6CGQ

Threonine synthase from Bacillus subtilis ATCC 6633 with PLP and PLP-Ala

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6cgqa_	Alpha and beta proteins (a/b)	Tryptophan synthase beta subunit-like PLP-dependent enzymes	Tryptophan synthase beta subunit-like PLP-dependent enzymes	automated matches	automated matches	(Bacillus spizizenii ) [TaxId: 96241 ],	SCOPe (2.08)
B	d6cgqb_	Alpha and beta proteins (a/b)	Tryptophan synthase beta subunit-like PLP-dependent enzymes	Tryptophan synthase beta subunit-like PLP-dependent enzymes	automated matches	automated matches	(Bacillus spizizenii ) [TaxId: 96241 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Tryptophan synthase beta subunit-like PLP-dependent enzymes	8097182	3001427	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Tryptophan synthase beta subunit-like PLP-dependent enzymes	8097182	3001427	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PALP	e6cgqA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Tryptophan synthase beta subunit-like PLP-dependent enzymes (From Topology)	T: Tryptophan synthase beta subunit-like PLP-dependent enzymes	F: PALP	ECOD (1.6)
B	PALP	e6cgqB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Tryptophan synthase beta subunit-like PLP-dependent enzymes (From Topology)	T: Tryptophan synthase beta subunit-like PLP-dependent enzymes	F: PALP	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1100	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	3.40.50.1100	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00291	Pyridoxal-phosphate dependent enzyme (PALP)	Pyridoxal-phosphate dependent enzyme	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Threonine synthase	threonine deaminase activity lyase activity ammonia-lyase activity catalytic activity carbon-nitrogen lyase activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding organic cyclic compound binding anion binding heterocyclic compound binding small molecule binding threonine deaminase activity lyase activity ammonia-lyase activity catalytic activity carbon-nitrogen lyase activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding organic cyclic compound binding anion binding heterocyclic compound binding small molecule binding L-serine ammonia-lyase activity carbon-oxygen lyase activity, acting on phosphates threonine synthase activity carbon-oxygen lyase activity	catabolic process oxoacid 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 threonine catabolic process threonine metabolic process small molecule metabolic process amino acid catabolic process aspartate family amino acid catabolic process catabolic process oxoacid 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 threonine catabolic process threonine metabolic process small molecule metabolic process amino acid catabolic process aspartate family amino acid catabolic process cellular metabolic process L-amino acid catabolic process carboxylic acid metabolic process primary metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process metabolic process cellular process small molecule catabolic process small molecule biosynthetic process cellular biosynthetic process organic acid biosynthetic process carboxylic acid biosynthetic process amino acid biosynthetic process biosynthetic process isoleucine biosynthetic process branched-chain amino acid biosynthetic process branched-chain amino acid metabolic process isoleucine metabolic process alpha-amino acid biosynthetic process serine family amino acid metabolic process L-serine catabolic process L-serine metabolic process serine family amino acid catabolic process aspartate family amino acid biosynthetic process L-amino acid biosynthetic process threonine biosynthetic process proteinogenic amino acid biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036052	Tryptophan synthase beta chain-like, PALP domain superfamily	Homologous Superfamily
A, B	IPR050147	Serine/Threonine Dehydratase	Family
A, B	IPR000634	Serine/threonine dehydratase, pyridoxal-phosphate-binding site	Binding Site
A, B	IPR004450	Threonine synthase-like	Family
A, B	IPR026260	Threonine synthase, bacterial/archaeal	Family
A, B	IPR001926	Tryptophan synthase beta chain-like, PALP 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.