2WR8

Structure of Pyrococcus horikoshii SAM hydroxide adenosyltransferase in complex with SAH

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF20257	e2wr8A2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Bacterial fluorinating enzyme-C	F: PF20257	ECOD (1.6)
A	PF01887	e2wr8A1	A: a/b three-layered sandwiches	X: Bacterial fluorinating enzyme, N-terminal domain (From Topology)	H: Bacterial fluorinating enzyme, N-terminal domain (From Topology)	T: Bacterial fluorinating enzyme, N-terminal domain	F: PF01887	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.10790	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	S-adenosyl-l-methionine hydroxide adenosyltransferase, N-terminal	CATH (4.3.0)
A	2.40.30.90	Mainly Beta	Beta Barrel	Elongation Factor Tu (Ef-tu)	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01887	SAM hydroxide adenosyltransferase N-terminal domain (SAM_HAT_N)	SAM hydroxide adenosyltransferase N-terminal domain	This is a family of proteins, previously known as DUF62, found in archaebacteria and bacteria. The structure of proteins in this family is similar to that of a bacterial fluorinating enzyme [1]. S-adenosyl-l-methionine hydroxide adenosyltransferases ...	This is a family of proteins, previously known as DUF62, found in archaebacteria and bacteria. The structure of proteins in this family is similar to that of a bacterial fluorinating enzyme [1]. S-adenosyl-l-methionine hydroxide adenosyltransferases utilises a rigorously conserved amino acid side chain triad (Asp-Arg-His) which may have a role in activating water to hydroxide ion [2]. This family used to be known as DUF62.	Domain
A	PF20257	SAM hydroxide adenosyltransferase C-terminal domain (SAM_HAT_C)	SAM hydroxide adenosyltransferase C-terminal domain	This is a family of proteins, previously known as DUF62, found in archaebacteria and bacteria. The structure of proteins in this family is similar to that of a bacterial fluorinating enzyme [1]. S-adenosyl-l-methionine hydroxide adenosyltransferases ...	This is a family of proteins, previously known as DUF62, found in archaebacteria and bacteria. The structure of proteins in this family is similar to that of a bacterial fluorinating enzyme [1]. S-adenosyl-l-methionine hydroxide adenosyltransferases utilises a rigorously conserved amino acid side chain triad (Asp-Arg-His) which may have a role in activating water to hydroxide ion [2]. This family used to be known as DUF62. This entry represents the C-terminal domain of these enzymes.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PUTATIVE UNCHARACTERIZED PROTEIN PH0463	hydrolase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR023227	S-adenosyl-l-methionine hydroxide adenosyltransferase, C-terminal domain superfamily	Homologous Superfamily
A	IPR023228	S-adenosyl-l-methionine hydroxide adenosyltransferase, N-terminal domain superfamily	Homologous Superfamily
A	IPR046469	S-adenosyl-l-methionine hydroxide adenosyltransferase, N-terminal domain	Domain
A	IPR002747	S-adenosyl-l-methionine hydroxide adenosyltransferase	Family
A	IPR046470	S-adenosyl-l-methionine hydroxide adenosyltransferase, C-terminal domain	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.