4H65

Crystal structure of SeMet derivative of HMP synthase Thi5 from S. cerevisiae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003674	molecular_function	molecular_function
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005575	cellular_component	cellular_component
A	0009228	biological_process	thiamine biosynthetic process
A	0009229	biological_process	thiamine diphosphate biosynthetic process
A	0016740	molecular_function	transferase activity
A	0046872	molecular_function	metal ion binding
A	0106344	molecular_function	4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP
B	0003674	molecular_function	molecular_function
B	0005506	molecular_function	iron ion binding
B	0005515	molecular_function	protein binding
B	0005575	cellular_component	cellular_component
B	0009228	biological_process	thiamine biosynthetic process
B	0009229	biological_process	thiamine diphosphate biosynthetic process
B	0016740	molecular_function	transferase activity
B	0046872	molecular_function	metal ion binding
B	0106344	molecular_function	4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Motif: {"description":"CCCFC; essential for catalytic activity, may be the site of iron coordination","evidences":[{"source":"PubMed","id":"23048037","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"23048037","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"23048037","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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