HAMAP annotation rule: MF_00235
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Accession MF_00235
Dates 1-JUN-2001 (Created)
9-DEC-2011 (Last updated, Version 35)
Data class Protein
Names Adenylate_kinase_Adk



Identifier KAD
Protein name
RecName: Full=Adenylate kinase;
Short=AK;
EC=2.7.4.3;
AltName: Full=ATP-AMP transphosphorylase;
Gene name adk
FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth (By similarity).
CATALYTIC ACTIVITY: ATP + AMP = 2 ADP.
PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).

case not <OC:Mycobacterium>
DOMAIN: Consists of three domains, a large central CORE domain and two small peripheral domains, AMP binding and LID. The LID domain closes over the site of phosphoryl transfer upon ATP binding (By similarity).
end case


case <OC:Mycobacterium>
DOMAIN: Consists of three domains, a large central CORE domain and two small peripheral domains, AMP binding and LID. The LID domain is a solvent-exposed domain that is much shorter in Mycobacterium than in many other bacteria like E.coli, in which it closes over the site of phosphoryl transfer upon ATP binding. The AMP binding domain seems to play an important role in the catalysis and structural stability of the protein (By similarity).
end case


case <FTGroup:1>
MISCELLANEOUS: The zinc ion does not participate in catalysis. It has a structural role in stabilizing the LID domain, which does not seem to be involved in directly binding DNA/RNA (By similarity).
end case

SIMILARITY: Belongs to the adenylate kinase family.
Pfam PF00406; ADK; 1;
PF05191; ADK_lid; 0-1;
PRINTS PR00094; ADENYLTKNASE; 1;
TIGRFAMs TIGR01351; Adk; 1;
PROSITE PS00113; ADENYLATE_KINASE; 1;

case (<OC:Escherichia> or <OC:Shigella>) and <FT:4>
end case


case <FTGroup:1>
end case

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.
From: KAD_ECOLI (P69441)
Key     From     To       Description   Condition   FTGroup
NP_BIND     7     15       ATP (By similarity)   G-x-[NP]-[GA]-x-G-K-[GST]-[ST]  
NP_BIND     31     59       AMP (By similarity)      
case <OC:Enterobacteriaceae>
Key     From     To       Description   Condition   FTGroup
REGION     122     159       LID      
end case

case <OC:Escherichia> or <OC:Shigella>
Key     From     To       Description   Condition   FTGroup
MOD_RES     192     192       N6-acetyllysine (By similarity)   K  
end case

case <OC:Mycobacterium>
From: KAD_MYCTU (P69440)
Key     From     To       Description   Condition   FTGroup
REGION     125     134       LID      
end case

From: KAD_BACSU (P16304)
Key     From     To       Description   Condition   FTGroup
METAL (Optional)     130     130       Zinc (By similarity)   C   1
METAL (Optional)     133     133       Zinc (By similarity)   C   1
METAL (Optional)     150     150       Zinc (By similarity)   C   1
METAL (Optional)     153     153       Zinc (By similarity)   [CD]   1
case <OC:Bacillales>
Key     From     To       Description   Condition   FTGroup
 
REGION     128     159       LID      
end case




Size range: 181-253 amino acids
Related UniRules: None
Template: P69441 (KAD_ECOLI); P69440 (KAD_MYCTU); P16304 (KAD_BACSU); P27142 (KAD_GEOSE); P84139 (KAD_BACGO): [Recover all]
Scope: Bacteria
Archaea
Fusion: Nter: None; Cter: None
Duplicate: in NOSS1, SYNY3
Plasmid encoded: None
Comments: FT condition for ATP binding is not fulfilled in the second copy of adk in NOSS1; not shown in alignment

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