| Accession |
MF_00235 |
| Dates |
1-JUN-2001 (Created) 26-SEP-2008 (Last updated, Version 30) |
| Protein name |
| RecName: |
Full=Adenylate kinase; Short=AK; EC=2.7.4.3; |
| AltName: |
Full=ATP-AMP transphosphorylase; |
|
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.
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>
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_BACST); P84139 (KAD_BACGO): [Recover all] |
| Scope: |
Bacteria
Archaea |
| Fusion: |
Nter: None; Cter: None |
| Duplicate: |
in ANASP, SYNY3 |
| Plasmid encoded: |
None |
| Comments: |
FT condition for ATP binding is not fulfilled in the second copy of adk in ANASP; not shown in alignment |
View rule in raw text format (no links)