Annotations: 1ZIO

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1zioa1	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Nucleotide and nucleoside kinases	Adenylate kinase	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
A	d1zioa2	Small proteins	Rubredoxin-like	Microbial and mitochondrial ADK, insert 'zinc finger' domain	Microbial and mitochondrial ADK, insert 'zinc finger' domain	Microbial and mitochondrial ADK, insert 'zinc finger' domain	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	P-loop nucleotide/nucleoside kinase-like	8054341	3002021	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	SKI	e1zioA2	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: SKI	ECOD (1.6)
A	ADK_lid	e1zioA1	A: few secondary structure elements	X: Rubredoxin-like	H: Rubredoxin-related	T: Rubredoxin-related	F: ADK_lid	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00406	Adenylate kinase (ADK)	Adenylate kinase	-	Domain
A	PF05191	Adenylate kinase, active site lid (ADK_lid)	Adenylate kinase, active site lid	Comparisons of adenylate kinases have revealed a particular divergence in the active site lid. In some organisms, particularly the Gram-positive bacteria, residues in the lid domain have been mutated to cysteines and these cysteine residues are resp ...	Comparisons of adenylate kinases have revealed a particular divergence in the active site lid. In some organisms, particularly the Gram-positive bacteria, residues in the lid domain have been mutated to cysteines and these cysteine residues are responsible for the binding of a zinc ion. The bound zinc ion in the lid domain, is clearly structurally homologous to Zinc-finger domains. However, it is unclear whether the adenylate kinase lid is a novel zinc-finger DNA/RNA binding domain, or that the lid bound zinc serves a purely structural function [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ADENYLATE KINASE	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding nucleobase-containing compound kinase activity nucleoside monophosphate kinase activity kinase activity adenylate kinase activity transferase activity catalytic activity phosphotransferase activity, phosphate group as acceptor transferase activity, transferring phosphorus-containing groups cation binding transition metal ion binding zinc ion binding metal ion binding	phosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process purine ribonucleoside monophosphate biosynthetic process nucleotide biosynthetic process organonitrogen compound biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleoside monophosphate biosynthetic process phosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process purine ribonucleoside monophosphate biosynthetic process nucleotide biosynthetic process organonitrogen compound biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleoside monophosphate biosynthetic process purine nucleoside monophosphate metabolic process organic substance biosynthetic process small molecule metabolic process ribose phosphate biosynthetic process cellular metabolic compound salvage nucleoside phosphate metabolic process primary metabolic process nucleotide metabolic process organic cyclic compound metabolic process biosynthetic process purine ribonucleotide salvage organophosphate biosynthetic process AMP biosynthetic process organic cyclic compound biosynthetic process nucleoside phosphate biosynthetic process purine ribonucleotide metabolic process purine nucleotide biosynthetic process ribose phosphate metabolic process AMP metabolic process nucleotide salvage purine ribonucleoside monophosphate metabolic process purine nucleotide metabolic process organic substance metabolic process ribonucleotide metabolic process ribonucleoside monophosphate metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process purine nucleotide salvage AMP salvage nucleoside monophosphate metabolic process carbohydrate derivative biosynthetic process organonitrogen compound metabolic process purine-containing compound salvage nucleobase-containing compound biosynthetic process nucleoside monophosphate biosynthetic process purine-containing compound metabolic process organophosphate metabolic process ribonucleoside monophosphate biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR006259	Adenylate kinase subfamily	Family
A	IPR007862	Adenylate kinase, active site lid domain	Domain
A	IPR000850	Adenylate kinase/UMP-CMP kinase	Family
A	IPR033690	Adenylate kinase, conserved site	Conserved Site
A	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	adenylate kinase M-CSA #290	This family of small, monomeric enzymes is most well known for the ubiquitous Adenylate kinase (EC 2.7.4.3) which serves a crucial role in adenosine phosphate homeostasis; in times of energy need, it enables ADP to be broken down to produce some more ATP, and then when energy is once more abundant it enables the recovery of AMP produced in this and other reactions. At least two other closely related enzymes have been identified - yeast uridylate kinase (no EC no. yet) and slime mould UMP/CMP kinase (EC 2.7.4.14). In all cases Mg(2+) is required for activity.	Defined by 5 residues: LYS:A-13ARG:A-88ARG:A-127ARG:A-160ARG:A-171 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.7.4.3 (PDB Primary Data) Search M-CSA Motif + EC 2.7.4.3

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.