8EIM

Structure of ALAS with C-terminal truncation from S. cerevisiae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003870	molecular_function	5-aminolevulinate synthase activity
A	0009058	biological_process	biosynthetic process
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0033014	biological_process	tetrapyrrole biosynthetic process
B	0003870	molecular_function	5-aminolevulinate synthase activity
B	0009058	biological_process	biosynthetic process
B	0016740	molecular_function	transferase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0033014	biological_process	tetrapyrrole biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00599
Number of Residues	10
Details	AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TLGKSFGSVG

Chain	Residue	Details
A	THR334-GLY343

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P18079

Chain	Residue	Details
A	LYS337
B	LYS337

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site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P18079

Chain	Residue	Details
A	ARG91
B	THR366
B	THR367
B	THR452
A	SER204
A	LYS223
A	THR366
A	THR367
A	THR452
B	ARG91
B	SER204
B	LYS223

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site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: in other chain => ECO:0000250|UniProtKB:P18079

Chain	Residue	Details
A	SER256
A	HIS284
A	THR334
B	SER256
B	HIS284
B	THR334

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:P18079

Chain	Residue	Details
A	LYS337
B	LYS337

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