1XDO

Crystal Structure of Escherichia coli Polyphosphate Kinase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006793	biological_process	phosphorus metabolic process
A	0006799	biological_process	polyphosphate biosynthetic process
A	0008976	molecular_function	polyphosphate kinase activity
A	0009358	cellular_component	polyphosphate kinase complex
A	0016020	cellular_component	membrane
A	0016301	molecular_function	kinase activity
A	0016776	molecular_function	phosphotransferase activity, phosphate group as acceptor
A	0016778	molecular_function	diphosphotransferase activity
A	0031241	cellular_component	periplasmic side of cell outer membrane
A	0042803	molecular_function	protein homodimerization activity
A	0043751	molecular_function	polyphosphate:AMP phosphotransferase activity
A	0046872	molecular_function	metal ion binding
B	0003824	molecular_function	catalytic activity
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006793	biological_process	phosphorus metabolic process
B	0006799	biological_process	polyphosphate biosynthetic process
B	0008976	molecular_function	polyphosphate kinase activity
B	0009358	cellular_component	polyphosphate kinase complex
B	0016020	cellular_component	membrane
B	0016301	molecular_function	kinase activity
B	0016776	molecular_function	phosphotransferase activity, phosphate group as acceptor
B	0016778	molecular_function	diphosphotransferase activity
B	0031241	cellular_component	periplasmic side of cell outer membrane
B	0042803	molecular_function	protein homodimerization activity
B	0043751	molecular_function	polyphosphate:AMP phosphotransferase activity
B	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_00347, ECO:0000269|PubMed:8962061, ECO:0000305|PubMed:15947782

Chain	Residue	Details
A	ALA436
B	ALA436

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site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00347, ECO:0007744|PDB:1XDP

Chain	Residue	Details
A	LEU46
B	THR469
B	GLY565
B	ASP593
A	VAL376
A	PHE406
A	THR469
A	GLY565
A	ASP593
B	LEU46
B	VAL376
B	PHE406

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