2ZF5

Crystal Structure of highly thermostable glycerol kinase from a hyperthermophilic archaeon

Functional Information from GO Data

Chain	GOid	namespace	contents
O	0000166	molecular_function	nucleotide binding
O	0004370	molecular_function	glycerol kinase activity
O	0005524	molecular_function	ATP binding
O	0005829	cellular_component	cytosol
O	0005975	biological_process	carbohydrate metabolic process
O	0006071	biological_process	glycerol metabolic process
O	0006072	biological_process	glycerol-3-phosphate metabolic process
O	0016301	molecular_function	kinase activity
O	0016740	molecular_function	transferase activity
O	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
O	0019563	biological_process	glycerol catabolic process
Y	0000166	molecular_function	nucleotide binding
Y	0004370	molecular_function	glycerol kinase activity
Y	0005524	molecular_function	ATP binding
Y	0005829	cellular_component	cytosol
Y	0005975	biological_process	carbohydrate metabolic process
Y	0006071	biological_process	glycerol metabolic process
Y	0006072	biological_process	glycerol-3-phosphate metabolic process
Y	0016301	molecular_function	kinase activity
Y	0016740	molecular_function	transferase activity
Y	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
Y	0019563	biological_process	glycerol catabolic process

Functional Information from PROSITE/UniProt

site_id	PS00445
Number of Residues	21
Details	FGGY_KINASES_2 FGGY family of carbohydrate kinases signature 2. GiIIGItrgtgre.HLARATLE

Chain	Residue	Details
O	GLY355-GLU375

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site_id	PS00933
Number of Residues	13
Details	FGGY_KINASES_1 FGGY family of carbohydrate kinases signature 1. YfSasKLKWLLDN

Chain	Residue	Details
O	TYR132-ASN144

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00186","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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