. Related phosphopantethiene--protein transferases also exist. There is an orthologous domain in eukaryotic proteins. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273114 [Multi-domain] Cd Length: 121 Bit Score: 37.36 E-value: 1.23e-03
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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