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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P18079","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P18079","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P18079","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"P18079","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---