2GSA | pdb_00002gsa

CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE, WILD-TYPE FORM)

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d2gsab_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	GABA-aminotransferase-like	Glutamate-1-semialdehyde aminomutase (aminotransferase)	(Synechococcus sp. ) [TaxId: 1131 ],	SCOPe (2.08)
A	d2gsaa_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	GABA-aminotransferase-like	Glutamate-1-semialdehyde aminomutase (aminotransferase)	(Synechococcus sp. ) [TaxId: 1131 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	PLP-dependent transferases	8032379	3000954	SCOP2B (2022-06-29)
A	SCOP2 Family	GABA-aminotransferase-like	8019999	4000675	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PLP-dependent transferases	8032379	3000954	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	PRK00062	e2gsaB2	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: PRK00062	ECOD (1.6)
B	Aminotran_3_N	e2gsaB3	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_3_N	ECOD (1.6)
A	PRK00062	e2gsaA1	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: PRK00062	ECOD (1.6)
A	Aminotran_3_N	e2gsaA2	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_3_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.90.1150.10	Alpha Beta	Alpha-Beta Complex	Aspartate Aminotransferase, domain 1	Aspartate Aminotransferase, domain 1	CATH (4.3.0)
B	3.40.640.10	Alpha Beta	3-Layer(aba) Sandwich	Aspartate Aminotransferase	domain 2	CATH (4.3.0)
A	3.90.1150.10	Alpha Beta	Alpha-Beta Complex	Aspartate Aminotransferase, domain 1	Aspartate Aminotransferase, domain 1	CATH (4.3.0)
A	3.40.640.10	Alpha Beta	3-Layer(aba) Sandwich	Aspartate Aminotransferase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00202	Aminotransferase class-III (Aminotran_3)	Aminotransferase class-III		Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	GLUTAMATE SEMIALDEHYDE AMINOTRANSFERASE	transferase activity, transferring nitrogenous groups transaminase activity transferase activity catalytic activity isomerase activity intramolecular aminotransferase activity glutamate-1-semialdehyde 2,1-aminomutase activity intramolecular transferase activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding anion binding transferase activity, transferring nitrogenous groups transaminase activity transferase activity catalytic activity isomerase activity intramolecular aminotransferase activity glutamate-1-semialdehyde 2,1-aminomutase activity intramolecular transferase activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding anion binding heterocyclic compound binding small molecule binding	heme metabolic process pigment metabolic process porphyrin-containing compound biosynthetic process tetrapyrrole metabolic process heme biosynthetic process protoporphyrinogen IX metabolic process pigment biosynthetic process protoporphyrinogen IX biosynthetic process tetrapyrrole biosynthetic process biosynthetic process metabolic process cellular process porphyrin-containing compound metabolic process chlorophyll metabolic process heme metabolic process pigment metabolic process porphyrin-containing compound biosynthetic process tetrapyrrole metabolic process heme biosynthetic process protoporphyrinogen IX metabolic process pigment biosynthetic process protoporphyrinogen IX biosynthetic process tetrapyrrole biosynthetic process biosynthetic process metabolic process cellular process porphyrin-containing compound metabolic process chlorophyll metabolic process chlorophyll biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR049704	Aminotransferases class-III pyridoxal-phosphate attachment site	Conserved Site
A, B	IPR015424	Pyridoxal phosphate-dependent transferase	Homologous Superfamily
A, B	IPR005814	Aminotransferase class-III	Family
A, B	IPR015421	Pyridoxal phosphate-dependent transferase, major domain	Homologous Superfamily
A, B	IPR015422	Pyridoxal phosphate-dependent transferase, small domain	Homologous Superfamily
A, B	IPR004639	Tetrapyrrole biosynthesis, glutamate-1-semialdehyde aminotransferase	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	glutamate-1-semialdehyde 2,1-aminomutase M-CSA #195	Tetrapyrroles are large macrocyclic compounds derived from a common biosynthetic pathway. The end-product, uroporphyrinogen III, is used to synthesise a number of important molecules, including vitamin B12, haem, sirohaem, chlorophyll, coenzyme F430 and phytochromobilin. This entry represents glutamate-1-semialdehyde (GSA) aminotransferase (EC:5.4.3.8), which catalyses a transamination reaction to produce 5-aminoaevulinic acid during the first stage of tetrapyrrole biosynthesis by the C5 pathway. It is a class III aminotransferase.	Defined by 3 residues: TYR:A-149 [auth A-150]ASP:A-244 [auth A-245]LYS:A-272 [auth A-273] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 5.4.3.8 (PDB Primary Data) Search M-CSA Motif + EC 5.4.3.8

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.