3L44

Crystal structure of Bacillus anthracis HemL-1, glutamate semialdehyde aminotransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0006782	biological_process	obsolete protoporphyrinogen IX biosynthetic process
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
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0006782	biological_process	obsolete protoporphyrinogen IX biosynthetic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0033014	biological_process	tetrapyrrole biosynthetic process
B	0042286	molecular_function	glutamate-1-semialdehyde 2,1-aminomutase activity

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	37
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. VIyDEVit.AF.RfMyggaqdllgvtp....DLTalGKvigGG

Chain	Residue	Details
A	VAL239-GLY275

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00375","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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