Annotations: 1QM4

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1qm4b1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)
A	d1qm4a1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	RAT (Rattus norvegicus ) [TaxId: 10116 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036405	3000766	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036406	3000766	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036408	3000766	SCOP2B (2022-06-29)
A	SCOP2 Family	S-adenosylmethionine synthetase	8024026	4002058	SCOP2 (2022-06-29)
A	SCOP2 Family	S-adenosylmethionine synthetase	8024027	4002058	SCOP2 (2022-06-29)
A	SCOP2 Family	S-adenosylmethionine synthetase	8024029	4002058	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	S-adenosylmethionine synthetase	8036405	3000766	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	S-adenosylmethionine synthetase	8036406	3000766	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	S-adenosylmethionine synthetase	8036408	3000766	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	S-AdoMet_synt_C	e1qm4B3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_C	ECOD (1.6)
B	S-AdoMet_synt_M	e1qm4B2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_M	ECOD (1.6)
B	S-AdoMet_synt_N	e1qm4B1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_N	ECOD (1.6)
A	S-AdoMet_synt_C	e1qm4A3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_C	ECOD (1.6)
A	S-AdoMet_synt_M	e1qm4A2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_M	ECOD (1.6)
A	S-AdoMet_synt_N	e1qm4A1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
A	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00438	S-adenosylmethionine synthetase, N-terminal domain (S-AdoMet_synt_N)	S-adenosylmethionine synthetase, N-terminal domain	The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.	Domain
A, B	PF02773	S-adenosylmethionine synthetase, C-terminal domain (S-AdoMet_synt_C)	S-adenosylmethionine synthetase, C-terminal domain	The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.	Domain
A, B	PF02772	S-adenosylmethionine synthetase, central domain (S-AdoMet_synt_M)	S-adenosylmethionine synthetase, central domain	The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	METHIONINE ADENOSYLTRANSFERASE, ALPHA FORM	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding ADP binding amino acid binding methionine adenosyltransferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity identical protein binding protein binding	cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein-containing complex assembly cellular process cellular component organization or biogenesis small molecule metabolic process metabolic process one-carbon metabolic process protein homotetramerization protein complex oligomerization protein tetramerization protein homooligomerization cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein-containing complex assembly cellular process cellular component organization or biogenesis small molecule metabolic process metabolic process one-carbon metabolic process protein homotetramerization protein complex oligomerization protein tetramerization protein homooligomerization sulfur compound biosynthetic process biosynthetic process S-adenosylmethionine biosynthetic process S-adenosylmethionine metabolic process sulfur compound metabolic process catabolic process oxoacid metabolic process sulfur amino acid metabolic process aspartate family amino acid metabolic process amino acid metabolic process organic acid catabolic process organic acid metabolic process alpha-amino acid metabolic process cellular catabolic process carboxylic acid catabolic process amino acid catabolic process aspartate family amino acid catabolic process carboxylic acid metabolic process L-amino acid catabolic process primary metabolic process methionine metabolic process L-amino acid metabolic process sulfur compound catabolic process proteinogenic amino acid metabolic process sulfur amino acid catabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process methionine catabolic process small molecule catabolic process	membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle cellular anatomical structure organelle lumen organelle nuclear periphery nuclear lumen nuclear matrix protein-containing complex membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle cellular anatomical structure organelle lumen organelle nuclear periphery nuclear lumen nuclear matrix protein-containing complex catalytic complex methionine adenosyltransferase complex transferase complex intracellular protein-containing complex cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR022636	S-adenosylmethionine synthetase superfamily	Homologous Superfamily
A, B	IPR022629	S-adenosylmethionine synthetase, central domain	Domain
A, B	IPR022628	S-adenosylmethionine synthetase, N-terminal	Domain
A, B	IPR022631	S-adenosylmethionine synthetase, conserved site	Conserved Site
A, B	IPR022630	S-adenosylmethionine synthetase, C-terminal	Domain
A, B	IPR002133	S-adenosylmethionine synthetase	Family

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.