HAMAP logo

HAMAP rule MF_00235

Send feedback

General rule information [?]

Accession MF_00235
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 47)
Name Adenylate_kinase_Adk
Scope(s) Bacteria
Archaea
Template(s) P69441 (KAD_ECOLI); P9WKF5 (KAD_MYCTU); P16304 (KAD_BACSU); P27142 (KAD_GEOSE); P84139 (KAD_SPOGL); [ Recover all ]
Triggered by
case c? <OC:Bacteria> or <OC:Archaea>
HAMAP; MF_00235 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier KAD
Protein name RecName: Full=Adenylate kinase;
                 Short=AK;
                 EC=2.7.4.3;
AltName: Full=ATP-AMP transphosphorylase;
AltName: Full=ATP:AMP phosphotransferase;
AltName: Full=Adenylate monophosphate kinase;
Gene name Name=adk;

Comments [?]

FUNCTIONCatalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
CATALYTIC ACTIVITY Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
PATHWAYPurine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
SUBUNITMonomer.
SUBCELLULAR LOCATIONCytoplasm.
case <FTGroup:1>
DOMAINConsists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
else
DOMAINConsists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
end case
SIMILARITYBelongs to the adenylate kinase family.

Keywords [?]


Gene Ontology [?]

GO:0004017; Molecular function:adenylate kinase activity
GO:0005524; Molecular function:ATP binding
case <FTGroup:1>
GO:0008270; Molecular function:zinc ion binding
end case
GO:0009165; Biological process:nucleotide biosynthetic process
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

Pfam PF00406; ADK; 1;
Pfam PF05191; ADK_lid; 0-1;
PRINTS PR00094; ADENYLTKNASE; 1;
NCBIfam TIGR01351; Adk; 1;
PROSITE PS00113; ADENYLATE_KINASE; 1;

Features [?]

From: KAD_ECOLI (P69441)
Key From To Description Tag Condition FTGroup
BINDING 10 15 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
[GA]-x-G-K-[GST]-[ST]
BINDING 57 59 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
x-[LYF]-[VILM]
BINDING 85 88 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
G-[FY]-P-R
BINDING 132 133 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
[STVI]-[YFH]
REGION 30 59 /note="NMP"
REGION 122 159 /note="LID"
BINDING 31 31 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
[TS]
BINDING 36 36 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
R
BINDING 92 92 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
Q
BINDING 123 123 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
R
BINDING 156 156 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
R
BINDING 167 167 /ligand="AMP"
/ligand_id="ChEBI:CHEBI:456215"
R
BINDING 200 200 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
From: KAD_BACSU (P16304)
Key From To Description Tag Condition FTGroup
BINDING 130 130 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_note="structural"
C 1
BINDING 133 133 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_note="structural"
C 1
BINDING 150 150 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_note="structural"
C 1
BINDING 153 153 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_note="structural"
[CD] 1

Additional information [?]

Size range 181-253 amino acids
Related rules MF_03168
MF_03169
MF_03170
MF_03171
MF_03172
Fusion Nter: None Cter: None



View rule in raw text format (no links)