1UKE

UMP/CMP KINASE FROM SLIME MOLD

Replaces:  1UKD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
A	0006221	biological_process	pyrimidine nucleotide biosynthetic process
A	0006225	biological_process	UDP biosynthetic process
A	0009123	biological_process	nucleoside monophosphate metabolic process
A	0009165	biological_process	nucleotide biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0016776	molecular_function	phosphotransferase activity, phosphate group as acceptor
A	0019205	molecular_function	nucleobase-containing compound kinase activity
A	0033862	molecular_function	UMP kinase activity
A	0036430	molecular_function	CMP kinase activity
A	0036431	molecular_function	dCMP kinase activity
A	0043100	biological_process	pyrimidine nucleobase salvage
A	0043173	biological_process	nucleotide salvage
A	0046705	biological_process	CDP biosynthetic process
A	0046940	biological_process	nucleoside monophosphate phosphorylation
A	0072528	biological_process	pyrimidine-containing compound biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 196

Chain	Residue
A	UP5195
A	HOH198
A	HOH215
A	HOH220
A	HOH227

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site_id	AC2
Number of Residues	37
Details	BINDING SITE FOR RESIDUE UP5 A 195

Chain	Residue
A	GLY18
A	LYS19
A	GLY20
A	THR21
A	ALA37
A	GLY38
A	LEU41
A	ARG42
A	ILE59
A	GLU63
A	ILE64
A	VAL65
A	THR70
A	GLY90
A	PHE91
A	ARG93
A	ARG127
A	ARG131
A	ARG137
A	ARG148
A	ARG176
A	VAL178
A	MG196
A	HOH198
A	HOH199
A	HOH200
A	HOH208
A	HOH212
A	HOH213
A	HOH215
A	HOH216
A	HOH220
A	HOH232
A	GLY14
A	PRO15
A	GLY16
A	SER17

---

Functional Information from PROSITE/UniProt

site_id	PS00113
Number of Residues	12
Details	ADENYLATE_KINASE Adenylate kinase signature. FLVDGFPRneeN

Chain	Residue	Details
A	PHE86-ASN97

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	29
Details	Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_03172","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10426946","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8703943","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9280438","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_03172","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10426946","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8703943","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9280438","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03172","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10426946","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8703943","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9280438","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03172","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10426946","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9280438","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1zio

Chain	Residue	Details
A	ARG148
A	LYS19
A	ARG131
A	ASP140
A	ASP139
A	ARG137

---