5TXT | pdb_00005txt

Structure of asymmetric apo/holo ALAS dimer from S. cerevisiae

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	PLP-dependent transferases	8098330	3000954	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	PLP-dependent transferases	8098330	3000954	SCOP2B (2022-06-29)
C [auth D]	SCOP2B Superfamily	PLP-dependent transferases	8098330	3000954	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	PLP-dependent transferases	8098330	3000954	SCOP2B (2022-06-29)
D [auth C]	SCOP2B Superfamily	PLP-dependent transferases	8098330	3000954	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	PLP-dependent transferases	8098330	3000954	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	Aminotran_1_2_C_9	e5txtA3	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: Aminotran_1_2_C_9	ECOD (1.6)
A	Aminotran_5_N	e5txtA4	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
A	UNK_F_TYPE	e5txtA1	A: extended segments	X: mitochondrial aminolevulinate synthase C-terminal domain (From Topology)	H: mitochondrial aminolevulinate synthase C-terminal domain (From Topology)	T: mitochondrial aminolevulinate synthase C-terminal domain	F: UNK_F_TYPE	ECOD (1.6)
E	Aminotran_1_2_C_9	e5txtE3	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: Aminotran_1_2_C_9	ECOD (1.6)
E	Aminotran_5_N	e5txtE4	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
E	UNK_F_TYPE	e5txtE2	A: extended segments	X: mitochondrial aminolevulinate synthase C-terminal domain (From Topology)	H: mitochondrial aminolevulinate synthase C-terminal domain (From Topology)	T: mitochondrial aminolevulinate synthase C-terminal domain	F: UNK_F_TYPE	ECOD (1.6)
C [auth D]	Aminotran_1_2_C_9	e5txtD2	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: Aminotran_1_2_C_9	ECOD (1.6)
C [auth D]	Aminotran_5_N	e5txtD4	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
C [auth D]	UNK_F_TYPE	e5txtD3	A: extended segments	X: mitochondrial aminolevulinate synthase C-terminal domain (From Topology)	H: mitochondrial aminolevulinate synthase C-terminal domain (From Topology)	T: mitochondrial aminolevulinate synthase C-terminal domain	F: UNK_F_TYPE	ECOD (1.6)
F	Aminotran_1_2_C_9	e5txtF3	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: Aminotran_1_2_C_9	ECOD (1.6)
F	Aminotran_5_N	e5txtF4	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
F	UNK_F_TYPE	e5txtF2	A: extended segments	X: mitochondrial aminolevulinate synthase C-terminal domain (From Topology)	H: mitochondrial aminolevulinate synthase C-terminal domain (From Topology)	T: mitochondrial aminolevulinate synthase C-terminal domain	F: UNK_F_TYPE	ECOD (1.6)
D [auth C]	Aminotran_1_2_C_9	e5txtC1	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: Aminotran_1_2_C_9	ECOD (1.6)
D [auth C]	Aminotran_5_N	e5txtC3	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
D [auth C]	UNK_F_TYPE	e5txtC2	A: extended segments	X: mitochondrial aminolevulinate synthase C-terminal domain (From Topology)	H: mitochondrial aminolevulinate synthase C-terminal domain (From Topology)	T: mitochondrial aminolevulinate synthase C-terminal domain	F: UNK_F_TYPE	ECOD (1.6)
B	Aminotran_1_2_C_9	e5txtB2	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: Aminotran_1_2_C_9	ECOD (1.6)
B	Aminotran_5_N	e5txtB4	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
B	UNK_F_TYPE	e5txtB3	A: extended segments	X: mitochondrial aminolevulinate synthase C-terminal domain (From Topology)	H: mitochondrial aminolevulinate synthase C-terminal domain (From Topology)	T: mitochondrial aminolevulinate synthase C-terminal domain	F: UNK_F_TYPE	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B, D [auth C], F	PF00155	Aminotransferase class I and II (Aminotran_1_2)	Aminotransferase class I and II		Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C [auth D], E	5-aminolevulinate synthase, mitochondrial	vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding anion binding heterocyclic compound binding small molecule binding N-succinyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity succinyltransferase activity catalytic activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding anion binding heterocyclic compound binding small molecule binding N-succinyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity succinyltransferase activity catalytic activity 5-aminolevulinate synthase activity N-acyltransferase activity	heme metabolic process pigment metabolic process porphyrin-containing compound biosynthetic process tetrapyrrole metabolic process heme biosynthetic process pigment biosynthetic process tetrapyrrole biosynthetic process biosynthetic process metabolic process cellular process porphyrin-containing compound metabolic process protoporphyrinogen IX metabolic process protoporphyrinogen IX biosynthetic process positive regulation of organelle organization heme metabolic process pigment metabolic process porphyrin-containing compound biosynthetic process tetrapyrrole metabolic process heme biosynthetic