2ZY2

dodecameric L-aspartate beta-decarboxylase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
A	0006520	biological_process	amino acid metabolic process
A	0006523	biological_process	alanine biosynthetic process
A	0006531	biological_process	aspartate metabolic process
A	0008483	molecular_function	transaminase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0009058	biological_process	biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
A	0047688	molecular_function	aspartate 4-decarboxylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP A 900

Chain	Residue
A	ARG37
A	TYR289
A	SER312
A	LYS315
A	ARG323
A	TYR134
A	GLY173
A	GLY174
A	THR175
A	PHE204
A	TYR207
A	ASN256
A	ASP286

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Functional Information from PROSITE/UniProt

site_id	PS00105
Number of Residues	14
Details	AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKyfGAtGWRLG

Chain	Residue	Details
A	SER312-GLY325

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"19368885","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZY2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	PHE204
A	ASP286
A	LYS315

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