8QZI

Crystal structure of PptT-ACP from Mycobacterium tuberculosis

External Resource: Annotation

Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
E, F	PF00550	Phosphopantetheine attachment site (PP-binding)	Phosphopantetheine attachment site	A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes memb ...	A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.	Domain
A, B, C, D	PF01648	4'-phosphopantetheinyl transferase superfamily (ACPS)	4'-phosphopantetheinyl transferase superfamily	Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of Pfam:PF00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of ...	Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of Pfam:PF00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP [1]. This superfamily consists of two subtypes: The ACPS type such as Swiss:P24224 and the Sfp type such as Swiss:P39135. The structure of the Sfp type is known [3], which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.	Domain
A, B, C, D	PF17837	4'-phosphopantetheinyl transferase N-terminal domain (4PPT_N)	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 Pfam:PF01648 domain with which it forms a pseudodimeric arrangement [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
E, F	Phenolphthiocerol/phthiocerol polyketide synthase subunit C	oxidoreductase activity catalytic activity vitamin binding amide binding modified amino acid binding binding phosphopantetheine binding small molecule binding acyltransferase activity 3-oxoacyl-[acyl-carrier-protein] synthase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity fatty acid synthase activity	cellular component biogenesis peptidoglycan-based cell wall biogenesis cell wall biogenesis cell wall organization or biogenesis Actinobacterium-type cell wall biogenesis cellular process cellular component organization or biogenesis polyol metabolic process small molecule biosynthetic process organic hydroxy compound metabolic process lipid biosynthetic process alcohol metabolic process primary metabolic process biosynthetic process cellular component biogenesis peptidoglycan-based cell wall biogenesis cell wall biogenesis cell wall organization or biogenesis Actinobacterium-type cell wall biogenesis cellular process cellular component organization or biogenesis polyol metabolic process small molecule biosynthetic process organic hydroxy compound metabolic process lipid biosynthetic process alcohol metabolic process primary metabolic process biosynthetic process organic hydroxy compound biosynthetic process phenol-containing compound metabolic process polyol biosynthetic process alcohol biosynthetic process phenol-containing compound biosynthetic process metabolic process small molecule metabolic process phenolic phthiocerol biosynthetic process lipid metabolic process glycol biosynthetic process diol biosynthetic process glycol metabolic process phthiocerol biosynthetic process diol metabolic process cellular component organization cellular component assembly DIM/DIP cell wall layer assembly fatty acid metabolic process monocarboxylic acid biosynthetic process oxoacid metabolic process carboxylic acid metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process monocarboxylic acid metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane protein-containing complex catalytic complex polyketide synthase complex
A, B, C, D	4'-phosphopantetheinyl transferase PptT	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding holo-[acyl-carrier-protein] synthase activity transferase activity catalytic activity phosphotransferase activity, for other substituted phosphate groups transferase activity, transferring phosphorus-containing groups	enterobactin biosynthetic process polyketide metabolic process organic hydroxy compound metabolic process catechol-containing compound metabolic process secondary metabolic process antibiotic biosynthetic process siderophore biosynthetic process antibiotic metabolic process secondary metabolite biosynthetic process siderophore metabolic process lactone biosynthetic process catechol-containing compound biosynthetic process catechol-containing siderophore biosynthetic process enterobactin metabolic process enterobactin biosynthetic process polyketide metabolic process organic hydroxy compound metabolic process catechol-containing compound metabolic process secondary metabolic process antibiotic biosynthetic process siderophore biosynthetic process antibiotic metabolic process secondary metabolite biosynthetic process siderophore metabolic process lactone biosynthetic process catechol-containing compound biosynthetic process catechol-containing siderophore biosynthetic process enterobactin metabolic process macrolide biosynthetic process macrolide metabolic process biosynthetic process peptide biosynthetic process polyketide biosynthetic process lactone metabolic process organic hydroxy compound biosynthetic process phenol-containing compound metabolic process phenol-containing compound biosynthetic process metabolic process cellular process nonribosomal peptide biosynthetic process peptide metabolic process	cell periphery cellular anatomical structure plasma membrane membrane protein-containing complex catalytic complex enterobactin synthetase complex intracellular protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
E, F	IPR016035	Acyl transferase/acyl hydrolase/lysophospholipase	Homologous Superfamily
E, F	IPR014031	Beta-ketoacyl synthase, C-terminal	Domain
E, F	IPR006162	Phosphopantetheine attachment site	PTM
E, F	IPR013154	Alcohol dehydrogenase-like, N-terminal	Domain
E, F	IPR020807	Polyketide synthase, dehydratase domain	Domain
E, F	IPR049552	Polyketide synthase, dehydratase domain, N-terminal	Domain
E, F	IPR049551	Polyketide synthase, dehydratase domain, C-terminal	Domain
E, F	IPR020843	Polyketide synthase, enoylreductase domain	Domain
E, F	IPR013968	Polyketide synthase, ketoreductase domain	Domain
E, F	IPR016036	Malonyl-CoA ACP transacylase, ACP-binding	Homologous Superfamily
E, F	IPR050091	Polyketide and Nonribosomal Peptide Biosynthesis Enzymes	Family
E, F	IPR020806	Polyketide synthase, phosphopantetheine-binding domain	Domain
E, F	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain	Domain
E, F	IPR036736	ACP-like superfamily	Homologous Superfamily
E, F	IPR014043	Acyl transferase domain	Domain
E, F	IPR011032	GroES-like superfamily	Homologous Superfamily
E, F	IPR009081	Phosphopantetheine binding ACP domain	Domain
E, F	IPR016039	Thiolase-like	Homologous Superfamily
E, F	IPR001227	Acyl transferase domain superfamily	Homologous Superfamily
E, F	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
E, F	IPR018201	Beta-ketoacyl synthase, active site	Active Site
E, F	IPR014030	Beta-ketoacyl synthase-like, N-terminal	Domain
E, F	IPR042104	Polyketide synthase, dehydratase domain superfamily	Homologous Superfamily
E, F	IPR049900	Polyketide/metazoan fatty acid synthase, dehydratase domain	Domain
A, B, C, D	IPR037143	4'-phosphopantetheinyl transferase domain superfamily	Homologous Superfamily
A, B, C, D	IPR003542	Enterobactin synthetase-like, component D	Family
A, B, C, D	IPR041354	4'-phosphopantetheinyl transferase, N-terminal domain	Domain
A, B, C, D	IPR008278	4'-phosphopantetheinyl transferase domain	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.

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8QZI

Crystal structure of PptT-ACP from Mycobacterium tuberculosis

External Resource: Annotation

Protein Family Annotation Pfam Database Homepage

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

InterPro: Protein Family Classification InterPro Database Homepage