process pigment biosynthetic process tetrapyrrole biosynthetic process biosynthetic process metabolic process cellular process porphyrin-containing compound metabolic process protoporphyrinogen IX metabolic process protoporphyrinogen IX biosynthetic process positive regulation of organelle organization regulation of biological process regulation of cellular process regulation of cellular component organization positive regulation of cellular component organization organelle assembly positive regulation of cellular component biogenesis biological regulation positive regulation of biological process regulation of cellular component biogenesis regulation of organelle organization cellular component biogenesis cellular component organization organelle organization cellular component assembly regulation of organelle assembly cellular component organization or biogenesis positive regulation of cellular process positive regulation of organelle assembly	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle membrane-enclosed lumen mitochondrial matrix intracellular organelle lumen organelle lumen
B, D [auth C], F	5-aminolevulinate synthase, mitochondrial	vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding anion binding heterocyclic compound binding small molecule binding N-succinyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity succinyltransferase activity catalytic activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding anion binding heterocyclic compound binding small molecule binding N-succinyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity succinyltransferase activity catalytic activity 5-aminolevulinate synthase activity N-acyltransferase activity	heme metabolic process pigment metabolic process porphyrin-containing compound biosynthetic process tetrapyrrole metabolic process heme biosynthetic process pigment biosynthetic process tetrapyrrole biosynthetic process biosynthetic process metabolic process cellular process porphyrin-containing compound metabolic process protoporphyrinogen IX metabolic process protoporphyrinogen IX biosynthetic process positive regulation of organelle organization heme metabolic process pigment metabolic process porphyrin-containing compound biosynthetic process tetrapyrrole metabolic process heme biosynthetic process pigment biosynthetic process tetrapyrrole biosynthetic process biosynthetic process metabolic process cellular process porphyrin-containing compound metabolic process protoporphyrinogen IX metabolic process protoporphyrinogen IX biosynthetic process positive regulation of organelle organization regulation of biological process regulation of cellular process regulation of cellular component organization positive regulation of cellular component organization organelle assembly positive regulation of cellular component biogenesis biological regulation positive regulation of biological process regulation of cellular component biogenesis regulation of organelle organization cellular component biogenesis cellular component organization organelle organization cellular component assembly regulation of organelle assembly cellular component organization or biogenesis positive regulation of cellular process positive regulation of organelle assembly	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle membrane-enclosed lumen mitochondrial matrix intracellular organelle lumen organelle lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C [auth D], E	IPR001917	Aminotransferase, class-II, pyridoxal-phosphate binding site	Binding Site
A, C [auth D], E	IPR015421	Pyridoxal phosphate-dependent transferase, major domain	Homologous Superfamily
A, C [auth D], E	IPR015422	Pyridoxal phosphate-dependent transferase, small domain	Homologous Superfamily
A, C [auth D], E	IPR015424	Pyridoxal phosphate-dependent transferase	Homologous Superfamily
A, C [auth D], E	IPR010961	Tetrapyrrole biosynthesis, 5-aminolevulinic acid synthase	Domain
A, C [auth D], E	IPR004839	Aminotransferase, class I/classII, large domain	Domain
A, C [auth D], E	IPR050087	8-amino-7-oxononanoate synthase class-II	Family
B, D [auth C], F	IPR001917	Aminotransferase, class-II, pyridoxal-phosphate binding site	Binding Site
B, D [auth C], F	IPR015421	Pyridoxal phosphate-dependent transferase, major domain	Homologous Superfamily
B, D [auth C], F	IPR015422	Pyridoxal phosphate-dependent transferase, small domain	Homologous Superfamily
B, D [auth C], F	IPR015424	Pyridoxal phosphate-dependent transferase	Homologous Superfamily
B, D [auth C], F	IPR010961	Tetrapyrrole biosynthesis, 5-aminolevulinic acid synthase	Domain
B, D [auth C], F	IPR004839	Aminotransferase, class I/classII, large domain	Domain
B, D [auth C], F	IPR050087	8-amino-7-oxononanoate synthase class-II	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
B, D [auth C], F	LLP	Parent Component: LYS RESID: AA0119 PSI-MOD : N6-pyridoxal phosphate-L-lysine MOD:00128

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.