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Annotation rule MF_03168 |
General rule information
[?]
Accession |
MF_03168 |
Dates |
19-FEB-2009 (Created) 20-NOV-2019 (Last updated, Version 12) |
Name |
Adenylate_kinase_AK2 |
case <OC:Eukaryota>
end case
Propagated annotation
[?]
Identifier, protein and gene names
[?]
case <OC:Vertebrata>
Protein name |
RecName:
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Full=Adenylate kinase 2, mitochondrial;
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Short=AK 2;
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EC 2.7.4.3;
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AltName:
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Full=ATP-AMP transphosphorylase 2;
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AltName:
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Full=ATP:AMP phosphotransferase;
|
AltName:
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Full=Adenylate monophosphate kinase;
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|
else
Protein name |
RecName:
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Full=Adenylate kinase;
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EC 2.7.4.3;
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AltName:
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Full=ATP-AMP transphosphorylase;
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AltName:
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Full=ATP:AMP phosphotransferase;
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AltName:
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Full=Adenylate kinase cytosolic and mitochondrial;
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AltName:
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Full=Adenylate monophosphate kinase;
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|
end case
case <OC:Saccharomyces>
end case
case <OC:Vertebrata>
end case
case <OC:Caenorhabditis>
end case
case <OC:Insecta>
end case
case <OC:Fungi>
end case
case <OC:Vertebrata>
Function |
Catalyzes 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. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis. |
else
Function |
Catalyzes 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. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. |
end case
case <OC:Vertebrata>
Subcellular location |
Mitochondrion intermembrane space. |
else
Subcellular location |
Cytoplasm, cytosol. Mitochondrion intermembrane space. Note=Predominantly mitochondrial. |
end case
Domain |
Consists 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. |
Similarity |
Belongs to the adenylate kinase family. AK2 subfamily. |
case not <OC:Vertebrata>
end case
case <FTTag:acetyl>
end case
case <FTTag:disulfid>
end case
GO:0005758; Cellular component: mitochondrial intermembrane space.
case not <OC:Vertebrata>
end case
GO:0004017; Molecular function: adenylate kinase activity.
GO:0006172; Biological process: ADP biosynthetic process.
GO:0046033; Biological process: AMP metabolic process.
GO:0046034; Biological process: ATP metabolic process.
From: KAD2_YEAST (P07170) |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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NP_BIND
|
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16
|
|
21
|
|
ATP
|
|
|
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G-[AS]-G-K-G-T
|
|
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NP_BIND
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63
|
|
65
|
|
AMP
|
|
|
|
x-L-V
|
|
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NP_BIND
|
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92
|
|
95
|
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AMP
|
|
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G-F-P-R
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NP_BIND
|
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143
|
|
144
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ATP
|
|
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[ST]-Y
|
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REGION
|
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36
|
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65
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NMPbind
|
|
|
|
|
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REGION
|
|
133
|
|
170
|
|
LID
|
|
|
|
|
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BINDING
|
|
37
|
|
37
|
|
AMP
|
|
|
|
T
|
|
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BINDING
|
|
42
|
|
42
|
|
AMP
|
|
|
|
R
|
|
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BINDING
|
|
99
|
|
99
|
|
AMP
|
|
|
|
Q
|
|
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BINDING
|
|
134
|
|
134
|
|
ATP
|
|
|
|
R
|
|
|
BINDING
|
|
167
|
|
167
|
|
AMP
|
|
|
|
R
|
|
|
BINDING
|
|
178
|
|
178
|
|
AMP
|
|
|
|
R
|
|
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BINDING
|
|
206
|
|
206
|
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ATP; via carbonyl oxygen
|
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|
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|
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case <OC:Saccharomyces>
PROPEP
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1
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2
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|
Removed in mature form
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|
|
|
|
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CHAIN
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3
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Cter
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Adenylate kinase
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|
|
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MOD_RES
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3
|
|
3
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N-acetylserine
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acetyl
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S
|
|
|
end case
case <OC:Mammalia>
From: KAD2_HUMAN (P54819) |
INIT_MET
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1
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1
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Removed
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M
|
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end case
case <OC:Vertebrata>
DISULFID
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42
|
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92
|
|
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disulfid
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C-x*-C
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|
end case
Additional information
[?]