7E9V

The Crystal Structure of human UMP-CMP kinase from Biortus.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004550	molecular_function	nucleoside diphosphate kinase activity
A	0004849	molecular_function	uridine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
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	0006222	biological_process	UMP biosynthetic process
A	0006225	biological_process	UDP biosynthetic process
A	0009220	biological_process	pyrimidine ribonucleotide biosynthetic process
A	0015949	biological_process	nucleobase-containing small molecule interconversion
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	0046705	biological_process	CDP biosynthetic process
A	0046940	biological_process	nucleoside monophosphate phosphorylation
A	0050145	molecular_function	nucleoside monophosphate kinase activity
A	0070062	cellular_component	extracellular exosome
A	0072528	biological_process	pyrimidine-containing compound biosynthetic process

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE89-ASN100

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03172

Chain	Residue	Details
A	GLY13
A	ARG39
A	LYS61
A	GLY93
A	ASN100
A	ARG134
A	ARG140
A	ARG151
A	LYS179

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER33

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBP5

Chain	Residue	Details
A	LYS43

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS55

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9DBP5

Chain	Residue	Details
A	LYS106

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q4KM73

Chain	Residue	Details
A	SER180

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site_id	SWS_FT_FI7
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS73

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