2CFB

Glutamate-1-semialdehyde 2,1-Aminomutase from Thermosynechococcus elongatus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006782	biological_process	protoporphyrinogen IX biosynthetic process
A	0008483	molecular_function	transaminase activity
A	0015995	biological_process	chlorophyll biosynthetic process
A	0016853	molecular_function	isomerase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0033014	biological_process	tetrapyrrole biosynthetic process
A	0042286	molecular_function	glutamate-1-semialdehyde 2,1-aminomutase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PLR A1412

Chain	Residue
A	SER100
A	LYS251
A	HOH2013
A	GLY101
A	THR102
A	TYR128
A	GLU190
A	ASN195
A	ASP223
A	VAL225
A	MET226

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Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	37
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LVfDEVmt.GF.RiAyggaqekfgvtp....DLTtlGKvigGG

Chain	Residue	Details
A	LEU220-GLY256

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00375

Chain	Residue	Details
A	LYS251

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	ASP223
A	TYR128

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site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	LYS251
A	ASP223
A	TYR128

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site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	ASP223
A	LYS251

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