1AW5

5-AMINOLEVULINATE DEHYDRATASE FROM SACCHAROMYCES CEREVISIAE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004655	molecular_function	porphobilinogen synthase activity
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006779	biological_process	porphyrin-containing compound biosynthetic process
A	0006782	biological_process	protoporphyrinogen IX biosynthetic process
A	0006783	biological_process	heme biosynthetic process
A	0008270	molecular_function	zinc ion binding
A	0016829	molecular_function	lyase activity
A	0033014	biological_process	tetrapyrrole biosynthetic process
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 400

Chain	Residue
A	CYS133
A	CYS135
A	CYS143

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	HIS142
A	CYS234

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site_id	CAT
Number of Residues	2
Details	LYS 263 FORMS SCHIFF BASE WITH SUBSTRATE. LYS 210 IS SPATIALLY ADJACENT AND IS ALSO IMPLICATED IN CATALYSIS.

Chain	Residue
A	LYS263
A	LYS210

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Functional Information from PROSITE/UniProt

site_id	PS00169
Number of Residues	13
Details	D_ALA_DEHYDRATASE Delta-aminolevulinic acid dehydratase active site. GaDgIIVKPStfY

Chain	Residue	Details
A	GLY256-TYR268

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Schiff-base intermediate with substrate

Chain	Residue	Details
A	PHE211
A	PRO264

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site_id	SWS_FT_FI2
Number of Residues	7
Details	BINDING:

Chain	Residue	Details
A	LEU134
A	GLU136
A	GLY144
A	ASP221
A	LYS233
A	GLY291
A	LEU330

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956

Chain	Residue	Details
A	GLU255

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