Annotations: 1SSQ

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B [auth D]	d1ssqd_	All beta proteins	Single-stranded left-handed beta-helix	Trimeric LpxA-like enzymes	Serine acetyltransferase	Serine acetyltransferase	(Haemophilus influenzae ) [TaxId: 727 ],	SCOPe (2.08)
A	d1ssqa_	All beta proteins	Single-stranded left-handed beta-helix	Trimeric LpxA-like enzymes	Serine acetyltransferase	Serine acetyltransferase	(Haemophilus influenzae ) [TaxId: 727 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B [auth D]	SCOP2B Superfamily	Trimeric LpxA-like enzymes	8039780	3001804	SCOP2B (2022-06-29)
A	SCOP2 Family	Serine acetyltransferase	8027401	4001889	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Trimeric LpxA-like enzymes	8039780	3001804	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 [auth D]	PF00132	e1ssqD2	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Trimeric LpxA-like enzymes (From Topology)	T: Trimeric LpxA-like enzymes	F: PF00132	ECOD (1.6)
B [auth D]	PF06426	e1ssqD1	A: alpha arrays	X: Serine acetyltransferase N-terminal domain (From Topology)	H: Serine acetyltransferase N-terminal domain (From Topology)	T: Serine acetyltransferase N-terminal domain	F: PF06426	ECOD (1.6)
A	PF00132	e1ssqA2	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Trimeric LpxA-like enzymes (From Topology)	T: Trimeric LpxA-like enzymes	F: PF00132	ECOD (1.6)
A	PF06426	e1ssqA3	A: alpha arrays	X: Serine acetyltransferase N-terminal domain (From Topology)	H: Serine acetyltransferase N-terminal domain (From Topology)	T: Serine acetyltransferase N-terminal domain	F: PF06426	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth D]	1.10.3130.10	Mainly Alpha	Orthogonal Bundle	serine acetyltransferase, domain 1	serine acetyltransferase, domain 1	CATH (4.3.0)
B [auth D]	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (4.3.0)
A	1.10.3130.10	Mainly Alpha	Orthogonal Bundle	serine acetyltransferase, domain 1	serine acetyltransferase, domain 1	CATH (4.3.0)
A	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth D]	PF00132	Bacterial transferase hexapeptide (six repeats) (Hexapep)	Bacterial transferase hexapeptide (six repeats)	-	Repeat
A, B [auth D]	PF06426	Serine acetyltransferase, N-terminal (SATase_N)	Serine acetyltransferase, N-terminal	The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants [2] and bacteria [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth D]	Serine acetyltransferase	acetyltransferase activity serine O-acyltransferase activity O-acyltransferase activity serine O-acetyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity O-acetyltransferase activity catalytic activity	serine family amino acid metabolic process oxoacid metabolic process cellular biosynthetic process sulfur amino acid metabolic process organonitrogen compound biosynthetic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process cysteine biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process serine family amino acid metabolic process oxoacid metabolic process cellular biosynthetic process sulfur amino acid metabolic process organonitrogen compound biosynthetic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process cysteine biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process sulfur compound metabolic process organonitrogen compound metabolic process cysteine biosynthetic process from serine small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process primary metabolic process L-amino acid biosynthetic process L-serine metabolic process L-amino acid metabolic process cysteine metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process sulfur compound biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process metabolic process cellular process serine family amino acid biosynthetic process sulfur amino acid biosynthetic process alpha-amino acid biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth D]	IPR045304	Serine acetyltransferase, LbH domain	Domain
A, B [auth D]	IPR042122	Serine acetyltransferase, N-terminal domain superfamily	Homologous Superfamily
A, B [auth D]	IPR011004	Trimeric LpxA-like superfamily	Homologous Superfamily
A, B [auth D]	IPR010493	Serine acetyltransferase, N-terminal	Domain
A, B [auth D]	IPR005881	Serine O-acetyltransferase	Family
A, B [auth D]	IPR018357	Hexapeptide transferase, conserved site	Conserved Site
A, B [auth D]	IPR001451	Hexapeptide repeat	Repeat

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 R01GM133198.